SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS20010 FitnessBrowser__Pedo557:CA265_RS20010 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 20 (the maximum) hits to proteins with known functional sites (download)

I3VE74 2-hydroxyisobutanoyl-CoA mutase small subunit; 2-hydroxyisobutyryl-CoA mutase small subunit; HCM small subunit; EC 5.4.99.64 from Aquincola tertiaricarbonis (see paper)
53% identity, 91% coverage: 8:134/139 of query aligns to 5:131/136 of I3VE74

query
sites
I3VE74

P

P

I

I

R

R

V

V

L

L

V

L

A

A

K

K

V

V

G

G

L

L

D

D

G

G

H
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H

D

D

R

R

G

G

A

V

K

K

V

V

I

V

A

A

T

R

S

A

L

L

R

R

D

D

A

A

G

G

M

M

E

D

V

V

I

I

Y

Y

T

S

G

G

L

L

R

H

Q

R

T

T

P

P

E

E

M

E

V

V

N

N

T

T

A

A

L

I

Q

Q

E

E

D

D

V

V

D

D

A

V

I

L

G

G

I

V

S

S

I

L

L

L

S

S

G

G

A

V

H

Q

M

L

T

T

V

V

F

F

P

P

K

K

I

I

I

F

H

K

F

L

M

L

K

D

E

E

K

R

Q

G

L

A

D

G

D

D

V

L

L

I

L

V

T

I

G

A

G

G

I

V

I

M

P

P

E

D

A

E

D

D

R

A

L

A

K

A

L

I

A

R

G

K

M

L

G

G

V

V

G

R

E

E

L

V

F

L

P

L

P

Q

G

D

T

T

T

P

M

P

A

Q

S

A

I

I

V

I

E

D

Y

S

I

I

Q

R

N

S

W

L

V

V

T

A

H18 (= H21) binding axial binding residue

4r3uC Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
53% identity, 91% coverage: 8:134/139 of query aligns to 3:129/131 of 4r3uC

query
sites
4r3uC

P

P

I

I

R

R

V

V

L

L

V

L

A

A

K
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K

V

V

G

G

L

L

D
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D

G
|
G

H
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H

D
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D

R
|
R

G
|
G

A

V

K

K

V

V

I
x
V

A

A

T

R

S

A

L

L

R

R

D

D

A

A

G

G

M

M

E

D

V

V

I

I

Y

Y

T

S

G

G

L

L

R

H

Q

R

T

T

P

P

E

E

M

E

V

V

N

N

T

T

A

A

L

I

Q

Q

E

E

D

D

V

V

D

D

A

V

I

L

G
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G

I

V

S
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S

I

L

L
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L

S

S

G

G

A

V

H

Q

M

L

T

T

V

V

F

F

P

P

K

K

I

I

I

F

H

K

F

L

M

L

K

D

E

E

K

R

Q

G

L

A

D

G

D

D

V

L

L

I

L

V

T
x
I

G
x
A

G
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G

I

V

I

M

P

P

E

D

A

E

D

D

R

A

L

A

K

A

L

I

A

R

G

K

M

L

G

G

V

V

G

R

E

E

L

V

F
x
L

P
x
L

P
x
Q

G

D

T
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T

T

P

M

P

A

Q

S

A

I

I

V

I

E

D

Y

S

I

I

Q

R

N

S

W

L

V

V

T

A

active site: K10 (= K15), D14 (= D19), H16 (= H21)
binding cobalamin: G15 (= G20), H16 (= H21), D17 (= D22), R18 (= R23), G19 (= G24), V23 (≠ I28), G59 (= G64), S61 (= S66), L63 (= L68), I89 (≠ T94), A90 (≠ G95), G91 (= G96), G92 (= G97), L111 (≠ F116), L112 (≠ P117), Q113 (≠ P118), T115 (= T120)

P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
46% identity, 86% coverage: 1:120/139 of query aligns to 608:726/750 of P22033

