SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_011969976.1 NCBI__GCF_000017145.1:WP_011969976.1 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)
54% identity, 86% coverage: 20:151/153 of query aligns to 3:134/136 of I3VE74

query
sites
I3VE74

N

Q

A

T

T

P

I

I

R

R

V

V

L

L

V

L

A

A

K

K

L

V

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G

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L

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H

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D

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R

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G

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K

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R

G

G

H18 (= H35) binding axial binding residue

4r3uC Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
53% identity, 86% coverage: 20:150/153 of query aligns to 1:131/131 of 4r3uC

query
sites
4r3uC

N

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T

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I

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R

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V

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L

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A

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K

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G

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D

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E

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R

active site: K10 (= K29), D14 (= D33), H16 (= H35)
binding cobalamin: G15 (= G34), H16 (= H35), D17 (= D36), R18 (= R37), G19 (= G38), V23 (= V42), G59 (= G78), S61 (= S80), L63 (= L82), I89 (≠ V108), A90 (= A109), G91 (= G110), G92 (= G111), L111 (≠ V130), L112 (≠ P131), Q113 (= Q132), T115 (≠ A134)

2xiqA Crystal structure of human methylmalonyl-coa mutase in complex with adenosylcobalamin and malonyl-coa (see paper)
47% identity, 70% coverage: 24:130/153 of query aligns to 581:687/714 of 2xiqA

query
sites
2xiqA

R

R

V

L

L

L

V

V

A

A

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K

L

M

G

G

L

Q

D
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D

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G

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H

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D

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R

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G

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K

K

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I

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A

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F

R

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D

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I

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F

active site: K586 (= K29), D590 (= D33), H592 (= H35)
binding cobalamin: G591 (= G34), H592 (= H35), D593 (= D36), R594 (= R37), G595 (= G38), I599 (≠ V42), G635 (= G78), S637 (= S80), L639 (= L82), A641 (≠ G84), G667 (= G110), G668 (= G111), F687 (≠ V130)

Sites not aligning to the query:

active site: 75, 229, 230
binding cobalamin: 75, 105, 108, 125, 193, 233, 320, 321, 357, 360, 361, 688, 691
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)
47% identity, 70% coverage: 24:130/153 of query aligns to 580:686/708 of 8dyjB

query
sites
8dyjB

R

R

V

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L

L

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V

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A

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K

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D

D

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F

binding cobalamin: G590 (= G34), H591 (= H35), D592 (= D36), R593 (= R37), G594 (= G38), I598 (≠ V42), S636 (= S80), L638 (= L82), A640 (≠ G84), G666 (= G110), G667 (= G111), V668 (= V112), F686 (≠ V130)

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, 687, 690

P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
46% identity, 69% coverage: 24:129/153 of query aligns to 616:721/750 of P22033

query
sites
P22033

R
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R

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x
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L
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L

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V

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A

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K

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D

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H

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D

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A

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D

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E

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D
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A
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N

I
x
V

R616 (= R24) to C: in MMAM; mut0; dbSNP:rs765284825
L617 (≠ V25) to R: in MMAM; mut0; dbSNP:rs1554158775
K621 (= K29) to N: in MMAM; mut0
G623 (= G31) to R: in MMAM; mut0; dbSNP:rs121918254
Q624 (≠ L32) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
D625 (= D33) 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 (= G34) to C: in MMAM; mut-; dbSNP:rs982110849
H627 (= H35) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
G630 (= G38) to E: in MMAM; mut0; dbSNP:rs143023066
V633 (= V41) 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 (≠ I45) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
F638 (≠ L46) to I: in MMAM; mut0
D640 (= D48) to Y: in MMAM; mut0; dbSNP:rs865815395
G642 (= G50) to R: in MMAM; mut-; dbSNP:rs747897332
G648 (≠ T56) 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 (≠ I77) to E: in MMAM; mut0; dbSNP:rs1360470463
I671 (≠ V79) to V: in dbSNP:rs8589
L674 (= L82) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
H678 (= H86) to R: in MMAM; mut-; dbSNP:rs147094927
E684 (= E92) natural variant: E -> EL (in MMAM; mut-)
L685 (= L93) to R: in MMAM; mut-; dbSNP:rs864309739
R694 (≠ A102) to L: in MMAM; mut-; decreased protein abundance; loss of methylmalonyl-CoA mutase activity; decreased affinity for adenosylcob(III)alamin; alters thermodynamic stability; dbSNP:rs756225782; 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 (≠ V108) 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 (= G111) to R: in MMAM; mut0; dbSNP:rs121918255
G717 (= G125) 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

