SitesBLAST

Q46EH4 Methanol--corrinoid protein; Methanol:corrinoid methyltransferase 1 subunit of 27 kDa; MT1 subunit 27 kDa from Methanosarcina barkeri (strain Fusaro / DSM 804) (see paper)
34% identity, 91% coverage: 7:216/231 of query aligns to 36:244/258 of Q46EH4

query
sites
Q46EH4

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H129 (≠ G101) mutation to K: Does not affect cobalamin-binding.
H136 (= H108) mutation H->G,K: Abolishes cobalamin-binding.

Sites not aligning to the query:

256:258 HKH→KKK: Does not affect cobalamin-binding.

4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
33% identity, 74% coverage: 39:208/231 of query aligns to 33:199/206 of 4jgiB

query
sites
4jgiB

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active site: D95 (= D106), H97 (= H108), A148 (≠ T159)
binding co-methylcobalamin: L63 (≠ V69), D95 (= D106), L96 (≠ V107), H97 (= H108), D98 (= D109), I99 (= I110), G100 (= G111), F104 (≠ V115), G140 (≠ A151), S142 (= S153), L145 (≠ M156), G173 (= G182), G174 (= G183), V175 (≠ A184), S191 (≠ A200), T192 (≠ P201), N193 (≠ D202), A194 (= A203)

8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
35% identity, 79% coverage: 10:192/231 of query aligns to 2:181/507 of 8sseA

query
sites
8sseA

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binding cobalamin: H97 (= H108), G100 (= G111), V104 (= V115), S142 (= S153), L145 (≠ M156), V146 (≠ T157), I169 (≠ L180), G171 (= G182), G172 (= G183), A173 (= A184)

Sites not aligning to the query:

binding cobalamin: 405, 409, 451, 452, 453, 454, 463, 485, 488, 490, 492

1y80A Structure of a corrinoid (factor iiim)-binding protein from moorella thermoacetica
48% identity, 49% coverage: 96:208/231 of query aligns to 5:119/125 of 1y80A

query
sites
1y80A

G

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active site: D15 (= D106), H17 (= H108), T68 (= T159)
binding co-5-methoxybenzimidazolylcobamide: D15 (= D106), L16 (≠ V107), H17 (= H108), D18 (= D109), I19 (= I110), G20 (= G111), V24 (= V115), G60 (≠ A151), M61 (≠ L152), S62 (= S153), L64 (≠ M155), L65 (≠ M156), T66 (= T157), I91 (≠ L180), G93 (= G182), G94 (= G183), A95 (= A184), P112 (= P201), D113 (= D202), A114 (= A203)

3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
33% identity, 78% coverage: 8:188/231 of query aligns to 11:189/576 of 3ivaA

query
sites
3ivaA

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active site: D107 (= D106), H109 (= H108), S160 (≠ T159)
binding cobalamin: H109 (= H108), G112 (= G111), V116 (= V115), G152 (≠ A151), L153 (= L152), S154 (= S153), L156 (≠ M155), I157 (≠ M156), T158 (= T157), G183 (= G182), G184 (= G183)

Sites not aligning to the query:

binding cobalamin: 208, 209, 303, 443, 486, 488, 489, 495, 520, 521, 524, 527, 528
binding s-adenosyl-l-homocysteine: 447, 484, 485, 489, 491, 539

3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
33% identity, 78% coverage: 8:188/231 of query aligns to 11:189/577 of 3bulA

query
sites
3bulA

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active site: D107 (= D106), H109 (= H108), S160 (≠ T159)
binding cobalamin: H109 (= H108), V116 (= V115), G152 (≠ A151), L153 (= L152), S154 (= S153), L156 (≠ M155), I157 (≠ M156), T158 (= T157), G183 (= G182), G184 (= G183)

Sites not aligning to the query:

binding cobalamin: 208, 209, 210, 213, 302, 443, 486, 487, 488, 489, 495, 498, 521, 524, 527, 528