query
sites
P22033

M
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M

S
x
E

K
x
R

V
x
E

L
x
G

N
x
R

R
|
R

P
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P

I

-

R
|
R

V
x
L

L
|
L

V
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V

A
|
A

K
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K

V
x
M

G
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G

L
x
Q

D
|
D

G
|
G

H
|
H

D
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D

R
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R

G
|
G

A
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A

K
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K

V
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V

I
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I

A
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A

T
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T

S
x
G

L
x
F

R
x
A

D
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D

A
x
L

G
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G

M
x
F

E
x
D

V
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V

I
x
D

Y
x
I

T
x
G

G
x
P

L
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L

R
x
F

Q
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Q

T
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T

P
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P

E
x
R

M
x
E

V
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V

V
x
A

N
x
Q

T
x
Q

A
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A

L
x
V

Q
x
D

E
x
A

D
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D

V
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V

D
x
H

A
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A

I
x
V

G
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G

I
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I

S
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S

I
x
T

L
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L

S
x
A

G
x
A

A
x
G

H
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H

M
x
K

T
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T

V
x
L

F
x
V

P
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P

K
x
E

I
x
L

I
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I

H
x
K

F
x
E

M
x
L

K
x
N

E
x
S

K
x
L

Q
x
G

L
x
R

D
x
P

D
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D

V
x
I

L
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L

L
x
V

T
x
M

G
x
C

G
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G

I
x
V

I
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I

P
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P

E
x
P

A
x
Q

D
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D

R
x
Y

L
x
E

K
x
F

L
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L

A
x
F

G
x
E

M
x
V

G
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G

V
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V

G
x
S

E
x
N

L
x
V

F
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F

P
x
G

P
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P

G
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G

T
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T

P615 (= P8) to L: in MMAM; mut0; affects proper folding; reduced strongly protein level; to R: in MMAM; mut0; dbSNP:rs1554158777; to T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
R616 (= R10) to C: in MMAM; mut0; dbSNP:rs765284825
L617 (≠ V11) to R: in MMAM; mut0; dbSNP:rs1554158775
K621 (= K15) to N: in MMAM; mut0
G623 (= G17) to R: in MMAM; mut0; dbSNP:rs121918254
Q624 (≠ L18) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
D625 (= D19) to G: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253847; to V: in MMAM; mut0; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity
G626 (= G20) to C: in MMAM; mut-; dbSNP:rs982110849
H627 (= H21) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
G630 (= G24) to E: in MMAM; mut0; dbSNP:rs143023066
V633 (= V27) to G: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability; dbSNP:rs200055428
G637 (≠ S31) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
F638 (≠ L32) to I: in MMAM; mut0
D640 (= D34) to Y: in MMAM; mut0; dbSNP:rs865815395
G642 (= G36) to R: in MMAM; mut-; dbSNP:rs747897332
G648 (≠ T42) to D: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs766721811
V669 (≠ I63) to E: in MMAM; mut0; dbSNP:rs1360470463
I671 (= I65) to V: in dbSNP:rs8589
L674 (= L68) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
H678 (= H72) to R: in MMAM; mut-; dbSNP:rs147094927
E684 (≠ K78) natural variant: E -> EL (in MMAM; mut-)
L685 (≠ I79) to R: in MMAM; mut-; dbSNP:rs864309739
R694 (≠ L88) to L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; to W: in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs777758903
M700 (≠ T94) to K: in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs140600746
G703 (= G97) to R: in MMAM; mut0; dbSNP:rs121918255
G717 (= G111) to V: in MMAM; mut-; no effect on protein abundance; interferes with the binding of the cofactor to the apoenzyme; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; decreased thermodynamic stability; dbSNP:rs121918252
G723 (≠ P117) to D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681

Sites not aligning to the query:

1:32 modified: transit peptide, Mitochondrion
7:750 natural variant: Missing (in MMAM; mut-)
50 binding
69 I → V: in MMAM; likely benign; dbSNP:rs115923556
86 P → L: in MMAM; mut0 and mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769348060
87 G → E: in MMAM; mut0; dbSNP:rs1554160986
93 R → H: in MMAM; mut0; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918251
94 G → R: in MMAM; mut0; dbSNP:rs727504022; G → V: in MMAM; mut- and mut0; dbSNP:rs535411418
95 P → R: in MMAM; mut0; dbSNP:rs190834116
96:99 binding
100 Y → C: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309735
105 W → R: in MMAM; mut0; dbSNP:rs121918249
106:110 binding
108 R → C: in MMAM; mut0; dbSNP:rs121918257; R → G: in MMAM; mut-; R → H: in MMAM; mut0; dbSNP:rs483352778
109 Q → R: in MMAM; mut0; dbSNP:rs1461110052
133 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253828
137 A → V: in MMAM; mut0; dbSNP:rs941483851
139 D → N: in MMAM; uncertain significance; dbSNP:rs879253829
140 L → P: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
141 A → T: in MMAM; decreased protein expression; dbSNP:rs1554160730
143 H → Y: in MMAM; mut0
145 G → S: in MMAM; mut0
148 S → L: in MMAM; mut0; dbSNP:rs1300547552
152:750 natural variant: Missing (in MMAM; mut0)
156 D → N: in MMAM; mut-
158 G → V: in MMAM; mut0
161 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; G → V: in MMAM; decreased protein expression
174 F → S: in MMAM; mut0; dbSNP:rs864309733
186 M → V: in MMAM; mut-; dbSNP:rs148331800
187 T → S: in MMAM; mut0; dbSNP:rs879253830
189 N → I: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs200908035; N → K: in MMAM; mut-; dbSNP:rs1561959114
191 A → E: in MMAM; mut- and mut0; affects proper folding; reduced protein level; decreased methylmalonyl-CoA mutase activity; dbSNP:rs760782399
197 A → E: in MMAM; mut0
203 G → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs778702777
205 natural variant: Missing (in MMAM; mut0; dbSNP:rs879253831)
215 G → C: in MMAM; mut- and mut0; dbSNP:rs121918258; G → S: in MMAM; mut0; dbSNP:rs121918258
216:218 binding
218 Q → H: in MMAM; mut0 and mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs1446389693
219 N → Y: in MMAM; mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs121918256
228 binding ; R → Q: in MMAM; mut0; dbSNP:rs770810987
228:750 natural variant: Missing (in MMAM; mut0)
230 T → I: in MMAM; mut-; T → R: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253833
231 Y → N: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309736
255 binding
262 S → N: in MMAM; mut0
265 binding ; H → Y: in MMAM; mut-
276 E → D: in MMAM; uncertain significance; mut-; dbSNP:rs12175488
281 L → S: in MMAM; mut0; dbSNP:rs796052007
284 G → E: in MMAM; mut0; dbSNP:rs879253835; G → R: in MMAM; mut0; dbSNP:rs761477436
288 S → P: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1179778233
291 G → E: in MMAM; mut0
293 Q → P: in MMAM; mut0
304:306 binding
305 L → S: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554160246
306 S → F: in MMAM; mut0; dbSNP:rs1085307929
309 W → G: in MMAM; decreased protein expression
312 G → V: in MMAM; mut0; dbSNP:rs864309734
316 Y → C: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; no decreased affinity for adenosylcob(III)alamin; dbSNP:rs781474200
324 A → T: in MMAM; mut-; dbSNP:rs780387525
326 R → K: in MMAM; uncertain significance; dbSNP:rs758577372
328 L → F: in MMAM; mut0; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; dbSNP:rs796052002; L → P: in MMAM; mut0; dbSNP:rs965316043
344 S → F: in MMAM; mut-; affects proper folding; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin
346 natural variant: Missing (in MMAM; mut0)
347 L → R: in MMAM; mut0; dbSNP:rs1026703654
350 H → Y: in MMAM; mut0; dbSNP:rs1407914109
358 L → P: in MMAM; mut0
366 N → S: in MMAM; mut-; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs864309737
369 R → C: in MMAM; mut0; dbSNP:rs772552898; R → H: in MMAM; mut- and mut0; no effect on protein abundance; loss of methylmalonyl-CoA mutase activity; alters thermodynamic stability; dbSNP:rs564069299
370 T → P: in MMAM; mut0; dbSNP:rs368790885
377 A → E: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs121918250
383 Q → H: in MMAM; mut0; Q → P: in MMAM; mut0
386 H → N: in MMAM; mut0; dbSNP:rs1554159937; H → R: in MMAM; mut0; dbSNP:rs866933356
387 T → I: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability
388 N → H: in MMAM; mut0; dbSNP:rs766010704; N → K: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253840
389 natural variant: Missing (in MMAM; mut0)
412 natural variant: Missing (in MMAM; mut0)
424 P → L: in MMAM; mut0; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs879253842
426 G → E: in MMAM; mut-; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs533755473; G → R: in MMAM; mut-; no effect on protein abundance; decreased methylmalonyl-CoA mutase activity; strong decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs769922244
427 G → D: in MMAM; mut0; dbSNP:rs753288303
454 G → E: in MMAM; mut0
499 A → T: in dbSNP:rs2229385
505 I → T: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity
514 Q → E: in MMAM; uncertain significance; Q → K: in MMAM; decreased protein expression
518 L → P: in MMAM; mut0; dbSNP:rs864309738
532 R → H: in dbSNP:rs1141321
535 A → P: in MMAM; mut0; dbSNP:rs760183775
552 A → V: in MMAM; uncertain significance; dbSNP:rs879253845
560 C → Y: in MMAM; mut0; dbSNP:rs1238333040
566 T → R: in MMAM; mut0
573 F → S: in MMAM; mut-; affects proper folding; no effect on protein abundance; no effect on methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; does not alter thermodynamic stability; dbSNP:rs775593146
587 Y → C: in MMAM; mut-
597 I → R: in MMAM; no changed in protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1554158951