Sites not aligning to the query:

1:32 modified: transit peptide, Mitochondrion
7:750 natural variant: Missing (in MMAM; mut-)
50 binding malonyl-CoA
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 malonyl-CoA
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 malonyl-CoA
108 R → C: in MMAM; mut0; dbSNP:rs121918257; R → G: in MMAM; mut-; dbSNP:rs121918257; 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; dbSNP:rs1237080100
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; dbSNP:rs2127420039; 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 malonyl-CoA
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 malonyl-CoA; R → Q: in MMAM; mut0; dbSNP:rs770810987
228:750 natural variant: Missing (in MMAM; mut0)
230 T → I: in MMAM; mut-; dbSNP:rs879253833; 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 malonyl-CoA
262 S → N: in MMAM; mut0; dbSNP:rs1767683356
265 binding malonyl-CoA; 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; dbSNP:rs138374956
304:306 binding malonyl-CoA
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; dbSNP:rs2127418704
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; dbSNP:rs1767612147
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; dbSNP:rs1400022403
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; dbSNP:rs2127416800
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; dbSNP:rs1767288356
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
615 P → L: in MMAM; mut0; affects proper folding; reduced strongly protein level; dbSNP:rs1554158777; P → R: in MMAM; mut0; dbSNP:rs1554158777; P → T: in MMAM; mut0; affects proper folding; reduced strongly protein level; loss of methylmalonyl-CoA mutase activity; dbSNP:rs1302409621
723 G → D: in MMAM; decreased protein expression; decreased methylmalonyl-CoA mutase activity; dbSNP:rs755077681

6oxdA Structure of mycobacterium tuberculosis methylmalonyl-coa mutase with adenosyl cobalamin (see paper)
43% identity, 71% coverage: 24:131/153 of query aligns to 605:712/736 of 6oxdA

query
sites
6oxdA

R

R

V

I

L

L

V

I

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G

G

A

Q

K

K

V

V

V

I

A

A

R

T

I

A

L

F

R

A

D

D

A

I

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

S

L

L

Y

F

K

S

S

T

P

P

K

E

D

E

V

V

V

A

Q

R

A

Q

A

A

I

A

Q

D

E

N

D

D

V

V

D

H

V

V

I

I

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G
x
A

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

D

C

A

L

L

R

A

E

Q

E

V

G

G

A

R

E

P

H

D

V

I

L

M

V

I

V

V

A

V

G
|
G

V

V

I

I

P

P

E

P

Q

G

D

D

Y

F

P

D

A

E

L

L

L

Y

E

A

C

A

G

G

V

A

D

T

A

A

I

I

V
x
F

P
|
P

active site: K610 (= K29), D614 (= D33), H616 (= H35)
binding cobalamin: G615 (= G34), H616 (= H35), D617 (= D36), R618 (= R37), S661 (= S80), L663 (= L82), A665 (≠ G84), G691 (= G110), G692 (= G111), F711 (≠ V130), P712 (= P131)

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, 715
binding Itaconyl coenzyme A: 86, 88, 89, 93, 96, 98, 100, 175, 177, 206, 218, 255, 294, 296, 298, 337, 338, 339, 341, 372

1e1cA Methylmalonyl-coa mutase h244a mutant (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 598:699/727 of 1e1cA

query
sites
1e1cA

R

R

V

I

L

L

V

L

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

V
x
I

A

A

R

T

I

A

L
x
Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G
|
G

V
|
V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

active site: K603 (= K29), D607 (= D33), H609 (= H35)
binding cobalamin: G608 (= G34), H609 (= H35), D610 (= D36), R611 (= R37), G612 (= G38), I616 (≠ V42), Y620 (≠ L46), S654 (= S80), L656 (= L82), G684 (= G110), G685 (= G111), V686 (= V112)

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, 704, 705, 708, 713
binding desulfo-coenzyme a: 74, 77, 80, 81, 84, 86, 113, 163, 165, 194, 282, 284, 327, 360