1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
33% identity, 78% coverage: 8:188/231 of query aligns to 11:189/246 of 1bmtA

query
sites
1bmtA

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V

M

K

C

S

A

A

D

R

A

V

L

M

Y

K

A

Q

G

A

L

V

E

A

I

Y

L

L

R

E

P

P

H

F

V

I

-

E

-

A

K

S

K

K

E

E

D

Q

I

G

K

K

V

T

K

N

G

G

Q

K

V

M

V

V

I

I

G

A

V

T

V

V

E

K

G

G

D
|
D

V
|
V

H
|
H

D
|
D

I
|
I

G

G

K

K

N

N

L
x
I

V

V

K

G

M

V

F

L

E

Q

V

C

A

N

G

N

F

Y

E

E

V

I

I

V

D

D

L

L

G

G

K

V

D

M

V

V

P

P

L

A

E

E

K

K

F

I

V

L

E

R

E

T

S

A

L

K

K

E

S

V

D

N

A

A

D

D

I

L

V

I

A
x
G

L
|
L

S
|
S

A

G

M
x
L

M
x
I

T
|
T

T

P

T
x
S

M

L

L

D

G

E

I

M

P

V

K

N

V

V

I

A

Q

K

M

E

I

M

R

E

E

R

K

Q

N

G

P

F

K

T

A

I

K

P

I

L

L

L

V

I

G
|
G

A
|
A

P

T

I

T

S

S

K

K

active site: D107 (= D106), H109 (= H108), S160 (≠ T159)
binding co-methylcobalamin: E44 (≠ M45), M48 (≠ V49), M51 (= M52), G55 (= G56), L65 (≠ V66), V68 (= V69), D107 (= D106), V108 (= V107), H109 (= H108), D110 (= D109), I111 (= I110), I115 (≠ L114), G152 (≠ A151), L153 (= L152), S154 (= S153), L156 (≠ M155), I157 (≠ M156), T158 (= T157), G183 (= G182), G184 (= G183), A185 (= A184)

Sites not aligning to the query:

binding co-methylcobalamin: 207, 209, 210

P13009 Methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS; EC 2.1.1.13 from Escherichia coli (strain K12) (see 5 papers)
33% identity, 78% coverage: 8:188/231 of query aligns to 661:839/1227 of P13009

query
sites
P13009

K

K

E

R

I

L

L

E

E

Y

K

S

L

L

K

V

R

K

G

G

V

I

V

T

E

E

F

F

D

I

E

E

D

Q

L

D

V

T

R

E

E

E

A

A

A

R

K

Q

E

Q

A

A

L

T

E

R

V

-

G

-

M

-

D

-

A

P

L

I

D

E

A

V

I

I

M
x
E

N

G

G

P

L

L

V

M

A

D

G

G

M

M

E

N

E

V

V

V

G

G

E

D

L

L

F

F

D

G

K

E

G

G

E

K

Y

M

F

F

V

L

P

P

E

Q

V

V

L

V

M

K

C

S

A

A

D

R

A

V

L

M

Y

K

A

Q

G

A

L

V

E

A

I

Y

L

L

R

E

P

P

H

F

V

I

-

E

-

A

K

S

K

K

E

E

D

Q

I

G

K

K

V

T

K

N

G

G

Q

K

V

M

V

V

I

I

G

A

V

T

V

V

E

K

G
|
G

D
|
D

V
|
V

H
|
H

D
|
D

I

I

G

G

K

K

N

N

L

I

V

V

K

G

M

V

F

L

E

Q

V

C

A

N

G

N

F

Y

E

E

V

I

I

V

D

D

L

L

G

G

K

V

D

M

V

V

P

P

L

A

E

E

K

K

F

I

V

L

E

R

E

T

S

A

L

K

K

E

S

V

D

N

A

A

D

D

I

L

V

I

A

G

L

L

S
|
S

A

G

M

L

M

I

T
|
T

T

P

T
x
S

M

L

L

D

G

E

I

M

P

V

K

N

V

V

I

A

Q

K

M

E

I

M

R

E

E

R

K

Q

N

G

P

F

K

T

A

I

K

P

I

L

L

L

V

I

G

G

A

A

P

T

I

T

S

S

K

K

E694 (≠ M45) binding
GDVHD 756:760 (= GDVHD 105:109) binding
D757 (= D106) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
H759 (= H108) binding axial binding residue; mutation to G: Loss of catalytic activity.
S804 (= S153) binding
T808 (= T157) binding
S810 (≠ T159) mutation to A: Decreases activity by about 40%.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
247 binding
310 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
311 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
860 binding
946 binding
1134 binding
1189:1190 binding