2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
45% identity, 86% coverage: 1:120/139 of query aligns to 573:691/714 of 2xiqA

query
sites
2xiqA

M

M

S

E

K

R

V

E

L

G

N

R

R

R

P

P

I

-

R

R

V

L

L

L

V

V

A

A

K
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K

V

M

G

G

L

Q

D
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D

G
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G

H
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H

D
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D

R
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R

G
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G

A

A

K

K

V

V

I
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I

A

A

T

T

S

G

L

F

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

I

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

R

M

E

V

V

V

A

N

Q

T

Q

A

A

L

V

Q

D

E

A

D

D

V

V

D

H

A

A

I

V

G
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G

I

V

S
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S

I

T

L
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L

S

A

G
x
A

A

G

H

H

M

K

T

T

V

L

F

V

P

P

K

E

I

L

I

I

H

K

F

E

M

L

K

N

E

S

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

V

T

M

G

C

G
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G

I

V

I

I

P

P

E

P

A

Q

D

D

R

Y

L

E

K

F

L

L

A

F

G

E

M

V

G

G

V

V

G

S

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N

L

V

F
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F

P
x
G

P

P

G

G

T
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T

active site: K586 (= K15), D590 (= D19), H592 (= H21)
binding cobalamin: G591 (= G20), H592 (= H21), D593 (= D22), R594 (= R23), G595 (= G24), I599 (= I28), G635 (= G64), S637 (= S66), L639 (= L68), A641 (≠ G70), G667 (= G96), G668 (= G97), F687 (= F116), G688 (≠ P117), T691 (= T120)

Sites not aligning to the query:

active site: 75, 229, 230
binding cobalamin: 75, 105, 108, 125, 193, 233, 320, 321, 357, 360, 361
binding malonyl-coenzyme a: 61, 63, 64, 68, 71, 73, 75, 150, 152, 181, 193, 220, 230, 269, 271, 273, 313, 314, 315, 317, 348

8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
45% identity, 86% coverage: 1:120/139 of query aligns to 572:690/708 of 8dyjB

query
sites
8dyjB

M

M

S

E

K

R

V

E

L

G

N

R

R

R

P

P

I

-

R

R

V

L

L

L

V

V

A

A

K

K

V

M

G

G

L

Q

D

D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

A

K

K

V

V

I
|
I

A

A

T

T

S

G

L

F

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

I

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

R

M

E

V

V

V

A

N

Q

T

Q

A

A

L

V

Q

D

E

A

D

D

V

V

D

H

A

A

I

V

G

G

I

V

S
|
S

I

T

L
|
L

S

A

G
x
A

A

G

H

H

M

K

T

T

V

L

F

V

P

P

K

E

I

L

I

I

H

K

F

E

M

L

K

N

E

S

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

V

T

M

G

C

G
|
G

I
x
V

I

I

P

P

E

P

A

Q

D

D

R

Y

L

E

K

F

L

L

A

F

G

E

M

V

G

G

V

V

G

S

E

N

L

V

F
|
F

P
x
G

P

P

G

G

T
|
T

binding cobalamin: G590 (= G20), H591 (= H21), D592 (= D22), R593 (= R23), G594 (= G24), I598 (= I28), S636 (= S66), L638 (= L68), A640 (≠ G70), G666 (= G96), G667 (= G97), V668 (≠ I98), F686 (= F116), G687 (≠ P117), T690 (= T120)

Sites not aligning to the query:

binding adenosine-5'-diphosphate: 74, 151, 192, 228, 229, 272, 316, 352, 356, 360, 361
binding cobalamin: 102, 104, 107, 124, 191, 192, 229, 232, 319, 320, 356, 359, 360

6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 596:710/727 of 6reqA

query
sites
6reqA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L
x
Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G

G

I

V

S
|
S

I

S

L
|
L

S

A

G
|
G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I

V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P

P

G

G

T
|
T

T

V

M

I

active site: K603 (= K15), D607 (= D19), H609 (= H21)
binding cobalamin: G608 (= G20), H609 (= H21), D610 (= D22), R611 (= R23), G612 (= G24), I616 (= I28), Y620 (≠ L32), S654 (= S66), L656 (= L68), G658 (= G70), G684 (= G96), G685 (= G97), Y704 (≠ F116), T705 (≠ P117), T708 (= T120)

Sites not aligning to the query:

active site: 88, 242, 243
binding 3-carboxypropyl-coenzyme a: 74, 76, 77, 80, 81, 84, 86, 88, 113, 163, 165, 194, 206, 243, 282, 284, 286, 327, 329, 360
binding cobalamin: 88, 116, 118, 121, 138, 206, 246, 332, 333, 369, 370, 372

1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 596:710/727 of 1e1cA

query
sites
1e1cA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L
x
Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G

G

I

V

S
|
S

I

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I
x
V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P