P11653 Methylmalonyl-CoA mutase large subunit; MCM-alpha; EC 5.4.99.2 from Propionibacterium freudenreichii subsp. shermanii (see 4 papers)
43% identity, 67% coverage: 24:125/153 of query aligns to 599:700/728 of P11653

query
sites
P11653

R

R

V

I

L

L

V

L

A

A

K

K

L

M

G

G

L

Q

D

D

G
|
G

H
|
H

D
|
D

R
|
R

G

G

A

Q

K

K

V

V

V

I

A

A

R

T

I

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G

G

G
|
G

V

V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

G609 (= G34) binding cob(II)alamin
H610 (= H35) binding axial binding residue
D611 (= D36) binding cob(II)alamin
R612 (= R37) binding cob(II)alamin
S655 (= S80) binding cob(II)alamin
L657 (= L82) binding cob(II)alamin
G686 (= G111) binding cob(II)alamin

Sites not aligning to the query:

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

4reqA Methylmalonyl-coa mutase substrate complex (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 597:698/726 of 4reqA

query
sites
4reqA

R

R

V

I

L

L

V

L

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

V
x
I

A

A

R

T

I

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G
|
G

V
|
V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

active site: K602 (= K29), D606 (= D33), H608 (= H35)
binding cobalamin: G607 (= G34), H608 (= H35), D609 (= D36), R610 (= R37), G611 (= G38), I615 (≠ V42), S653 (= S80), L655 (= L82), G683 (= G110), G684 (= G111), V685 (= V112)

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, 703, 704, 707
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

5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 596:697/725 of 5reqA

query
sites
5reqA

R

R

V

I

L

L

V

L

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

V
x
I

A

A

R

T

I

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G
|
G

V
|
V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

active site: K601 (= K29), D605 (= D33), H607 (= H35)
binding cobalamin: G606 (= G34), H607 (= H35), D608 (= D36), R609 (= R37), G610 (= G38), I614 (≠ V42), S652 (= S80), L654 (= L82), G682 (= G110), G683 (= G111), V684 (= V112)

Sites not aligning to the query:

active site: 86, 240, 241
binding cobalamin: 116, 136, 204, 241, 244, 330, 331, 367, 368, 370, 702, 703, 706
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

6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 598:699/727 of 6reqA

query
sites
6reqA

R

R

V

I

L

L

V

L

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

V
x
I

A

A

R

T

I

A

L
x
Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G
|
G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G
|
G

V

V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

active site: K603 (= K29), D607 (= D33), H609 (= H35)
binding cobalamin: G608 (= G34), H609 (= H35), D610 (= D36), R611 (= R37), G612 (= G38), I616 (≠ V42), Y620 (≠ L46), S654 (= S80), L656 (= L82), G658 (= G84), G684 (= G110), G685 (= G111)

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, 704, 705, 708

7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 596:697/725 of 7reqA

query
sites
7reqA

R

R

V

I

L

L

V

L

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

V
x
I

A

A

R

T

I

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G

G

V

V

S
|
S

L

S

L
|
L

S

A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G
|
G

V

V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

active site: K601 (= K29), D605 (= D33), H607 (= H35)
binding cobalamin: G606 (= G34), H607 (= H35), D608 (= D36), R609 (= R37), G610 (= G38), I614 (≠ V42), S652 (= S80), L654 (= L82), G682 (= G110), G683 (= G111)

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, 702, 703, 706

3reqA Methylmalonyl-coa mutase, substrate-free state (poor quality structure) (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 596:697/725 of 3reqA

query
sites
3reqA

R

R

V

I

L

L

V

L

A

A

K
|
K

L

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

A

Q

K

K

V

V

V
x
I

A

A

R

T

I

A

L

Y

R

A

D

D

A

L

G

G

M

F

E

D

V

V

V

D

Y

V

T

G

G

P

L

L

Y

F

K

Q

S

T

P

P

K

E

D

E

V

T

V

A

Q

R

A

Q

A

A

I

V

Q

E

E

A

D

D

V

V

D

H

V

V

I

V

G
|
G

V

V

S
|
S

L

S

L
|
L

S

A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

V

I

L

L

V

I

V

T

A

V

G
|
G

V

V

I

I

P

P

E

E

Q

Q

D

D

Y

F

P

D

A

E

L

L

L

R

E

K

C

D

G

G

active site: K601 (= K29), D605 (= D33), H607 (= H35)
binding cobalamin: G606 (= G34), H607 (= H35), D608 (= D36), R609 (= R37), G610 (= G38), I614 (≠ V42), G650 (= G78), S652 (= S80), L654 (= L82), G682 (= G110), G683 (= G111)

