SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_026124693.1 NCBI__GCF_000341205.1:WP_026124693.1 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)
49% identity, 93% coverage: 5:133/138 of query aligns to 4:132/136 of I3VE74

query
sites
I3VE74

S

T

T

P

V

I

R

R

V

V

V

L

I

L

A

A

K

K

P

V

G

G

L

L

D

D

G

G

H
|
H

D

D

R

R

G

G

V

V

K

K

V

V

A

A

R

R

A

A

L

L

R

R

D

D

A

A

G

G

V

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

I

V

V

V

S

N

A

T

A

A

L

I

Q

Q

E

E

D

D

A

V

D

D

A

V

I

L

G

G

L

V

S

S

V

L

L

L

S

S

G

G

A

V

H

Q

M

L

T

T

I

V

F

F

A

P

R

K

V

I

M

F

E

K

L

L

E

D

E

E

N

R

G

G

A

A

T

G

D

D

V

L

R

I

V

V

F

I

G

A

G

G

I

V

I

M

P

P

E

D

E

E

D

D

I

A

P

A

E

A

L

I

E

R

R

K

L

L

G

G

V

V

A

R

K

E

I

V

F

L

T

L

P

Q

G

D

A

T

T

P

S

Q

E

A

I

I

G

I

E

D

W

S

V

I

R

R

D

S

N

L

I

V

P

A

A

A

H18 (= H19) binding axial binding residue

4r3uC Crystal structure of 2-hydroxyisobutyryl-coa mutase (see paper)
49% identity, 93% coverage: 5:133/138 of query aligns to 2:130/131 of 4r3uC

query
sites
4r3uC

S

T

T

P

V

I

R

R

V

V

V

L

I

L

A

A

K
|
K

P

V

G

G

L

L

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

V

K

K

V

V

V
|
V

A

A

R

R

A

A

L

L

R

R

D

D

A

A

G

G

V

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

I

V

V

V

S

N

A

T

A

A

L

I

Q

Q

E

E

D

D

A

V

D

D

A

V

I

L

G
|
G

L

V

S
|
S

V

L

L
|
L

S

S

G

G

A

V

H

Q

M

L

T

T

I

V

F

F

A

P

R

K

V

I

M

F

E

K

L

L

E

D

E

E

N

R

G

G

A

A

T

G

D

D

V

L

R

I

V

V

F
x
I

G
x
A

G
|
G

I

V

I

M

P

P

E

D

E

E

D

D

I

A

P

A

E

A

L

I

E

R

R

K

L

L

G

G

V

V

A

R

K

E

I

V

F
x
L

T
x
L

P
x
Q

G

D

A
x
T

T

P

S

Q

E

A

I

I

G

I

E

D

W

S

V

I

R

R

D

S

N

L

I

V

P

A

A

A

active site: K10 (= K13), D14 (= D17), H16 (= H19)
binding cobalamin: G15 (= G18), H16 (= H19), D17 (= D20), R18 (= R21), G19 (= G22), V23 (= V26), G59 (= G62), S61 (= S64), L63 (= L66), I89 (≠ F92), A90 (≠ G93), G91 (= G94), G92 (= G95), L111 (≠ F114), L112 (≠ T115), Q113 (≠ P116), T115 (≠ A118)

7reqA Methylmalonyl-coa mutase, 2-carboxypropyl-coa inhibitor complex (see paper)
41% identity, 83% coverage: 8:122/138 of query aligns to 596:710/725 of 7reqA

query
sites
7reqA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L

Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G

G

L

V

S
|
S

V

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I

V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K601 (= K13), D605 (= D17), H607 (= H19)
binding cobalamin: G606 (= G18), H607 (= H19), D608 (= D20), R609 (= R21), G610 (= G22), I614 (≠ V26), S652 (= S64), L654 (= L66), G682 (= G94), G683 (= G95), Y702 (≠ F114), T703 (= T115), T706 (≠ A118)