P

G

G

T
|
T

T

V

M

I

active site: K603 (= K15), D607 (= D19), H609 (= H21)
binding cobalamin: G608 (= G20), H609 (= H21), D610 (= D22), R611 (= R23), G612 (= G24), I616 (= I28), Y620 (≠ L32), S654 (= S66), L656 (= L68), G684 (= G96), G685 (= G97), V686 (≠ I98), Y704 (≠ F116), T705 (≠ P117), T708 (= T120)

Sites not aligning to the query:

active site: 88, 242, 243
binding cobalamin: 88, 118, 121, 138, 205, 206, 246, 332, 333, 369, 370, 372, 373, 713
binding desulfo-coenzyme a: 74, 77, 80, 81, 84, 86, 113, 163, 165, 194, 282, 284, 327, 360

7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 594:708/725 of 7reqA

query
sites
7reqA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G

G

I

V

S
|
S

I

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I

V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P

P

G

G

T
|
T

T

V

M

I

active site: K601 (= K15), D605 (= D19), H607 (= H21)
binding cobalamin: G606 (= G20), H607 (= H21), D608 (= D22), R609 (= R23), G610 (= G24), I614 (= I28), S652 (= S66), L654 (= L68), G682 (= G96), G683 (= G97), Y702 (≠ F116), T703 (≠ P117), T706 (= T120)

Sites not aligning to the query:

active site: 86, 240, 241
binding 2-carboxypropyl-coenzyme a: 72, 74, 75, 78, 79, 82, 84, 86, 161, 163, 192, 204, 241, 280, 282, 284, 325, 358
binding cobalamin: 86, 116, 136, 204, 244, 330, 331, 367, 368, 370

3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 594:708/725 of 3reqA

query
sites
3reqA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G
|
G

I

V

S
|
S

I

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I

V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P
|
P

G

G

T
|
T

T

V

M

I

active site: K601 (= K15), D605 (= D19), H607 (= H21)
binding cobalamin: G606 (= G20), H607 (= H21), D608 (= D22), R609 (= R23), G610 (= G24), I614 (= I28), G650 (= G64), S652 (= S66), L654 (= L68), G682 (= G96), G683 (= G97), Y702 (≠ F116), T703 (≠ P117), P704 (= P118), T706 (= T120)

Sites not aligning to the query:

active site: 86, 240, 241
binding adenosine: 86, 240, 244, 330
binding cobalamin: 116, 203, 204, 244, 330, 331, 368

2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 594:708/725 of 2reqA

query
sites
2reqA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G
|
G

I

V

S
|
S

I

S

L
|
L

S
x
A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I

V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P

P

G

G

T
|
T

T

V

M

I

active site: K601 (= K15), D605 (= D19), H607 (= H21)
binding cobalamin: G606 (= G20), H607 (= H21), D608 (= D22), R609 (= R23), G610 (= G24), I614 (= I28), G650 (= G64), S652 (= S66), L654 (= L68), A655 (≠ S69), G682 (= G96), G683 (= G97), Y702 (≠ F116), T703 (≠ P117), T706 (= T120)

Sites not aligning to the query:

active site: 86, 240, 241
binding cobalamin: 203, 204, 244, 245, 331, 368
binding coenzyme a: 72, 79, 318

P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
44% identity, 83% coverage: 7:122/139 of query aligns to 597:711/728 of P11653

query
sites
P11653

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K

K

V

M

G

G

L

Q

D

D

G
|
G

H
|
H

D
|
D

R
|
R

G

G

A

Q

K

K

V

V

I

I

A

A

T

T

S

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G

G

I

V

S
|
S

I

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G

G

G
|
G

I

V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F

Y

P

T

P

P

G

G

T
|
T

T

V

M

I

G609 (= G20) binding
H610 (= H21) binding axial binding residue
D611 (= D22) binding
R612 (= R23) binding
S655 (= S66) binding
L657 (= L68) binding
G686 (= G97) binding
T709 (= T120) binding

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
75 binding
78 binding
82 binding
85 binding
87 binding
89 binding ; Y→F: Does not significantly affect affinity for succiny-CoA, but kcat is lowered about 580-fold.
114 binding
117 binding
139 binding
195 binding
197 binding
206 binding
207 binding ; binding
244 binding
283 binding
285 binding
333 binding
370 binding
373 binding

5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 594:708/725 of 5reqA

query
sites
5reqA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G

G

I

V

S
|
S

I

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I
x
V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P

P

G

G

T
|
T

T

V

M

I

active site: K601 (= K15), D605 (= D19), H607 (= H21)
binding cobalamin: G606 (= G20), H607 (= H21), D608 (= D22), R609 (= R23), G610 (= G24), I614 (= I28), S652 (= S66), L654 (= L68), G682 (= G96), G683 (= G97), V684 (≠ I98), Y702 (≠ F116), T703 (≠ P117), T706 (= T120)