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, 702, 703, 704, 706

2reqA Methylmalonyl-coa mutase, non-productive coa complex, in open conformation representing substrate-free state (see paper)
43% identity, 67% coverage: 24:125/153 of query aligns to 596:697/725 of 2reqA

query
sites
2reqA

R

R

V

I

L

L

V

L

A

A

K
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K

L

M

G

G

L

Q

D
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D

G
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G

H
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H

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D

R
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R

G
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G

A

Q

K

K

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x
I

A

A

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Y

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D

A

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G

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E

D

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V

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Y

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G

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Y

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P

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E

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A

A

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Q

E

E

A

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D

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D

H

V

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I

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G
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G

V

V

S
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S

L

S

L
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L

S
x
A

G

G

S

G

H

H

V

L

P

T

L

L

F

V

R

P

E

A

L

L

C

R

R

K

C

E

L

L

R

D

E

K

E

L

G

G

A

R

E

P

H

D

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I

L

L

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I

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T

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G

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I

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E

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Q

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D

Y

F

P

D

A

E

L

L

L

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E

K

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D

G

G

active site: K601 (= K29), D605 (= D33), H607 (= H35)
binding cobalamin: G606 (= G34), H607 (= H35), D608 (= D36), R609 (= R37), G610 (= G38), I614 (≠ V42), G650 (= G78), S652 (= S80), L654 (= L82), A655 (≠ S83), G682 (= G110), G683 (= G111)

Sites not aligning to the query:

active site: 86, 240, 241
binding cobalamin: 203, 204, 244, 245, 331, 368, 702, 703, 706
binding coenzyme a: 72, 79, 318

8gjuJ Crystal structure of human methylmalonyl-coa mutase (mmut) in complex with methylmalonic acidemia type a protein (mmaa), coenzyme a, and gdp (see paper)
43% identity, 70% coverage: 24:130/153 of query aligns to 563:664/689 of 8gjuJ

query
sites
8gjuJ

R

R

V

L

L

L

V

V

A

A

K

K

L

M

G

-

L

-

D

-

G

-

H

-

D

D

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R

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G

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A

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K

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V

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A

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A

A

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E

A

D

D

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H

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A

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G

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V

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S

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T

L

L

S

A

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A

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L

F

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E

E

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L

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N

E

S

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L

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G

A

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E

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L

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A

C

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G

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V

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P

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Q

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D

Y

Y

P

E

A

F

L

L

L

F

E

E

C

V

G

G

V

V

D

S

A

N

I

V

V

F

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

5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
41% identity, 56% coverage: 23:108/153 of query aligns to 7:92/1063 of 5cjwA

query
sites
5cjwA

I

V

R

R

V

F

L

V

V

T

A

A

K

A

L

S

G

L

L

F

D

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G

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H

D
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D

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x
A

G
x
S

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N

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x
M

A

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A

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E

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D

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V

D

Q

V

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I

I

G

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S

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x
Y

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x
Q

G

G

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G

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H

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F

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R

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binding cobalamin: G18 (= G34), H19 (= H35), D20 (= D36), A21 (≠ R37), S22 (≠ G38), M26 (≠ V42), Y66 (≠ L82), Q67 (≠ S83)

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: 94, 96, 98, 116, 117, 118, 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

5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
41% identity, 56% coverage: 23:108/153 of query aligns to 7:92/1061 of 5cjvA

query
sites
5cjvA

I

V

R

R

V

F

L

V

V

T

A

A

K

A

L

S

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L

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G

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H

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D

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x
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M

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A

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I

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x
Y

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x
Q

G

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H

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F

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binding cobalamin: G18 (= G34), H19 (= H35), D20 (= D36), A21 (≠ R37), S22 (≠ G38), M26 (≠ V42), Y66 (≠ L82), Q67 (≠ S83)

