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, 93% coverage: 7:204/213 of query aligns to 39:234/258 of Q46EH4

query
sites
Q46EH4

L

L

L

I

H

Y

E

P

V

I

A

A

D

K

A

A

V

I

I

F

S

E

C

G

K

E

E

D

K

D

V

V

L

V

E

E

A

G

V

L

E

Q

K

A

A

A

-

I

R

E

A

A

E

G

V

K

P

D

P

P

E

I

E

D

I

L

I

I

E

D

K

D

G

A

L

L

S

M

A

V

G

G

M

M

N

G

Q

V

V

V

G

I

V

R

L

L

F

Y

E

D

R

E

G

G

K

V

L

I

F

F

L

L

P

P

H

N

V

V

M

M

A

S

A

A

D

D

A

A

M

M

T

L

T

E

G

G

V

I

K

E

L

Y

L

C

E

K

A

E

D

N

L

S

P

G

A

A

G

T

A

P

E

K

K

T

K

K

L

-

G

G

V

T

I

V

V

V

N

C

G
x
H

T

V

V

A

E

E

G

G

D

D

V

V

H
|
H

D

D

I

I

G

G

K

K

S

N

I

I

V

V

S

T

T

A

M

L

L

L

Q

R

S

A

A

N

G

G

F

Y

E

N

V

V

H

V

D

D

I

L

G

G

R

R

D

D

V

V

P

P

I

A

R

E

D

E

F

V

I

L

E

A

K

A

A

V

K

Q

E

K

T

E

D

K

A

P

D

I

M

M

I

L

G

T

I

G

S

T

A

A

L

L

M

M

T

T

L

M

Q

Y

G

A

Q

F

R

K

D

E

V

V

I

N

E

D

L

M

L

L

K

L

E

E

E

N

G

G

L

I

R

-

S

-

R

K

V

I

K

P

V

F

M

A

V

C

G

G

A

G

P

A

A

V

T

N

Q

Q

A

D

W

F

A

V

D

S

K

Q

I

F

G

A

A

L

D

G

C

V

Y

Y

A

G

E

E

N

E

A

A

S

A

E

D

A

A

H129 (≠ G97) mutation to K: Does not affect cobalamin-binding.
H136 (= H104) mutation H->G,K: Abolishes cobalamin-binding.

Sites not aligning to the query:

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

1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
38% identity, 90% coverage: 21:212/213 of query aligns to 23:221/246 of 1bmtA

query
sites
1bmtA

E

E

K

F

V

I

L

E

E

Q

A

D

V

T

E

E

K

E

A

A

R

R

A

Q

E

Q

V

A

P

T

-

R

P

P

E

I

E

E

I

V

I

I

E
|
E

K

G

G

P

L

L

S
x
M

A

D

G

G

M
|
M

N

N

Q

V

V

V

G
|
G

V

D

L

L

F

F

E

G

R

E

G

G

K

K

L

M

F

F

L
|
L

P

P

H

Q

V
|
V

M

V

M

K

A

S

A

A

D

R

A

V

M

M

T

K

T

Q

G

A

V

V

K

A

L

Y

L

L

E

E

A

P

D

F

L

I

P

E

A

A

G

S

A

K

E

E

-

Q

-

G

K

K

K

T

L

N

G

G

V

K

I

M

V

V

N

I

G

A

T

T

V

V

E

K

G

G

D
|
D

V
|
V

H
|
H

D
|
D

I
|
I

G

G

K

K

S

N

I
|
I

V

V

S

G

T

V

M

V

L

L

Q

Q

S

C

A

N

G

N

F

Y

E

E

V

I

H

V

D

D

I

L

G

G

R

V

D

M

V

V

P

P

I

A

R

E

D

K

F

I

I

L

E

R

K

T

A

A

K

K

E

E

T

V

D

N

A

A

D

D

M

L

I

I

G
|
G

I
x
L

S
|
S

A

G

L
|
L

M
x
I

T
|
T

T

P

T
x
S

L

L

Q

D

G

E

Q

M

R

V

D

N

V

V

I

A

E

K

L

E

L

M

K

E

E

R

E

Q

G

G

L

F

R

-

S

-

R

T

V

I

K

P

V

L

M

L

V

I

G
|
G

A
|
A

P

T

A

T

T

S

Q

K

A

A

W

H

A

T

-

A

-

V

-

K

-

I

-

E

-

Q

D

N

K

Y

I

S

G

G

A

P

D

T

C

V

Y

Y

A
x
V

E

Q

N
|
N

A
|
A

S

S

E

R

A

T

V

V

A

G

K

V

A

V

K

A

E

A

L

L

active site: D107 (= D102), H109 (= H104), S160 (≠ T155)
binding co-methylcobalamin: E44 (= E41), M48 (≠ S45), M51 (= M48), G55 (= G52), L65 (= L62), V68 (= V65), D107 (= D102), V108 (= V103), H109 (= H104), D110 (= D105), I111 (= I106), I115 (= I110), G152 (= G147), L153 (≠ I148), S154 (= S149), L156 (= L151), I157 (≠ M152), T158 (= T153), G183 (= G180), G184 (= G181), A185 (= A182), V207 (≠ A198), N209 (= N200), A210 (= A201)

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)
38% identity, 90% coverage: 21:212/213 of query aligns to 673:871/1227 of P13009

query
sites
P13009

E

E

K

F

V

I

L

E

E

Q

A

D

V

T

E

E

K

E

A

A

R

R

A

Q

E

Q

V

A

P

T

-

R

P

P

E

I

E

E

I

V

I

I

E
|
E

K

G

G

P

L

L

S

M

A

D

G

G

M

M

N

N

Q

V

V

V

G

G

V

D

L

L

F

F

E

G

R

E

G

G

K

K

L

M

F

F

L

L

P

P

H

Q

V

V

M

V

M

K

A

S

A

A

D

R

A

V

M

M

T

K

T

Q

G

A

V

V

K

A

L

Y

L

L

E

E

A

P

D

F

L

I

P

E

A

A

G

S

A

K

E

E

-

Q

-

G

K

K

K

T

L

N

G

G

V

K

I

M

V

V

N

I

G

A

T

T

V

V

E

K

G
|
G

D
|
D

V
|
V

H
|
H

D
|
D

I

I

G

G

K

K

S

N

I

I

V

V

S

G

T

V

M

V

L

L

Q

Q

S

C

A

N

G

N

F

Y

E

E

V

I

H

V

D

D

I

L

G

G

R

V

D

M

V

V

P

P

I

A

R

E

D

K

F

I

I

L

E

R

K

T

A

A

K

K

E

E

T

V

D

N

A

A

D

D

M

L

I

I

G

G

I

L

S
|
S

A

G

L

L

M

I

T
|
T

T

P

T
x
S

L

L

Q

D

G

E

Q

M

R

V

D

N

V

V

I

A

E

K

L

E

L

M

K

E

E

R

E

Q

G

G

L

F

R

-

S

-

R

T

V

I

K

P

V

L

M

L

V

I

G

G

A

A

P

T

A

T

T

S

Q

K

A

A

W

H

A

T

-

A

-

V

-

K

-

I

-

E

-

Q

D

N

K

Y

I

S

G

G

A

P

D

T

C

V

Y

Y

A

V

E

Q

N

N

A
|
A

S

S

E

R

A

T

V

V

A

G

K

V

A

V

K

A

E

A

L

L

E694 (= E41) binding methylcob(III)alamin
GDVHD 756:760 (= GDVHD 101:105) binding methylcob(III)alamin
D757 (= D102) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
H759 (= H104) binding axial binding residue; mutation to G: Loss of catalytic activity.
S804 (= S149) binding methylcob(III)alamin
T808 (= T153) binding methylcob(III)alamin
S810 (≠ T155) mutation to A: Decreases activity by about 40%.
A860 (= A201) binding methylcob(III)alamin

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
247 binding Zn(2+)
310 binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
311 binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
946 binding S-adenosyl-L-methionine
1134 binding S-adenosyl-L-methionine
1189:1190 binding S-adenosyl-L-methionine

3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
38% identity, 90% coverage: 21:212/213 of query aligns to 23:221/576 of 3ivaA

query
sites
3ivaA

E

E

K

F

V

I

L

E

E

Q

A

D

V

T

E

E

K

E

A

A

R

R

A

Q

E

Q

V

A

P

T

-

R

P

P

E

C

E

E

I

V

I

I

E

E

K

G

G

P

L

L

S

M

A

D

G

G

M

M

N

N

Q

V

V

V

G

G

V

D

L

L

F

F

E

G

R

E

G

G

K

K

L

M

F

F

L

L

P

P

H

Q

V

V

M

V

M

K

A

S

A

A

D

R

A

V

M

M

T

K

T

Q

G

A

V

V

K

A

L

Y

L

L

E

E

A

P

D

F

L

I

P

E

A

A

G

S

A

K

E

E

-

Q

-

C

K

K

K

T

L

N

G

G

V

K

I

M

V

V

N

I

G

A

T

T

V

V

E

K

G

G

D
|
D

V

V

H
|
H

D

D

I

I

G
|
G

K

K

S

N

I

I

V
|
V

S

G

T

V

M

V

L

L

Q

Q

S

C

A

N

G

N

F

Y

E

E

V

I

H

V

D

D

I

L

G

G

R

V

D

M

V

V

P

P

I

A

R

E

D

K

F

I

I

L

E

R

K

T

A

A

K

K

E

E

T

V

D

N

A

A

D

D

M

L

I

I

G
|
G

I
x
L

S
|
S

A

G

L
|
L

M
x
I

T
|
T

T

P

T
x
S

L

L

Q

D

G

E

Q

M

R

V

D

N

V

V

I

A

E

K

L

E

L

M

K

E

E

R

E

Q

G

G

L

F

R

-

S

-

R

T

V

I

K

P

V

L

M

L

V

I

G
|
G

A

A

P

T

A

T

T

S

Q

K

A

A

W

H

A

T

-

A

-

V

-

K

-

I

-

E

-

Q

D

N

K

Y

I

S

G

G

A

P

D

T

C

V

Y

Y

A

V

E
x
Q

N
|
N

A

A

S

S

E

R

A

T

V

V

A

G

K

V

A

V

K

A

E

A

L

L

active site: D107 (= D102), H109 (= H104), S160 (≠ T155)
binding cobalamin: H109 (= H104), G112 (= G107), V116 (= V111), G152 (= G147), L153 (≠ I148), S154 (= S149), L156 (= L151), I157 (≠ M152), T158 (= T153), G183 (= G180), G184 (= G181), Q208 (≠ E199), N209 (= N200)

Sites not aligning to the query:

binding cobalamin: 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)
38% identity, 90% coverage: 21:212/213 of query aligns to 23:221/577 of 3bulA

query
sites
3bulA

E

E

K

F

V

I

L

E

E

Q

A

D

V

T

E

E

K

E

A

A

R

R

A

Q

E

Q

V

A

P

T

-

R

P

P

E

C

E

E

I

V

I

I

E

E

K

G

G

P

L

L

S

M

A

D

G

G

M

M

N

N

Q

V

V

V

G

G

V

D

L

L

F

F

E

G

R

E

G

G

K

K

L

M

F

F

L

L

P

P

H

Q

V

V

M

V

M

K

A

S

A

A

D

R

A

V

M

M

T

K

T

Q

G

A

V

V

K

A

L

Y

L

L

E

E

A

P

D

F

L

I

P

E

A

A

G

S

A

K

E

E

-

Q

-

C

K

K

K

T

L

N

G

G

V

K

I

M

V

V

N

I

G

A

T

T

V

V

E

K

G

G

D
|
D

V

V

H
|
H

D

D

I

I

G

G

K

K

S

N

I

I

V
|
V

S

G

T

V

M

V

L

L

Q

Q

S

C

A

N

G

N

F

Y

E

E

V

I

H

V

D

D

I

L

G

G

R

V

D

M

V

V

P

P

I

A

R

E

D

K

F

I

I

L

E

R

K

T

A

A

K

K

E

E

T

V

D

N

A

A

D

D

M

L

I

I

G
|
G

I
x
L

S
|
S

A

G

L
|
L

M
x
I

T
|
T

T

P

T
x
S

L

L

Q

D

G

E

Q

M

R

V

D

N

V

V

I

A

E

K

L

E

L

M

K

E

E

R

E

Q

G

G

L

F

R

-

S

-

R

T

V

I

K

P

V

L

M

L

V

I

G
|
G

A

A

P

T

A

T

T

S

Q

K

A

A

W

H

A

T

-

A

-

V

-

K

-

I

-

E

-

Q

D

N

K

Y

I

S

G

G

A

P

D

T

C

V

Y

Y

A

V

E
x
Q

N
|
N

A
|
A

S

S

E

R

A
x
T

V

V

A

G

K

V

A

V

K

A

E

A

L

L

active site: D107 (= D102), H109 (= H104), S160 (≠ T155)
binding cobalamin: H109 (= H104), V116 (= V111), G152 (= G147), L153 (≠ I148), S154 (= S149), L156 (= L151), I157 (≠ M152), T158 (= T153), G183 (= G180), G184 (= G181), Q208 (≠ E199), N209 (= N200), A210 (= A201), T213 (≠ A204)

Sites not aligning to the query:

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

8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
34% identity, 92% coverage: 15:211/213 of query aligns to 635:832/841 of 8g3hA

query
sites
8g3hA

V

V

I

L

S

E

C

G

K

K

K

R

E

V

K

G

V

L

L

E

E

E

A

D

V

L

E

A

K

E

A

A

R

L

A

G

E

R

V

M

P

R

P

P

E

L

E

E

I

I

E

N

K

G

G

P

L

L

S

L

A

E

G

A

M

M

N

K

Q

E

V

V

G

G

V

E

L

L

F
|
F

E

G

R

A

G

G

K

K

L

M

F

Q

L

L

P

P

H

F

V
|
V

M

L

M

Q

A

A

D

E

A

V

M

M

T
x
K

T

Q

G

A

V

V

K

A

L

Y

L

L

E

E

A

P

D

H

L

M

P

E

A

K

G

K

A

G

E

E

K

G

K

K

L

-

G

G

V

K

I

L

V

V

N

L

G

A

T

T

V

V

E

K

G
|
G

D

D

V
|
V

H
|
H

D
|
D

I
|
I

G
|
G

K

K

S

N

I

L

V
|
V

S

D

T

I

M

I

L

L

Q

T

S

N

A

N

G

G

F

Y

E

T

V

V

H

Y

D

N

I

L

G

G

R

I

D

K

V

V

P

P

I

I

R

E

D

E

F

M

I

L

E

K

K

A

A

V

K

D

E

E

T

V

D

K

A

P

D

H

M

A

I

L

G

G

I
x
M

S
|
S

A

G

L
|
L

M

L

T
x
V

T

K

T

S

L

T

Q

Q

G

V

Q

M

R

K

D

E

V

N

I

L

E

E

L

Y

L

M

K

R

E

A

E

R

G

G

L

Y

R

-

S

-

R

T

V

L

K

P

V

V

M
x
I

V
x
L

G
|
G

A
|
A

P

A

A

L

T

T

Q

R

A

A

W

Y

A

V

D

E

K

E

I

L

G

R

A

S

D

I

-

Y

-

P

-

E

-

V

C

Y

Y
|
Y

A
|
A

E
|
E

N
x
D

A

A

S

F

E

E

A

G

V

L

A

A

K

L

A

M

K

E

E

E

L

L

binding cobalamin: F675 (= F55), V685 (= V65), K693 (≠ T73), G720 (= G101), V722 (= V103), H723 (= H104), D724 (= D105), I725 (= I106), G726 (= G107), V730 (= V111), M767 (≠ I148), S768 (= S149), L770 (= L151), V772 (≠ T153), I795 (≠ M178), L796 (≠ V179), G797 (= G180), G798 (= G181), A799 (= A182), Y818 (= Y197), A819 (= A198), E820 (= E199), D821 (≠ N200)

Sites not aligning to the query:

binding cobalamin: 328, 330, 331

8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
32% identity, 96% coverage: 7:211/213 of query aligns to 2:206/507 of 8sseA

query
sites
8sseA

L

L

H

E

E

R

V

L

A

K

D

R

A

R

V

V

I

V

S

E

C

G

K

R

K

K

E

Q

K

G

V

L

L

E

E

A

A

D

V

L

E

E

K

E

A

A

-

L

R

K

A

A

E

G

V

H

P

K

P

P

E

L

E

D

I

L

I

I

E

N

K

G

G

P

L

L

S

L

A

A

G

G

M

M

N

K

Q

E

V

V

G

G

V

D

L

L

F

F

E

G

R

A

G

G

K

K

L

M

F

Q

L

L

P

P

H

F

V

V

M

L

M

Q

A

A

D

E

A

V

M

M

T

K

T

R

G

A

V

V

K

A

L

Y

L

L

E

E

A

-

D

-

L

-

P

P

A

H

G

M

A

E

E

K

K

E

K

G

L

K

G

G

V

T

I

L

V

V

N

L

G

A

T

T

V

V

E

K

G

G

D

D

V

V

H
|
H

D

D

I

I

G
|
G

K

K

S

N

I

L

V
|
V

S

D

T

I

M

I

L

L

Q

S

S

N

A

N

G

G

F

Y

E

R

V

V

H

V

D

N

I

L

G

G

R

I

D

K

V

V

P

P

I

I

R

E

D

E

F

I

I

L

E

K

K

A

A

V

K

E

E

A

T

H

D

K

A

P

D

H

M

A

I

V

G

G

I

M

S
|
S

A

G

L

L

M
x
L

T
x
V

T

K

T

S

L

T

Q

L

G

V

Q

M

R

K

D

E

V

N

I

L

E

E

L

Y

L

M

K

R

E

D

E

R

G

G

L

Y

R

-

S

-

R

T

V

L

K

P

V

V

M
x
I

V

L

G
|
G

A
|
A

P

A

A

L

T

T

Q

R

A

S

W

Y

A

V

D

E

K

E

I

L

G

R

A

A

D

I

-

Y

-

P

-

N

-

V

C

Y

Y

Y

A

A

E

E

N

D

A

A

S

F

E

E

A

G

V

L

A

R

K

L

A

M

K

E

E

E

L

L

binding cobalamin: H97 (= H104), G100 (= G107), V104 (= V111), S142 (= S149), L145 (≠ M152), V146 (≠ T153), I169 (≠ M178), G171 (= G180), G172 (= G181), A173 (= A182)

Sites not aligning to the query:

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

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)
35% identity, 82% coverage: 14:187/213 of query aligns to 678:866/1265 of Q99707

query
sites
Q99707

A

A

V

L

I

V

S

K

C

G

K

I

K

E

E

K

K

H

V

I

L

I

E

E

A

D

V

T

E

E

K

E

A

A

R

R

-

L

-

N

-

Q

A

K

E

K

V

Y

P

P

-

R

P

P

E

L

E

N

I

I

E

E

K

G

G

P

L

L

S

M

A

N

G

G

M

M

N

K

Q

I

V

V

G

G

V

D

L

L

F

F

E

G

R

A

G

G

K

K

L

M

F

F

L

L

P

P

H

Q

V

V

M

I

M

K

A

S

A

A

D

R

A

V

M

M

T

K

G

A

V

V

K

G

L

H

L

L

-

I

-

P

-

F

-

M

-

E

-

K

-

E

-

R

-

E

E

E

A

T

D

R

L

V

P

L

A

N

G

G

A

T

-

V

-

E

E

D

K

P

K

Y

L

Q

G

G

V

T

I

I

V

V

N

L

G

A

T

T

V

V

E

K

G

G

D

D

V

V

H

H

D

D

I

I

G

G

K

K

S

N

I

I

V

V

S

G

T

V

M

V

L

L

Q

G

S

C

A

N

G

N

F

F

E

R

V

V

H

I

D

D

I

L

G

G

R

V

D

M

V

T

P

P

I

C

R

D

D

K

F

I

I

L

E

K

K

A

A

A

K

L

E

D

T

H

D

K

A

A

D

D

M

I

I

I

G

G

I

L

S

S

A

G

L

L

M

I

T

T

T

P

T

S

L

L

Q

D

G

-

Q

-

R

-

D

E

V

M

I

I

E

F

L

V

L

A

K

K

E

E

-

M

E

E

G

R

L

L

R

A

S

I

R

R

V

I

K

P

V

L

M

L

V

I

G

G

A

A

P

T

A

T

T

S

Q

K

A

T

Sites not aligning to the query:

61 natural variant: R -> K
255 C → Y: in dbSNP:rs1140598
382:384 binding (6S)-5,6,7,8-tetrahydrofolate
449 binding (6S)-5,6,7,8-tetrahydrofolate
470 binding (6S)-5,6,7,8-tetrahydrofolate
537 binding (6S)-5,6,7,8-tetrahydrofolate
579 binding (6S)-5,6,7,8-tetrahydrofolate
585 binding (6S)-5,6,7,8-tetrahydrofolate
591 binding (6S)-5,6,7,8-tetrahydrofolate
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.

8t0qA Open state of lysine 5,6-aminomutase from thermoanaerobacter tengcongensis
29% identity, 49% coverage: 93:196/213 of query aligns to 111:226/257 of 8t0qA

query
sites
8t0qA

V

V

I

V

V

V

N

G

G

A

T

T

V

T

E

G

G

T

D

D

V

A

H
|
H

D

T

I
x
V

G
|
G

K

L

S

D

I

A

V
x
I

S

M

T

N

M

M

L

K

Q

G

S
x
Y

A

A

G

G

-

H

-

Y

-

G

-

L

-

E

-

R

-

Y

-

E

-

M

F

I

E

E

V

A

H

Y

D

N

I

L

G

G

R

S

D

Q

V

V

P

P

I

N

R

E

D

E

F

F

I

V

E

K

K

K

A

A

K

I

E

E

T

V

D

G

A

A

D

D

M

A

I

L

G
x
L

I

V

S
|
S

A

Q

L

T

M

V

T

T

T

Q

T

K

-

D

-

A

-

H

L

I

Q

K

G

N

Q

L

R

T

D

H

V

L

I

V

E

E

L

L

K

E

E

A

E

E

G

G

L

I

R

R

S

D

R

K

V

V

K

L

V

L

M

I

V
x
C

G
|
G

A
x
P

P

R

A

I

T

T

Q

H

A

E

W

L

A

A

D

K

K

E

I

L

G

G

A

Y

D

D

C

A

binding cobalamin: H122 (= H104), V124 (≠ I106), G125 (= G107), I129 (≠ V111), Y135 (≠ S117), L174 (≠ G147), S176 (= S149), C209 (≠ V179), G210 (= G180), G211 (= G181), P212 (≠ A182)

Sites not aligning to the query:

binding cobalamin: 228, 229, 230, 232

1xrsB Crystal structure of lysine 5,6-aminomutase in complex with plp, cobalamin, and 5'-deoxyadenosine (see paper)
30% identity, 49% coverage: 93:196/213 of query aligns to 73:188/212 of 1xrsB

query
sites
1xrsB

V

V

I

V

V

V

N

G

G

A

T

S

V

T

E

G

G

T

D
|
D

V
x
A

H
|
H

D
x
T

I
x
V

G

G

K

I

S

D

I

A

V
x
I

S

M

T

N

M

M

L
x
K

Q

G

S
x
Y

A

A

G

G

-

H

-

Y

-

G

-

L

-

E

-

R

-

Y

-

E

-

M

F

I

E

D

V

A

H

Y

D

N

I

L

G

G

R

S

D

Q

V

V

P

A

I

N

R

E

D

D

F

F

I

I

E

K

K

K

A

A

K

V

E

E

T

L

D

E

A

A

D

D

M

V

I

L

G
x
L

I
x
V

S
|
S

A

Q

L

T

M

V

T
|
T

T

Q

T

K

-

N

-

V

-

H

L

I

Q

Q

G

N

Q

M

R

T

D

H

V

L

I

I

E

E

L

L

K

E

E

A

E

E

G

G

L

L

R

R

S

D

R

R

V

F

K

V

V

L

M
x
L

V
x
C

G
|
G

A
x
P

P

R

A

I

T

N

Q

N

A

E

W

I

A

A

D

K

K

E

I

L

G

G

A

Y

D

D

C

A

active site: K95 (≠ L115)
binding cobalamin: D82 (= D102), A83 (≠ V103), H84 (= H104), T85 (≠ D105), V86 (≠ I106), I91 (≠ V111), Y97 (≠ S117), L136 (≠ G147), V137 (≠ I148), S138 (= S149), T142 (= T153), L170 (≠ M178), C171 (≠ V179), G172 (= G180), G173 (= G181), P174 (≠ A182)

Sites not aligning to the query:

binding cobalamin: 190, 191, 192, 194

E3PRJ4 Lysine 5,6-aminomutase beta subunit; 5,6-LAM; D-lysine 5,6-aminomutase beta subunit; L-beta-lysine 5,6-aminomutase beta subunit; EC 5.4.3.3 from Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) (see paper)
30% identity, 49% coverage: 93:196/213 of query aligns to 122:237/262 of E3PRJ4

query
sites
E3PRJ4

V

V

I

V

V

V

N

G

G

A

T

S

V

T

E

G

G
x
T

D
|
D

V
x
A

H
|
H

D
x
T

I
x
V

G
|
G

K

I

S

D

I

A

V

I

S

M

T

N

M

M

L
x
K

Q

G

S

Y

A

A

G

G

-

H

-

Y

-

G

-

L

-

E

-

R

-

Y

-

E

-

M

F

I

E

D

V

A

H

Y

D

N

I

L

G

G

R

S

D

Q

V

V

P

A

I

N

R

E

D

D

F

F

I

I

E

K

K

K

A

A

K

V

E

E

T

L

D

E

A

A

D

D

M

V

I

L

G
x
L

I
x
V

S
|
S

A
x
Q

L
x
T

M
x
V

T
|
T

T
x
Q

T

K

-

N

-

V

-

H

L

I

Q

Q

G

N

Q

M

R

T

D

H

V

L

I

I

E

E

L

L

K

E

E

A

E

E

G

G

L

L

R

R

S

D

R

R

V

F

K

V

V

L

M
x
L

V
x
C

G
|
G

A
x
P

P

R

A

I

T

N

Q

N

A

E

W

I

A

A

D

K

K

E

I

L

G

G

A

Y

D

D

C

A

130:136 (vs. 101:107, 43% identical) binding adenosylcob(III)alamin
K144 (≠ L115) modified: N6-(pyridoxal phosphate)lysine
185:192 (vs. 147:154, 25% identical) binding adenosylcob(III)alamin
LCGGP 219:223 (≠ MVGGA 178:182) binding adenosylcob(III)alamin

Sites not aligning to the query:

239:244 binding adenosylcob(III)alamin

1id8A Nmr structure of glutamate mutase (b12-binding subunit) complexed with the vitamin b12 nucleotide (see paper)
38% identity, 48% coverage: 88:190/213 of query aligns to 2:103/137 of 1id8A

query
sites
1id8A

E

E

K

K

L

-

G

-

V

T

I

I

V

V

N

L

G

G

T
x
V

V

I

E

G

G

S

D
|
D

V

C

H
|
H

D

A

I

V

G

G

K

N

S

K

I

I

V

L

S

D

T

H

M

S

L

F

Q

T

S

N

A

A

G

G

F

F

E

N

V

V

H

V

D

N

I

I

G

G

R

V

D

L

V

S

P

S

I

Q

R

E

D

D

F

F

I

I

E

N

K

A

A

A

K

I

E

E

T

T

D

K

A

A

D

D

M

L

I

I

G

C

I

V

S
|
S

A

S

L
|
L

M

Y

T

G

T

-

L

-

Q

Q

G

G

Q

E

R

I

D

D

-

C

-

K

-

G

V

L

I

R

E

E

L

K

L

C

K

D

E

E

E

A

G

G

L

L

R

K

S

G

R

-

V

I

K

K

V

L

M

F

V

V

G
|
G

G

G

-

N

-

I

A

V

P

V

A

G

T

K

Q

Q

A

N

W

W

A

P

D

D

active site: V10 (≠ T98), D14 (= D102), H16 (= H104)
binding phosphoric acid mono-[5-(5,6-dimethyl-benzoimidazol-1-yl)-4-hydroxy-2-hydroxymethyl-tetrahydro-furan-3-yl] ester: S61 (= S149), L63 (= L151), G91 (= G180)

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: 117, 119, 121

8j2yA Acidimicrobiaceae bacterium photocobilins protein, dark state (see paper)
26% identity, 80% coverage: 11:181/213 of query aligns to 11:175/327 of 8j2yA

query
sites
8j2yA

V

L

A

G

D

D

A

A

V

I

I

V

S

G

C

N

K

R

E

P

K

A

V

V

L

R

E

L

A

T

V

L

E

D

K

L

A

L

R

D

A

H

E

R

V

V

P

P

P

E

E

A

E

D

I

I

I

V

E

E

K

D

G

L

L

L

S
x
A

A

A

G

A

M
x
Q

N
x
R

Q

E

V

V

G

G

V

E

L

R

F

W

E

Y

R

R

G

N

K

E

L

L

F

S

L

P

P

A

H

D

V
x
E

M

H

M

L

A

A

A

S

D

G

A

V

M

A

T

G

T

A

G

A

V

L

K

D

L

A

L

L

E

A

A

A

D

E

L

L

P

P

A

P

G

-

A

-

E

P

K

T

K

R

L

D

G

G

V

L

I

V

V

V

N

V

G

A

T

C

V

A

E

E

G

G

D
|
D

V
x
W

H
|
H

D

S

I
x
L

G
x
S

K

A

S

Q

I
x
M

V
x
F

S

G

T

E

M

T

L

L

Q

R

S

A

A

S

G

G

F

F

E

D

V

V

H

S

D

V

I

L

G

G

R

A

D

S

V

T

P

P

-

R

-

T

-

A

I

V

R

V

D

D

F

F

I

L

E

T

K

R

A

A

K

G

E

-

T

-

D

-

A

G

D

D

M

S

I

L

G

A

I

V

S
|
S

A

C

L

N

M

M

T

P

T

I

T
x
F

L

F

Q

P

G

G

Q

V

R

A

D

Q

V

L

I

I

E

N

L

A

K

H

E

E

E

I

G

G

L

-

R

-

S

-

R

-

V

V

K

P

V

V

M

I

V
|
V

G
|
G

binding cobalamin: A45 (≠ S45), Q48 (≠ M48), R49 (≠ N49), E65 (≠ V65), D100 (= D102), W101 (≠ V103), H102 (= H104), L104 (≠ I106), S105 (≠ G107), M108 (≠ I110), F109 (≠ V111), S147 (= S149), F153 (≠ T155), V173 (= V179), G174 (= G180), G175 (= G181)

Sites not aligning to the query:

binding cobalamin: 176, 286

1i9cA Glutamate mutase from clostridium cochlearium: complex with adenosylcobalamin and substrate (see paper)
37% identity, 48% coverage: 88:190/213 of query aligns to 2:103/137 of 1i9cA

query
sites
1i9cA

E

E

K

K

L

-

G

-

V

T

I

I

V

V

N

L

G

G

T
x
V

V

I

E

G

G
x
S

D
|
D

V
x
C

H
|
H

D
x
A

I

V

G
|
G

K

N

S

K

I

I

V
x
L

S

D

T

H

M

A

L

F

Q

T

S

N

A

A

G

G

F

F

E

N

V

V

H

V

D

N

I

I

G

G

R

V

D

L

V

S

P

P

I

Q

R

E

D

N

F

F

I

I

E

K

K

A

A

A

K

I

E

E

T

T

D

K

A

A

D

D

M

A

I

I

G

L

I

V

S
|
S

A

S

L
|
L

M
x
Y

T
x
G

T

-

L

-

Q

Q

G

G

Q

E

R

I

D

D

V

C

I

K

E

G

L

L

L

R

K

Q

-

K

-

C

-

D

E

E

E

A

G

G

L

L

R

E

S

G

R

-

V

I

K

L

V

L

M

Y

V

V

G
|
G

-
x
N

-

I

A
x
V

P
x
V

A

G

T

K

Q

Q

A

H

W

W

A

P

D

D

active site: V10 (≠ T98), D14 (= D102), H16 (= H104)
binding cobalamin: S13 (≠ G101), D14 (= D102), C15 (≠ V103), H16 (= H104), A17 (≠ D105), G19 (= G107), L23 (≠ V111), S61 (= S149), L63 (= L151), Y64 (≠ M152), G65 (≠ T153), G91 (= G180), G92 (= G181), N93 (vs. gap), V95 (≠ A182), V96 (≠ P183)

Sites not aligning to the query:

binding cobalamin: 121

1ccwA Structure of the coenzyme b12 dependent enzyme glutamate mutase from clostridium cochlearium (see paper)
37% identity, 48% coverage: 88:190/213 of query aligns to 2:103/137 of 1ccwA

query
sites
1ccwA

E

E

K

K

L

-

G

-

V

T

I

I

V

V

N

L

G

G

T
x
V

V

I

E

G

G

S

D
|
D

V
x
C

H
|
H

D
x
A

I

V

G
|
G

K

N

S

K

I
|
I

V

L

S

D

T

H

M

A

L

F

Q

T

S

N

A

A

G

G

F

F

E

N

V

V

H

V

D

N

I

I

G

G

R

V

D

L

V

S

P

P

I

Q

R

E

D

L

F

F

I

I

E

K

K

A

A

A

K

I

E

E

T

T

D

K

A

A

D

D

M

A

I

I

G

L

I

V

S
|
S

A

S

L
|
L

M
x
Y

T
x
G

T

-

L

-

Q

Q

G

G

Q

E

R

I

D

D

V

C

I

K

E

G

L

L

L

R

K

Q

-

K

-

C

-

D

E

E

E

A

G

G

L

L

R

E

S

G

R

-

V

I

K

L

V

L

M

Y

V

V

G
|
G

-
x
N

-

I

A
x
V

P

V

A

G

T

K

Q

Q

A

H

W

W

A

P

D

D

active site: V10 (≠ T98), D14 (= D102), H16 (= H104)
binding cyanocobalamin: D14 (= D102), C15 (≠ V103), H16 (= H104), A17 (≠ D105), G19 (= G107), I22 (= I110), S61 (= S149), L63 (= L151), Y64 (≠ M152), G65 (≠ T153), G91 (= G180), G92 (= G181), N93 (vs. gap), V95 (≠ A182)

Sites not aligning to the query:

binding cyanocobalamin: 117, 121, 123

Query Sequence

>WP_011022395.1 NCBI__GCF_000007345.1:WP_011022395.1
MADIEGLLHEVADAVISCKKEKVLEAVEKARAEVPPEEIIEKGLSAGMNQVGVLFERGKL
FLPHVMMAADAMTTGVKLLEADLPAGAEKKLGVIVNGTVEGDVHDIGKSIVSTMLQSAGF
EVHDIGRDVPIRDFIEKAKETDADMIGISALMTTTLQGQRDVIELLKEEGLRSRVKVMVG
GAPATQAWADKIGADCYAENASEAVAKAKELLL

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