Sites not aligning to the query:

active site: 86, 240, 241
binding cobalamin: 116, 136, 204, 241, 244, 330, 331, 367, 368, 370
binding methylmalonyl(carbadethia)-coenzyme a: 72, 74, 75, 79, 82, 84, 86, 111, 161, 163, 192, 194, 204, 233, 241, 280, 282, 284, 324, 325, 358, 359
binding succinyl(carbadethia)-coenzyme a: 72, 74, 75, 79, 82, 84, 86, 161, 163, 192, 204, 233, 241, 280, 282, 284, 325, 358

4reqA Methylmalonyl-coa mutase substrate complex (see paper)
44% identity, 83% coverage: 7:122/139 of query aligns to 595:709/726 of 4reqA

query
sites
4reqA

R

R

P

P

I

-

R

R

V

I

L

L

V

L

A

A

K
|
K

V

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

I
|
I

A

A

T

T

S

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

I

D

Y

V

T

G

G

P

L

L

R

F

Q

Q

T

T

P

P

E

E

M

E

V

T

V

A

N

R

T

Q

A

A

L

V

Q

E

E

A

D

D

V

V

D

H

A

V

I

V

G

G

I

V

S
|
S

I

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

V

L

F

V

P

P

K

A

I

L

I

R

H

K

F

E

M

L

K

D

E

K

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

I

T

T

G

V

G
|
G

I
x
V

I

I

P

P

E

E

A

Q

D

D

R

F

L

D

K

E

L

L

A

R

G

K

M

D

G

G

V

A

G

V

E

E

L

I

F
x
Y

P
x
T

P

P

G

G

T
|
T

T

V

M

I

active site: K602 (= K15), D606 (= D19), H608 (= H21)
binding cobalamin: G607 (= G20), H608 (= H21), D609 (= D22), R610 (= R23), G611 (= G24), I615 (= I28), S653 (= S66), L655 (= L68), G683 (= G96), G684 (= G97), V685 (≠ I98), Y703 (≠ F116), T704 (≠ P117), T707 (= T120)

Sites not aligning to the query:

active site: 87, 241, 242
binding cobalamin: 87, 117, 137, 204, 205, 242, 245, 331, 332, 368, 369, 371, 372
binding methylmalonyl-coenzyme a: 73, 76, 79, 80, 83, 85, 87, 112, 162, 164, 193, 205, 234, 241, 242, 281, 283, 285, 326, 328, 359, 360
binding succinyl-coenzyme a: 73, 76, 79, 80, 83, 85, 87, 162, 164, 193, 195, 205, 234, 241, 242, 281, 283, 285, 324, 326, 359

6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
43% identity, 84% coverage: 7:123/139 of query aligns to 603:718/736 of 6oxdA

query
sites
6oxdA

R

R

P

P

I

-

R

R

V

I

L

L

V

I

A

A

K
|
K

V

M

G

G

L

Q

D
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D

G
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G

H
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H

D
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D

R
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R

G

G

A

Q

K

K

V

V

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I

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A

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A

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F

R

A

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D

A

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Y

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G

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L

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S

T

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P

E

E

M

E

V

V

V

A

N

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T

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A

A

L

A

Q

D

E

N

D

D

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V

D

H

A

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S

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L

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A

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x
A

A

G

H

H

M

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T

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L

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V

P

P

K

A

I

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I

R

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F

A

M

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K

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Q

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G

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P

E

P

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D

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E

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A

Y

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A

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A

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T

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I

A

A

active site: K610 (= K15), D614 (= D19), H616 (= H21)
binding cobalamin: G615 (= G20), H616 (= H21), D617 (= D22), R618 (= R23), S661 (= S66), L663 (= L68), A665 (≠ G70), G691 (= G96), G692 (= G97), F711 (= F116), P712 (= P117), T715 (= T120)

Sites not aligning to the query:

active site: 100, 254, 255
binding cobalamin: 100, 130, 133, 150, 218, 258, 344, 345, 381, 382, 384, 385
binding Itaconyl coenzyme A: 86, 88, 89, 93, 96, 98, 100, 175, 177, 206, 218, 255, 294, 296, 298, 337, 338, 339, 341, 372