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)
41% identity, 83% coverage: 8:122/138 of query aligns to 596:710/725 of 3reqA

query
sites
3reqA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L

Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G
|
G

L

V

S
|
S

V

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I

V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P
|
P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K601 (= K13), D605 (= D17), H607 (= H19)
binding cobalamin: G606 (= G18), H607 (= H19), D608 (= D20), R609 (= R21), G610 (= G22), I614 (≠ V26), G650 (= G62), S652 (= S64), L654 (= L66), G682 (= G94), G683 (= G95), Y702 (≠ F114), T703 (= T115), P704 (= P116), T706 (≠ A118)

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)
41% identity, 83% coverage: 8:122/138 of query aligns to 596:710/725 of 2reqA

query
sites
2reqA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L

Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G
|
G

L

V

S
|
S

V

S

L
|
L

S
x
A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I

V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K601 (= K13), D605 (= D17), H607 (= H19)
binding cobalamin: G606 (= G18), H607 (= H19), D608 (= D20), R609 (= R21), G610 (= G22), I614 (≠ V26), G650 (= G62), S652 (= S64), L654 (= L66), A655 (≠ S67), G682 (= G94), G683 (= G95), Y702 (≠ F114), T703 (= T115), T706 (≠ A118)

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)
41% identity, 83% coverage: 8:122/138 of query aligns to 599:713/728 of P11653

query
sites
P11653

R

R

V

I

V

L

I

L

A

A

K

K

P

M

G

G

L

Q

D

D

G
|
G

H
|
H

D
|
D

R
|
R

G

G

V

Q

K

K

V

V

V

I

A

A

R

T

A

A

L

Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G

G

L

V

S
|
S

V

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G

G

G
|
G

I

V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F

Y

T

T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

G609 (= G18) binding cob(II)alamin
H610 (= H19) binding axial binding residue
D611 (= D20) binding cob(II)alamin
R612 (= R21) binding cob(II)alamin
S655 (= S64) binding cob(II)alamin
L657 (= L66) binding cob(II)alamin
G686 (= G95) binding cob(II)alamin
T709 (≠ A118) 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

5reqA Methylmalonyl-coa mutase, y89f mutant, substrate complex (see paper)
41% identity, 83% coverage: 8:122/138 of query aligns to 596:710/725 of 5reqA

query
sites
5reqA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L

Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G

G

L

V

S
|
S

V

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I
x
V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K601 (= K13), D605 (= D17), H607 (= H19)
binding cobalamin: G606 (= G18), H607 (= H19), D608 (= D20), R609 (= R21), G610 (= G22), I614 (≠ V26), S652 (= S64), L654 (= L66), G682 (= G94), G683 (= G95), V684 (≠ I96), Y702 (≠ F114), T703 (= T115), T706 (≠ A118)

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)
41% identity, 83% coverage: 8:122/138 of query aligns to 597:711/726 of 4reqA

query
sites
4reqA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L

Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G

G

L

V

S
|
S

V

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I
x
V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K602 (= K13), D606 (= D17), H608 (= H19)
binding cobalamin: G607 (= G18), H608 (= H19), D609 (= D20), R610 (= R21), G611 (= G22), I615 (≠ V26), S653 (= S64), L655 (= L66), G683 (= G94), G684 (= G95), V685 (≠ I96), Y703 (≠ F114), T704 (= T115), T707 (≠ A118)

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

6reqA Methylmalonyl-coa mutase, 3-carboxypropyl-coa inhibitor complex (see paper)
41% identity, 83% coverage: 8:122/138 of query aligns to 598:712/727 of 6reqA

query
sites
6reqA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L
x
Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G

G

L

V

S
|
S

V

S

L
|
L

S

A

G
|
G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I

V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K603 (= K13), D607 (= D17), H609 (= H19)
binding cobalamin: G608 (= G18), H609 (= H19), D610 (= D20), R611 (= R21), G612 (= G22), I616 (≠ V26), Y620 (≠ L30), S654 (= S64), L656 (= L66), G658 (= G68), G684 (= G94), G685 (= G95), Y704 (≠ F114), T705 (= T115), T708 (≠ A118)