Sites not aligning to the query:

active site: 6, 569, 750, 751
binding cobalamin: 94, 96, 98, 116, 117, 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

5cjtA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isobutyryl-coenzyme a (see paper)
41% identity, 56% coverage: 23:108/153 of query aligns to 7:92/1062 of 5cjtA

query
sites
5cjtA

I

V

R

R

V

F

L

V

V

T

A

A

K

A

L

S

G

L

L

F

D

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G

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H

D
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D

R
x
A

G
x
S

A

I

K

N

V

I

V
x
M

A

R

R

R

I

I

L

L

R

Q

D

S

A

Q

G

G

M

C

E

E

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V

V

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Y

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G

G

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S

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V

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E

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V

Q

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A

A

I

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Q

Q

E

E

D

D

V

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D

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V

G

I

I

G

A

V

I

S

S

L

S

L
x
Y

S
x
Q

G

G

S

G

H

H

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V

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E

L

Y

F

F

R

K

E

Y

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C

I

R

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C

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L

L

R

R

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E

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G

G

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H

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V

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binding cobalamin: G18 (= G34), H19 (= H35), D20 (= D36), A21 (≠ R37), S22 (≠ G38), M26 (≠ V42), Y66 (≠ L82), Q67 (≠ S83)

Sites not aligning to the query:

active site: 6, 569, 750, 751
binding cobalamin: 94, 96, 98, 116, 117, 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

4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
41% identity, 56% coverage: 23:108/153 of query aligns to 6:91/1053 of 4xc7A

query
sites
4xc7A

I

V

R

R

V

F

L

V

V

T

A

A

K

A

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L

L

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G

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H

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D

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A

G

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V

I

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R

R

R

I

I

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L

R

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S

A

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G

G

M

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E

E

V

V

V

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Y

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G

L

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V

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A

I

L

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E

E

D

D

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V

D

Q

V

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I

I

G

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I

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S

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S

L

Y

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G

G

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H

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E

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F

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Y

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E

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F

Sites not aligning to the query:

active site: 5, 566, 747, 748
binding Butyryl Coenzyme A: 553, 557, 564, 566, 590, 645, 647, 696, 698, 740, 789, 791, 824, 829, 831

4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
41% identity, 56% coverage: 23:108/153 of query aligns to 7:92/1067 of 4xc6A

query
sites
4xc6A

I

V

R

R

V

F

L

V

V

T

A

A

K

A

L

S

G

L

L

F

D

D

G
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G

H
|
H

D
|
D

R
x
A

G
x
S

A

I

K

N

V

I

V
x
M

A

R

R

R

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I

L

L

R

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D

S

A

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G

M

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E

E

V

V

V

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Y

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G

G

L

H

Y

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S

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V

Q

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A

A

I

L

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Q

E

E

D

D

V

V

D

Q

V

G

I

I

G

A

V

I

S

S

L

S

L
x
Y

S
x
Q

G

G

S

G

H

H

V

V

P

E

L

Y

F

F

R

K

E

Y

L

M

C

I

R

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C

L

L

L

R

R

E

E

E

H

G

G

A

G

E

E

H

H

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L

Q

V

V

V

F

binding cobalamin: G18 (= G34), H19 (= H35), D20 (= D36), A21 (≠ R37), S22 (≠ G38), M26 (≠ V42), Y66 (≠ L82), Q67 (≠ S83)

Sites not aligning to the query:

active site: 6, 572, 753, 754
binding cobalamin: 94, 96, 98, 116, 117, 118, 129, 601, 606, 624, 716, 754, 757, 758, 842, 843, 879, 880, 882, 967
binding guanosine-5'-diphosphate: 199, 201, 202, 203, 204, 245, 337, 338, 340, 375, 377, 947
binding magnesium ion: 203, 229, 242, 242, 290, 290

Query Sequence

>WP_011969976.1 NCBI__GCF_000017145.1:WP_011969976.1
MADTKGAGAVIEANEASHTNATIRVLVAKLGLDGHDRGAKVVARILRDAGMEVVYTGLYK
SPKDVVQAAIQEDVDVIGVSLLSGSHVPLFRELCRCLREEGAEHVLVVAGGVIPEQDYPA
LLECGVDAIVPQEARAGLIVTAITDLVAARGRI

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