8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
30% identity, 83% coverage: 2:193/231 of query aligns to 627:808/841 of 8g3hA

query
sites
8g3hA

V

V

D

E

E

E

A

R

K

L

R

R

K

R

E

R

I

V

L

L

E

E

K

G

L

K

K

R

R

V

G

G

V

L

V

-

E

-

F

-

D

E

E

E

D

D

L

L

V

A

R

E

E

A

A

L

A

G

K

R

E

-

A

-

L

-

E

-

V

-

G

-

M

M

D

R

A

P

L

L

D

E

A

I

I

I

M

N

N

G

G

P

L

L

V

L

A

E

G

A

M

M

E

K

E

E

V

V

G

G

E

E

L

L

F
|
F

D

G

K

A

G

G

E

K

Y

M

F

Q

V

L

P

P

E

F

V
|
V

L

L

M

Q

C

A

A

A

D

E

A

V

L

M

Y
x
K

A

Q

G

A

L

V

E

A

I

Y

L

L

R

E

P

P

H

H

V

M

K

E

K

K

E

K

D

G

I

-

K

E

V

G

K

K

G

G

Q

K

V

L

V

V

I

L

G

A

V

T

V

V

E

K

G
|
G

D

D

V
|
V

H
|
H

D
|
D

I
|
I

G
|
G

K

K

N

N

L

L

V
|
V

K

D

M

I

F

L

E

T

V

N

A

N

G

G

F

Y

E

T

V

V

I

Y

D

N

L

L

G

G

K

I

D

K

V

V

P

P

L

I

E

E

K

E

F

M

V

L

E

K

E

A

S

V

L

D

K

E

S

V

D

K

A

P

D

H

I

A

V

L

A

G

L
x
M

S
|
S

A

G

M
x
L

M

L

T
x
V

T

K

T

S

M

T

L

Q

G

V

I

M

P

K

K

E

V

N

I

L

Q

E

M

Y

I

M

R

R

E

A

K

R

N

G

P

Y

K

T

A

L

K

P

I

V

L
x
I

V
x
L

G
|
G

A
|
A

P

A

I

L

S

T

K

R

E

A

T

Y

A

V

E

E

K

E

binding cobalamin: F675 (= F59), V685 (= V69), K693 (≠ Y77), G720 (= G105), V722 (= V107), H723 (= H108), D724 (= D109), I725 (= I110), G726 (= G111), V730 (= V115), M767 (≠ L152), S768 (= S153), L770 (≠ M155), V772 (≠ T157), I795 (≠ L180), L796 (≠ V181), G797 (= G182), G798 (= G183), A799 (= A184)

Sites not aligning to the query:

binding cobalamin: 328, 330, 331, 818, 819, 820, 821

Q99707 Methionine synthase; MS; 5-methyltetrahydrofolate--homocysteine methyltransferase; Cobalamin-dependent methionine synthase; Vitamin-B12 dependent methionine synthase; EC 2.1.1.13 from Homo sapiens (Human) (see 6 papers)
31% identity, 89% coverage: 2:207/231 of query aligns to 663:890/1265 of Q99707