8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
42% identity, 86% coverage: 1:120/139 of query aligns to 555:668/689 of 8gjuJ

query
sites
8gjuJ

M

M

S

E

K

R

V

E

L

G

N

R

R

R

P

P

I

-

R

R

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L

L

V

V

A

A

K

K

V

M

G

-

L

-

D

-

G

-

H

-

D

D

R

R

G

G

A

A

K

K

V

V

I

I

A

A

T

T

S

G

L

F

R

A

D

D

A

L

G

G

M

F

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V

V

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D

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I

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G

G

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L

L

R

F

Q

Q

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T

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P

E

R

M

E

V

V

V

A

N

Q

T

Q

A

A

L

V

Q

D

E

A

D

D

V

V

D

H

A

A

I

V

G

G

I

V

S

S

I

T

L

L

S

A

G

A

A

G

H

H

M

K

T

T

V

L

F

V

P

P

K

E

I

L

I

I

H

K

F

E

M

L

K

N

E

S

K

L

Q

G

L

R

D

P

D

D

V

I

L

L

L

V

T

M

G

C

G

G

I

V

I

I

P

P

E

P

A

Q

D

D

R

Y

L

E

K

F

L

L

A

F

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M

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G

G

V

V

G

S

E

N

L

V

F

F

P

G

P

P

G

G

T

T

Sites not aligning to the query:

binding coenzyme a: 61, 63, 68, 71, 73, 150, 152, 181, 183, 222, 269, 271, 313, 314, 315, 348

Q59268 2-methyleneglutarate mutase; Alpha-methyleneglutarate mutase; EC 5.4.99.4 from Eubacterium barkeri (Clostridium barkeri) (see paper)
30% identity, 99% coverage: 1:137/139 of query aligns to 465:613/614 of Q59268

query
sites
Q59268

M

V

S

E

K

K

V

A

L

P

N

T

R

R

P

P

I

E

R

K

V

I

L

V

V

L

A

A

K

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G

G

L

A

D
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D

G

A

H
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H

D

V

R

N

G

G

A

I

K

N

V

V

I

I

A

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T

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S

A

L

F

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D

A

A

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Y

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G

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M

Q

N

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P

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M

S

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V

A

N

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A

A

L

A

Q

E

E

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G

V

A

D

D

A

A

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G

G

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V

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S

I

N

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L

S

L

G

G

A

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G

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I

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G

L

L

-

R

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D

D

K

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M

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C

G

A

G

G

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R

I

I

P

A

E

E

A

K

-

E

-

H

-

R

-

Q

-

F

-

E

D

E

R

K

L

I

K

Q

L

K

A

E

G

G

-

S

-

A

-

F

M

M

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G

V

M

G

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E

G

L

F

F

F

P

G

P

P

G

G

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M

P

A

E

S

D

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C

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V

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K

Y

I

I

I

Q

G

N

D

W

M

V

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T

N

E

A

N

K

R

K

D483 (= D19) mutation to N: Activity reduced 2000-fold.
H485 (= H21) mutation to Q: Loss of activity.

Sites not aligning to the query:

464 H→Q: No effect on activity.

Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
33% identity, 79% coverage: 9:118/139 of query aligns to 11:122/1086 of Q5KUG0

query
sites
Q5KUG0

I

V

R

R

V

F

L

V

V

T

A

A

K

S

V

S

G

L

L

F

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D

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H

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G

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A

A

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I

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F

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E

E

K

R

Q

G

L

A

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H

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I

L

R

L

I

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Y

G

G

-

G

-

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P

E

R

A

E

D

I

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K

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L

L

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M

Y

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G

A

E

R

L

I

F

F

P

S

P

P

Sites not aligning to the query:

213 K→A: Loss of GTPase and ATPase activities. No effect on the mutase activity.

5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
33% identity, 79% coverage: 9:118/139 of query aligns to 7:118/1061 of 5cjvA

query
sites
5cjvA

I

V

R

R

V

F

L

V

V

T

A

A

K

A

V

S

G

L

L

F

D

D

G
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G

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H

D
|
D

R
x
A

G
x
S

A

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K

N

V

I

I
x
M

A

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R

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L

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A

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G

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E

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V

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G

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N

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M

E

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V

N

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T

A

A

A

L

L

Q

Q

E

E

D

D

V

V

D

Q

A

G

I

I

G

A

I

I

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S

I

S

L
x
Y

S
x
Q

G

G

A

G

H

H

M

V

T

E

V

Y

F

F

P

K

K

Y

I

M

I

I

H

D

F

L

M

L

K

R

E

E

-

H

-

G

K

E

Q

H

L

I

D

Q

D

V

V

F

L

G

L
x
G

T

G

G
|
G

G

G

G
x
V

I

I

I

V

P

P

E

D

A

E

D

I

R

R

L

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K

E

L

L

A

Q

G

A

M

Y

G

G

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V

G

A

E

R

L

I

F
x
Y

P
x
S

P

P

binding cobalamin: G18 (= G20), H19 (= H21), D20 (= D22), A21 (≠ R23), S22 (≠ G24), M26 (≠ I28), Y66 (≠ L68), Q67 (≠ S69), G94 (≠ L93), G96 (= G95), V98 (≠ G97), Y116 (≠ F116), S117 (≠ P117)