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)
41% identity, 83% coverage: 8:122/138 of query aligns to 598:712/727 of 1e1cA

query
sites
1e1cA

R

R

V

I

V

L

I

L

A

A

K
|
K

P

M

G

G

L

Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

Q

K

K

V

V

V
x
I

A

A

R

T

A

A

L
x
Y

R

A

D

D

A

L

G

G

V

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

I

T

V

A

S

R

A

Q

A

A

L

V

Q

E

E

A

D

D

A

V

D

H

A

V

I

V

G

G

L

V

S
|
S

V

S

L
|
L

S

A

G

G

A

G

H

H

M

L

T

T

I

L

F

V

A

P

R

A

V

L

M

R

E

K

L

E

L

L

E

D

E

K

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

I

F

T

G

V

G
|
G

I
x
V

I

I

P

P

E

E

E

Q

D

D

I

F

P

D

E

E

L

L

E

R

R

K

L

D

G

G

V

A

A

V

K

E

I

I

F
x
Y

T
|
T

P

P

G

G

A
x
T

T

V

T

I

S

P

E

E

active site: K603 (= K13), D607 (= D17), H609 (= H19)
binding cobalamin: G608 (= G18), H609 (= H19), D610 (= D20), R611 (= R21), G612 (= G22), I616 (≠ V26), Y620 (≠ L30), S654 (= S64), L656 (= L66), G684 (= G94), G685 (= G95), V686 (≠ I96), Y704 (≠ F114), T705 (= T115), T708 (≠ A118)

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

Q5KUG0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Geobacillus kaustophilus (strain HTA426) (see paper)
44% identity, 80% coverage: 7:116/138 of query aligns to 11:122/1086 of Q5KUG0

query
sites
Q5KUG0

V

V

R

R

V

F

V

V

I

T

A

A

K

S

P

S

G

L

L

F

D

D

G

G

H

H

D

D

R

A

G

S

V

I

K

N

V

I

V

M

A

R

R

R

A

I

L

L

R

Q

D

A

A

S

G

G

V

A

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

E

M

E

I

I

V

V

S

N

A

A

L

I

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

V

S

S

V

S

L

Y

S

Q

G

G

A

G

H

H

M

M

T

E

I

F

F

F

A

K

R

Y

V

M

M

Y

E

D

L

L

E

Q

E

E

N

R

G

G

A

A

T

S

D

H

V

I

R

R

V

I

F

Y

G

G

-

G

-

V

I

I

P

P

E

R

E

E

D

-

I

I

P

K

E

E

L

L

E

H

R

E

L

Y

G

G

V

I

A

A

K

R

I

I

F

F

T

S

P

P

Sites not aligning to the query:

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

5cjwA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate pivalyl-coenzyme a (see paper)
42% identity, 83% coverage: 2:116/138 of query aligns to 2:118/1063 of 5cjwA

query
sites
5cjwA

G

G

A

P

A

A

S

N

T
x
K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G
|
G

H
|
H

D
|
D

R
x
A

G
x
S

V

I

K

N

V

I

V
x
M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L
x
Y

S
x
Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

G
|
G

G

G

-
x
G

-

G

-
x
V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F
x
Y

T
x
S

P
|
P

active site: K6 (≠ T6)
binding cobalamin: G18 (= G18), H19 (= H19), D20 (= D20), A21 (≠ R21), S22 (≠ G22), M26 (≠ V26), Y66 (≠ L66), Q67 (≠ S67), G94 (= G94), G96 (vs. gap), V98 (vs. gap), Y116 (≠ F114), S117 (≠ T115), P118 (= P116)

Sites not aligning to the query:

active site: 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)
42% identity, 83% coverage: 2:116/138 of query aligns to 2:118/1062 of 5cjtA

query
sites
5cjtA

G

G

A

P

A

A

S

N

T
x
K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G
|
G

H
|
H

D
|
D

R
x
A

G
x
S

V

I

K

N

V

I

V
x
M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L
x
Y

S
x
Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

G
|
G

G

G

-
x
G

-

G

-
x
V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F
x
Y

T
x
S

P

P

active site: K6 (≠ T6)
binding cobalamin: G18 (= G18), H19 (= H19), D20 (= D20), A21 (≠ R21), S22 (≠ G22), M26 (≠ V26), Y66 (≠ L66), Q67 (≠ S67), G94 (= G94), G96 (vs. gap), V98 (vs. gap), Y116 (≠ F114), S117 (≠ T115)

Sites not aligning to the query:

active site: 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

5cjvA Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, mg (holo-icmf/gdp), and substrate isovaleryl-coenzyme a (see paper)
42% identity, 83% coverage: 2:116/138 of query aligns to 2:118/1061 of 5cjvA

query
sites
5cjvA

G

G

A

P

A

A

S

N

T
x
K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G
|
G

H
|
H

D
|
D

R
x
A

G
x
S

V

I

K

N

V

I

V
x
M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L
x
Y

S
x
Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

G
|
G

G

G

-
x
G

-

G

-
x
V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F
x
Y

T
x
S

P

P

active site: K6 (≠ T6)
binding cobalamin: G18 (= G18), H19 (= H19), D20 (= D20), A21 (≠ R21), S22 (≠ G22), M26 (≠ V26), Y66 (≠ L66), Q67 (≠ S67), G94 (= G94), G96 (vs. gap), V98 (vs. gap), Y116 (≠ F114), S117 (≠ T115)

Sites not aligning to the query:

active site: 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

Q1LRY0 Fused isobutyryl-CoA mutase; EC 5.4.99.13; EC 3.6.5.- from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see 2 papers)
42% identity, 83% coverage: 2:116/138 of query aligns to 22:138/1093 of Q1LRY0

query
sites
Q1LRY0

G

G

A

P

A

A

S

N

T

K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G

G

H
|
H

D

D

R

A

G

S

V

I

K

N

V

I

V

M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L

Y

S

Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

-

G

-

V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F

Y

T

S

P

P

H39 (= H19) binding axial binding residue

Sites not aligning to the query:

169:417 GTPase chaperone MeaI
219:224 binding GTP
223 binding Mg(2+)
248 binding Mg(2+)
249 binding Mg(2+)
262 binding Mg(2+); binding Mg(2+)
265 binding GTP
310 binding Mg(2+); binding Mg(2+)
311 binding Mg(2+)
357:360 binding GTP
418:579 Linker
587 binding substrate
598 F→A: Switches the substrate specificity and enhances the catalytic efficiency of the isovaleryl-CoA mutase over the native isobutyryl-CoA mutase activity about 4000-fold. Is even more susceptible to inactivation than wild-type during turnover.
622 binding substrate
728 binding substrate
772 binding substrate
821 binding substrate
856 binding substrate
861 binding substrate
973 binding GTP
1092 binding GTP

4xc6A Isobutyryl-coa mutase fused with bound adenosylcobalamin, gdp, and mg (holo-icmf/gdp) (see paper)
42% identity, 83% coverage: 2:116/138 of query aligns to 2:118/1067 of 4xc6A

query
sites
4xc6A

G

G

A

P

A

A

S

N

T
x
K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G
|
G

H
|
H

D
|
D

R
x
A

G
x
S

V

I

K

N

V

I

V
x
M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L
x
Y

S
x
Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

G
|
G

G

G

-
x
G

-

G

-
x
V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F
x
Y

T
x
S

P
|
P

active site: K6 (≠ T6)
binding cobalamin: G18 (= G18), H19 (= H19), D20 (= D20), A21 (≠ R21), S22 (≠ G22), M26 (≠ V26), Y66 (≠ L66), Q67 (≠ S67), G94 (= G94), G96 (vs. gap), V98 (vs. gap), Y116 (≠ F114), S117 (≠ T115), P118 (= P116)

Sites not aligning to the query:

active site: 572, 753, 754
binding cobalamin: 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

8sslA Isobutyryl-coa mutase fused q341a in the presence of gtp (see paper)
42% identity, 83% coverage: 2:116/138 of query aligns to 1:117/1072 of 8sslA

query
sites
8sslA

G

G

A

P

A

A

S

N

T

K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G

G

H

H

D

D

R

A

G

S

V

I

K

N

V

I

V

M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L

Y

S

Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

-

G

-

V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F

Y

T

S

P

P

Sites not aligning to the query:

binding guanosine-5'-diphosphate: 200, 201, 202, 241, 244, 337, 339, 374, 375, 376, 1071
binding magnesium ion: 201, 241

4xc7A Isobutyryl-coa mutase fused with bound butyryl-coa and without cobalamin or gdp (apo-icmf) (see paper)
42% identity, 83% coverage: 2:116/138 of query aligns to 1:117/1053 of 4xc7A

query
sites
4xc7A

G

G

A

P

A

A

S

N

T
x
K

V

V

R

R

V

F

V

V

I

T

A

A

K

A

P

S

G

L

L

F

D

D

G

G

H

H

D

D

R

A

G

S

V

I

K

N

V

I

V

M

A

R

R

R

A

I

L

L

R

Q

D

S

A

Q

G

G

V

C

E

E

V

V

I

I

Y

H

T

L

G

G

L

H

R

N

Q

R

T

S

P

V

E

Q

M

E

I

V

V

V

S

T

A

A

L

L

Q

Q

E

E

D

D

A

V

D

Q

A

G

I

I

G

A

L

I

S

S

V

S

L

Y

S

Q

G

G

A

G

H

H

M

V

T

E

I

Y

F

F

A

K

R

Y

V

M

M

I

E

D

L

L

E

R

E

E

N

H

G

G

A

G

T

E

D

H

V

I

R

Q

V

V

F

F

G

G

-

G

-

V

I

I

I

V

P

P

E

D

E

E

D

-

I

I

P

R

E

E

L

L

E

Q

R

A

L

Y

G

G

V

V

A

A

K

R

I

I

F

Y

T

S

P

P

active site: K5 (≠ T6)

Sites not aligning to the query:

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

P22033 Methylmalonyl-CoA mutase, mitochondrial; MCM; Methylmalonyl-CoA isomerase; EC 5.4.99.2 from Homo sapiens (Human) (see 28 papers)
37% identity, 90% coverage: 8:131/138 of query aligns to 616:739/750 of P22033

query
sites
P22033

R
|
R

V
x
L

I
x
V

A
|
A

K
|
K

P
x
M

G
|
G

L
x
Q

D
|
D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V
x
A

K
|
K

V
|
V

V
x
I

A
|
A

R
x
T

A
x
G

L
x
F

R
x
A

D
|
D

A
x
L

G
|
G

V
x
F

E
x
D

V
|
V

I
x
D

Y
x
I

T
x
G

G
x
P

L
|
L

R
x
F

Q
|
Q

T
|
T

P
|
P

E
x
R

M
x
E

I
x
V

V
x
A

S
x
Q

A
x
Q

A
|
A

L
x
V

Q
x
D

E
x
A

D
|
D

A
x
V

D
x
H

A
|
A

I
x
V

G
|
G

L
x
I

S
|
S

V
x
T

L
|
L

S
x
A

G
x
A

A
x
G

H
|
H

M
x
K

T
|
T

I
x
L

F
x
V

A
x
P

R
x
E

V
x
L

M
x
I

E
x
K

L
x
E

L
|
L

E
x
N

E
x
S

N
x
L

G
|
G

A
x
R

T
x
P

D
|
D

V
x
I

R
x
L

V
|
V

F
x
M

G
x
C

G
|
G

I
x
V

I
|
I

P
|
P

E
x
P

E
x
Q

D
|
D

I
x
Y

P
x
E

E
x
F

L
|
L

E
x
F

R
x
E

L
x
V

G
|
G

V
|
V

A
x
S

K
x
N

I
x
V

F
|
F

T
x
G

P
|
P

G
|
G

A
x
T

T
x
R

T
x
I

S
x
P

E
x
K

I
x
A

G
x
A

E
x
V

W
x
Q

V
|
V

R
x
L

D
|
D

N
x
D

I
|
I

R616 (= R8) to C: in MMAM; mut0; dbSNP:rs765284825
L617 (≠ V9) to R: in MMAM; mut0; dbSNP:rs1554158775
K621 (= K13) to N: in MMAM; mut0
G623 (= G15) to R: in MMAM; mut0; dbSNP:rs121918254
Q624 (≠ L16) to R: in MMAM; no effect on protein abundance; dbSNP:rs768521956
D625 (= D17) 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 (= G18) to C: in MMAM; mut-; dbSNP:rs982110849
H627 (= H19) binding axial binding residue; to R: in MMAM; mut0; dbSNP:rs372486357
G630 (= G22) to E: in MMAM; mut0; dbSNP:rs143023066
V633 (= V25) 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 (≠ A29) to E: in MMAM; mut-; to R: in MMAM; mut0; dbSNP:rs781501004
F638 (≠ L30) to I: in MMAM; mut0
D640 (= D32) to Y: in MMAM; mut0; dbSNP:rs865815395
G642 (= G34) to R: in MMAM; mut-; dbSNP:rs747897332
G648 (≠ T40) 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 (≠ I61) to E: in MMAM; mut0; dbSNP:rs1360470463
I671 (≠ L63) to V: in dbSNP:rs8589
L674 (= L66) to F: in MMAM; decreased protein abundance; decreased methylmalonyl-CoA mutase activity; dbSNP:rs1164271240
H678 (= H70) to R: in MMAM; mut-; dbSNP:rs147094927
E684 (≠ R76) natural variant: E -> EL (in MMAM; mut-)
L685 (≠ V77) to R: in MMAM; mut-; dbSNP:rs864309739
R694 (≠ A86) 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 (≠ F92) 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 (= G95) to R: in MMAM; mut0; dbSNP:rs121918255
G717 (= G109) 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 (≠ T115) 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 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

8dyjB Crystal structure of human methylmalonyl-coa mutase in complex with adp and cob(ii)alamin (see paper)
37% identity, 90% coverage: 8:131/138 of query aligns to 580:703/708 of 8dyjB

query
sites
8dyjB

R

R

V

L

I

V

A

A

K

K

P

M

G

G

L

Q

D

D

G
|
G

H
|
H

D
|
D

R
|
R

G
|
G

V

A

K

K

V

V

V
x
I

A

A

R

T

A

G

L

F

R

A

D

D

A

L

G

G

V

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

I

V

V

A

S

Q

A

Q

A

A

L

V

Q

D

E

A

D

D

A

V

D

H

A

A

I

V

G

G

L

V

S
|
S

V

T

L
|
L

S

A

G
x
A

A

G

H

H

M

K

T

T

I

L

F

V

A

P

R

E

V

L

M

I

E

K

L

E

L

L

E

N

E

S

N

L

G

G

A

R

T

P

D

D

V

I

R

L

V

V

F

M

G

C

G
|
G

I
x
V

I

I

P

P

E

P

E

Q

D

D

I

Y

P

E

E

F

L

L

E

F

R

E

L

V

G

G

V

V

A

S

K

N

I

V

F
|
F

T
x
G

P

P

G

G

A
x
T

T

R

T

I

S

P

E

K

I

A

G

A

E

V

W

Q

V

V

R

L

D

D

N

D

I

I

binding cobalamin: G590 (= G18), H591 (= H19), D592 (= D20), R593 (= R21), G594 (= G22), I598 (≠ V26), S636 (= S64), L638 (= L66), A640 (≠ G68), G666 (= G94), G667 (= G95), V668 (≠ I96), F686 (= F114), G687 (≠ T115), T690 (≠ A118)

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

Query Sequence

>WP_026124693.1 NCBI__GCF_000341205.1:WP_026124693.1
MGAASTVRVVIAKPGLDGHDRGVKVVARALRDAGVEVIYTGLRQTPEMIVSAALQEDADA
IGLSVLSGAHMTIFARVMELLEENGATDVRVFGGGIIPEEDIPELERLGVAKIFTPGATT
SEIGEWVRDNIPALHAAG

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