query
sites
Q99707

V

T

D

D

E

E

A

W

K

R

R

N

K

G

E

P

I

V

L

E

E

E

K

R

L

L

K

E

R

Y

G

A

V

L

V

V

E

K

F

G

D

I

E

E

D

K

L

H

V

I

R

I

E

E

A

D

A

T

K

E

E

E

A

A

L

R

-

L

-

N

-

Q

E

K

V

K

G

Y

M

P

D

R

A

P

L

L

D

N

A

I

I

I

M

E

N

G

G

P

L

L

V

M

A

N

G

G

M

M

E

K

E

I

V

V

G

G

E

D

L

L

F

F

D

G

K

A

G

G

E

K

Y

M

F

F

V

L

P

P

E

Q

V

V

L

I

M

K

C

S

A

A

D

R

A

V

L

M

Y

K

A

K

G

A

L

V

E

G

I

H

L

L

R

I

P

P

H

F

V

M

K

E

K

K

E

E

-

R

-

E

-

T

-

R

-

V

-

L

-

N

-

G

-

T

-

V

-

E

D

E

I

D

K

P

V

Y

K

Q

G

G

Q

T

V

I

V

V

I

L

G

A

V

T

V

V

E

K

G

G

D

D

V

V

H

H

D

D

I

I

G

G

K

K

N

N

L

I

V

V

K

G

M

V

F

L

E

G

V

C

A

N

G

N

F

F

E

R

V

V

I

I

D

D

L

L

G

G

K

V

D

M

V

T

P

P

L

C

E

D

K

K

F

I

V

L

E

K

E

A

S

A

L

L

K

D

S

H

D

K

A

A

D

D

I

I

V

I

A

G

L

L

S

S

A

G

M

L

M

I

T

T

T

P

T

S

-

L

-

D

-

E

M

M

L

I

G

F

I

V

P

A

K

K

V

E

I

M

Q

E

M

R

I

L

R

A

E

I

K

R

N

I

P

P

K

-

A

-

K

-

I

L

L

L

V

I

G

G

A

A

P

T

I

T

S

S

K

K

-

T

E

H

T

T

A

A

E

V

K

K

W

I

G

A

A

P

D

R

G

Y

W

S

A

A

P

P

-

V

-

I

-

H

-

V

-

L

D

D

A

A

T

S

N

K

A

S

V

V

Sites not aligning to the query:

61 natural variant: R -> K
255 C → Y: in dbSNP:rs1140598
382:384 binding
449 binding
470 binding
537 binding
579 binding
585 binding
591 binding
919 D → G: in dbSNP:rs1805087
963 D→E: Decreases binding to MTRR; when associated with N-1071.
1071 K→N: Decreases binding to MTRR; when associated with E-963.

1i9cA Glutamate mutase from clostridium cochlearium: complex with adenosylcobalamin and substrate (see paper)
31% identity, 27% coverage: 95:156/231 of query aligns to 3:64/137 of 1i9cA

query
sites
1i9cA

K

K

G

K

Q

T

V

I

V

V

I

L

G

G

V
|
V

V

I

E

G

G
x
S

D
|
D

V
x
C

H
|
H

D
x
A

I

V

G
|
G

K

N

N

K

L

I

V
x
L

K

D

M

H

M

A

F

F

E

T

V

N

A

A

G

G

F

F

E

N

V

V

I

V

D

N

L

I

G

G

K

V

D

L

V

S

P

P

L

Q

E

E

K

N

F

F

V

I

E

K

E

A

S

A

L

I

K

E

S

T

D

K

A

A

D

D

I

A

V

I

A

L

L

V

S
|
S

A

S

M
x
L

M
x
Y

active site: V10 (= V102), D14 (= D106), H16 (= H108)
binding cobalamin: S13 (≠ G105), D14 (= D106), C15 (≠ V107), H16 (= H108), A17 (≠ D109), G19 (= G111), L23 (≠ V115), S61 (= S153), L63 (≠ M155), Y64 (≠ M156)

Sites not aligning to the query:

binding cobalamin: 65, 91, 92, 93, 95, 96, 121

8j2xA Saccharothrix syringae photocobilins protein, light state (see paper)
28% identity, 49% coverage: 94:206/231 of query aligns to 89:201/337 of 8j2xA

query
sites
8j2xA

V

T

K

R

G

G

Q

H

V

V

I

V

G

A

V

C

V

L

E

D

G

G

D

E

V
x
W

H
|
H

D
x
A

I
x
L

G
x
P

K

A

N

R

L

I

V
|
V

K

A

M

E

M

V

F

L

E

R

V

G

A

R

G

G

F

W

E

R

V

V

I

T

D

F

L

L

G

G

K

A

D

S

V

V

P

P

L

A

E

A

K

H

F

L

V

V

E

P

E

Y

S

L

L

E

K

E

S

H

D

G

A

P

D

D

I

A

V

V

A
|
A

L
|
L

S
|
S

A

C

M

T

M
x
L

T

P

T

R

T

-

M

-

L

-

G

G

I

L

P

P

K

R

V

A

I

D

Q

Q

M

V

I

V

R

A

E

A

-

C

K

R

N

A

P

T

K

G

A

T

K

P

I

V

L
|
L

V
|
V

G
|
G

A

L

P

G

I

F

S

G

K

P

E

D

T

G

A

-

E

-

K

R

W

W

-

A

-

R

-

V

-

L

G

G

A

A

D

G

G

T

W

W

A
|
A

P
|
P

D
x
T

A
|
A

T

R

N

A

A

A

binding cobalamin: W102 (≠ V107), H103 (= H108), A104 (≠ D109), L105 (≠ I110), P106 (≠ G111), V110 (= V115), A146 (= A151), L147 (= L152), S148 (= S153), L151 (≠ M156), L173 (= L180), V174 (= V181), G175 (= G182), G176 (= G183), A195 (= A200), P196 (= P201), T197 (≠ D202), A198 (= A203)

Sites not aligning to the query:

binding cobalamin: 46, 49, 53, 56, 57, 287
binding biliverdine ix alpha: 56, 250, 253, 254, 257, 258, 261, 264, 287, 292, 295, 297, 301

5c8dE Crystal structure of full-length thermus thermophilus carh bound to adenosylcobalamin (dark state) (see paper)
25% identity, 91% coverage: 10:220/231 of query aligns to 84:280/280 of 5c8dE

query
sites
5c8dE

I

L

L

L

E

E

K

A

L

L

K

L

R

R

G

G

V

D

V

L

E

A

F

G

D

A

E

E

D

A

L

L

V

F

R

R

E

R

A

G

A

L

K

R

E

F

A

W

L

G

E

P

V

E

G

G

M

V

D

-

A

-

L

-

D

-

A

-

I

L

M

E

N

H

G

L

L

L

V
x
L

A

P

G

V

M

L

E
x
R

E

E

V

V

G
|
G

E

E

L

A

F

W

D

H

K

R

G

G

E

E

Y

I

F

G

V

V

P

A

E

E

V
x
E

L

H

M

L

C

A

A
x
S

D

T

A

F

L

L

Y

R

A

A

G

R

L

L

E

Q

I

E

L

L

R

-

P

-

H

-

V

L

K

D

K

L

E

A

D

G

I

F

K

P

V

P

K

G

G

P

Q

P

V

V

V

L

I

V

G

T

V

T

V

P

E

P

G
|
G

D

E

V
x
R

H
|
H

D
x
E

I

I

G
|
G

K

A

N

M

L

L

V

A

K

A

M

Y

M

H

F

L

E

R

V

R

A

K

G

G

F

V

E

P

V

A

I

L

D

Y

L

L

G

G

K

P

D

D

V

T

P

P

L

L

E

P

K

D

F

L

V

R

E

A

E

L

S

A

L

R

K

R

S

L

D

G

A

A

D

G

I

A

V

V

A

V

L

L

S
|
S

A

A

M

V

M
x
L

T

S

T

E

T

P

M

L

L

R

G

A

I

L

P

P

K

D

V

-

I

-

Q

G

M

A

I

L

R

K

E

D

K

L

N

A

P

P

K

-

A

-

K

R

I

V

L

F

V

L

G
|
G

A

Q

P

G

I

A

S

G

K

P

E

E

T

E

A

A

E

R

K

R

W

L

G

G

A

A

D

E

G

Y

W
x
M

A

-

P

-

D

E

A
x
D

T
x
L

N

K

A

G

V

L

Q

A

E

E

A

A

I

L

N

W

M

L

I

P

K

R

G

G

L

P

K

E

K

K

E

E

binding cobalamin: L118 (≠ V49), R122 (≠ E53), G125 (= G56), E138 (≠ V69), S142 (≠ A73), G171 (= G105), R173 (≠ V107), H174 (= H108), E175 (≠ D109), G177 (= G111), S219 (= S153), L222 (≠ M156), G244 (= G182), G245 (= G183), M261 (≠ W199), D263 (≠ A203), L264 (≠ T204)

1ccwA Structure of the coenzyme b12 dependent enzyme glutamate mutase from clostridium cochlearium (see paper)
31% identity, 27% coverage: 95:156/231 of query aligns to 3:64/137 of 1ccwA

query
sites
1ccwA

K

K

G

K

Q

T

V

I

V

V

I

L

G

G

V
|
V

V

I

E

G

G

S

D
|
D

V
x
C

H
|
H

D
x
A

I

V

G
|
G

K

N

N

K

L
x
I

V

L

K

D

M

H

M

A

F

F

E

T

V

N

A

A

G

G

F

F

E

N

V

V

I

V

D

N

L

I

G

G

K

V

D

L

V

S

P

P

L

Q

E

E

K

L

F

F

V

I

E

K

E

A

S

A

L

I

K

E

S

T

D

K

A

A

D

D

I

A

V

I

A

L

L

V

S
|
S

A

S

M
x
L

M
x
Y

active site: V10 (= V102), D14 (= D106), H16 (= H108)
binding cyanocobalamin: D14 (= D106), C15 (≠ V107), H16 (= H108), A17 (≠ D109), G19 (= G111), I22 (≠ L114), S61 (= S153), L63 (≠ M155), Y64 (≠ M156)

Sites not aligning to the query:

binding cyanocobalamin: 65, 91, 92, 93, 95, 117, 121, 123

1cb7A Glutamate mutase from clostridium cochlearium reconstituted with methyl-cobalamin (see paper)
31% identity, 27% coverage: 95:156/231 of query aligns to 3:64/137 of 1cb7A

query
sites
1cb7A

K

K

G

K

Q

T

V

I

V

V

I

L

G

G

V
|
V

V

I

E

G

G

S

D
|
D

V
x
C

H
|
H

D
x
A

I

V

G
|
G

K

N

N

K

L

I

V
x
L

K

D

M

H

M

A

F

F

E

T

V

N

A

A

G

G

F

F

E

N

V

V

I

V

D

N

L

I

G

G

K

V

D

L

V

S

P

P

L

Q

E

E

K

L

F

F

V

I

E

K

E

A

S

A

L

I

K

E

S

T

D

K

A

A

D

D

I

A

V

I

A

L

L

V

S
|
S

A

S

M
x
L

M
x
Y

active site: V10 (= V102), D14 (= D106), H16 (= H108)
binding co-methylcobalamin: D14 (= D106), C15 (≠ V107), H16 (= H108), A17 (≠ D109), G19 (= G111), L23 (≠ V115), S61 (= S153), L63 (≠ M155), Y64 (≠ M156)

Sites not aligning to the query:

binding co-methylcobalamin: 65, 91, 92, 93, 95, 96, 121

5c8eA Crystal structure of thermus thermophilus carh bound to adenosylcobalamin and a 26-bp DNA segment (see paper)
25% identity, 81% coverage: 10:197/231 of query aligns to 83:258/273 of 5c8eA

query
sites
5c8eA

I

L

L

L

E

E

K

A

L

L

K

L

R

R

G

G

V

D

V

L

E

A

F

G

D

A

E

E

D

A

L

L

V

F

R

R

E

R

A

G

A

L

K

R

E

F

A

W

L

G

E

P

V

E

G

G

M

V

D

-

A

-

L

-

D

-

A

-

I

L

M

E

N

H

G

L

L

L

V
x
L

A

P

G

V

M
x
L

E

R

E

E

V

V

G
|
G

E

E

L

A

F

W

D

H

K

R

G

G

E

E

Y

I

F

G

V

V

P

A

E

E

V
x
E

L

H

M

L

C

A

A

S

D

T

A

F

L

L

Y

R

A

A

G

R

L

L

E

Q

I

E

L

L

R

-

P

-

H

-

V

L

K

D

K

L

E

A

D

G

I

F

K

P

V

P

K

G

G

P

Q

P

V

V

V

L

I

V

G

T

V

T

V

P

E

P

G
|
G

D

E

V
x
R

H
|
H

D
x
E

I

I

G
|
G

K

A

N

M

L

L

V

A

K

A

M

Y

M

H

F

L

E

R

V

R

A

K

G

G

F

V

E

P

V

A

I

L

D

Y

L

L

G

G

K

P

D

D

V

T

P

P

L

L

E

P

K

D

F

L

V

R

E

A

E

L

S

A

L

R

K

R

S

L

D

G

A

A

D

G

I

A

V

V

A

V

L

L

S
|
S

A

A

M

V

M
x
L

T

S

T

E

T

P

M

L

L

R

G

A

I

L

P

P

K

D

V

-

I

-

Q

G

M

A

I

L

R

K

E

D

K

L

N

A

P

P

K

-

A

-

K

R

I

V

L

F

V

L

G
|
G

A

Q

P

G

I

A

S

G

K

P

E

E

T

E

A

A

E

R

K

R

W

L

G

G

A

A

D

E

binding cobalamin: L117 (≠ V49), L120 (≠ M52), G124 (= G56), E137 (≠ V69), G170 (= G105), R172 (≠ V107), H173 (= H108), E174 (≠ D109), G176 (= G111), S218 (= S153), L221 (≠ M156), G243 (= G182), G244 (= G183)

Sites not aligning to the query:

binding cobalamin: 260, 263
binding : 20, 25, 26, 33, 36, 37, 38, 38, 39, 62

1id8A Nmr structure of glutamate mutase (b12-binding subunit) complexed with the vitamin b12 nucleotide (see paper)
29% identity, 27% coverage: 95:156/231 of query aligns to 3:64/137 of 1id8A

query
sites
1id8A

K

K

G

K

Q

T

V

I

V

V

I

L

G

G

V
|
V

V

I

E

G

G

S

D
|
D

V

C

H
|
H

D

A

I

V

G

G

K

N

N

K

L

I

V

L

K

D

M

H

M

S

F

F

E

T

V

N

A

A

G

G

F

F

E

N

V

V

I

V

D

N

L

I

G

G

K

V

D

L

V

S

P

S

L

Q

E

E

K

D

F

F

V

I

E

N

E

A

S

A

L

I

K

E

S

T

D

K

A

A

D

D

I

L

V

I

A

C

L

V

S
|
S

A

S

M
x
L

M

Y

active site: V10 (= V102), D14 (= D106), H16 (= H108)
binding phosphoric acid mono-[5-(5,6-dimethyl-benzoimidazol-1-yl)-4-hydroxy-2-hydroxymethyl-tetrahydro-furan-3-yl] ester: S61 (= S153), L63 (≠ M155)

Sites not aligning to the query:

binding phosphoric acid mono-[5-(5,6-dimethyl-benzoimidazol-1-yl)-4-hydroxy-2-hydroxymethyl-tetrahydro-furan-3-yl] ester: 91, 117, 119, 121

Query Sequence

>WP_012966230.1 NCBI__GCF_000025505.1:WP_012966230.1
MVDEAKRKEILEKLKRGVVEFDEDLVREAAKEALEVGMDALDAIMNGLVAGMEEVGELFD
KGEYFVPEVLMCADALYAGLEILRPHVKKEDIKVKGQVVIGVVEGDVHDIGKNLVKMMFE
VAGFEVIDLGKDVPLEKFVEESLKSDADIVALSAMMTTTMLGIPKVIQMIREKNPKAKIL
VGGAPISKETAEKWGADGWAPDATNAVQEAINMIKGLKKEIMGEEKGEEKN

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