Sites not aligning to the query:

active site: 6, 569, 750, 751
binding cobalamin: 129, 598, 603, 621, 713, 754, 755, 839, 840, 876, 877, 879, 964
binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 338, 373, 375, 944
binding Isovaleryl-coenzyme A: 556, 558, 560, 567, 569, 593, 648, 650, 699, 701, 703, 713, 743, 751, 792, 794, 832, 834
binding magnesium ion: 203, 229, 242, 242, 288, 288

5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
33% identity, 79% coverage: 9:118/139 of query aligns to 7:118/1063 of 5cjwA

query
sites
5cjwA

I

V

R

R

V

F

L

V

V

T

A

A

K

A

V

S

G

L

L

F

D

D

G
|
G

H
|
H

D
|
D

R
x
A

G
x
S

A

I

K

N

V

I

I
x
M

A

R

T

R

S

I

L

L

R

Q

D

S

A

Q

G

G

M

C

E

E

V

V

I

I

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G

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N

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P

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Q

M

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V

N

T

T

A

A

A

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Q

E

E

D

D

V

V

D

Q

A

G

I

I

G

A

I

I

S

S

I

S

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x
Y

S
x
Q

G

G

A

G

H

H

M

V

T

E

V

Y

F

F

P

K

K

Y

I

M

I

I

H

D

F

L

M

L

K

R

E

E

-

H

-

G

K

E

Q

H

L

I

D

Q

D

V

V

F

L

G

L
x
G

T

G

G
|
G

G

G

G
x
V

I

I

I

V

P

P

E

D

A

E

D

I

R

R

L

-

K

E

L

L

A

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G

A

M

Y

G

G

V

V

G

A

E

R

L

I

F
x
Y

P
x
S

P
|
P

binding cobalamin: G18 (= G20), H19 (= H21), D20 (= D22), A21 (≠ R23), S22 (≠ G24), M26 (≠ I28), Y66 (≠ L68), Q67 (≠ S69), G94 (≠ L93), G96 (= G95), V98 (≠ G97), Y116 (≠ F116), S117 (≠ P117), P118 (= P118)

Sites not aligning to the query:

active site: 6, 571, 752, 753
binding pivalyl-coenzyme A: 558, 560, 562, 569, 571, 595, 650, 652, 701, 703, 705, 745, 752, 753, 794, 796, 829, 834, 836
binding cobalamin: 600, 605, 623, 715, 753, 756, 757, 841, 842, 878, 879, 881, 966
binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377, 1062
binding magnesium ion: 203, 229, 242, 242, 290, 290

5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
33% identity, 79% coverage: 9:118/139 of query aligns to 7:118/1062 of 5cjtA

query
sites
5cjtA

I

V

R

R

V

F

L

V

V

T

A

A

K

A

V

S

G

L

L

F

D

D

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G

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H

D
|
D

R
x
A

G
x
S

A

I

K

N

V

I

I
x
M

A

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L

L

R

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S

A

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G

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G

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N

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T

T

A

A

A

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Q

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E

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A

G

I

I

G

A

I

I

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S

I

S

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x
Y

S
x
Q

G

G

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H

M

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E

V

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F

F

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M

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I

H

D

F

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M

L

K

R

E

E

-

H

-

G

K

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H

L

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L
x
G

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G

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x
V

I

I

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P

E

D

A

E

D

I

R

R

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K

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G

G

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S

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P

binding cobalamin: G18 (= G20), H19 (= H21), D20 (= D22), A21 (≠ R23), S22 (≠ G24), M26 (≠ I28), Y66 (≠ L68), Q67 (≠ S69), G94 (≠ L93), G96 (= G95), V98 (≠ G97), Y116 (≠ F116), S117 (≠ P117)

Sites not aligning to the query:

active site: 6, 569, 750, 751
binding cobalamin: 598, 603, 621, 713, 751, 754, 755, 839, 840, 876, 877, 879, 964
binding isobutyryl-coenzyme a: 556, 558, 560, 567, 569, 593, 648, 650, 699, 701, 703, 743, 750, 751, 792, 794, 827, 832, 834
binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 336, 337, 339, 374, 376, 944
binding magnesium ion: 203, 229, 242, 242, 289, 289

Query Sequence

>CA265_RS20010 FitnessBrowser__Pedo557:CA265_RS20010
MSKVLNRPIRVLVAKVGLDGHDRGAKVIATSLRDAGMEVIYTGLRQTPEMVVNTALQEDV
DAIGISILSGAHMTVFPKIIHFMKEKQLDDVLLTGGGIIPEADRLKLAGMGVGELFPPGT
TMASIVEYIQNWVTENRNF

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory