SitesBLAST

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)
24% identity, 91% coverage: 1:197/216 of query aligns to 663:862/1227 of P13009

query
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P13009

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E694 (= E36) binding methylcob(III)alamin
GDVHD 756:760 (≠ GDIHD 95:99) binding methylcob(III)alamin
D757 (= D96) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
H759 (= H98) binding axial binding residue; mutation to G: Loss of catalytic activity.
S804 (= S143) binding methylcob(III)alamin
T808 (≠ S147) binding methylcob(III)alamin
S810 (≠ C149) mutation to A: Decreases activity by about 40%.
A860 (≠ I195) 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

1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
25% identity, 85% coverage: 22:205/216 of query aligns to 30:220/246 of 1bmtA

query
sites
1bmtA

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active site: D107 (= D96), H109 (= H98), S160 (≠ C149)
binding co-methylcobalamin: E44 (= E36), M48 (≠ Q39), M51 (≠ V42), G55 (= G46), L65 (= L56), V68 (≠ L59), D107 (= D96), V108 (≠ I97), H109 (= H98), D110 (= D99), I111 (≠ L100), I115 (= I104), G152 (= G141), L153 (≠ I142), S154 (= S143), L156 (= L145), I157 (≠ L146), T158 (≠ S147), G183 (= G174), G184 (= G175), A185 (≠ Y176), V207 (≠ T192), N209 (≠ D194), A210 (≠ I195)

3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
25% identity, 82% coverage: 21:197/216 of query aligns to 29:212/576 of 3ivaA

query
sites
3ivaA

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active site: D107 (= D96), H109 (= H98), S160 (≠ C149)
binding cobalamin: H109 (= H98), G112 (= G101), V116 (≠ I105), G152 (= G141), L153 (≠ I142), S154 (= S143), L156 (= L145), I157 (≠ L146), T158 (≠ S147), G183 (= G174), G184 (= G175), Q208 (≠ N193), N209 (≠ D194)

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)
25% identity, 82% coverage: 21:197/216 of query aligns to 29:212/577 of 3bulA

query
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3bulA

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active site: D107 (= D96), H109 (= H98), S160 (≠ C149)
binding cobalamin: H109 (= H98), V116 (≠ I105), G152 (= G141), L153 (≠ I142), S154 (= S143), L156 (= L145), I157 (≠ L146), T158 (≠ S147), G183 (= G174), G184 (= G175), Q208 (≠ N193), N209 (≠ D194), A210 (≠ I195)

Sites not aligning to the query:

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

2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
28% identity, 81% coverage: 5:180/216 of query aligns to 43:216/258 of 2i2xB

query
sites
2i2xB

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active site: D134 (= D96), H136 (= H98), T187 (≠ C149)
binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G95), D134 (= D96), V135 (≠ I97), H136 (= H98), D137 (= D99), I138 (≠ L100), G139 (= G101), V143 (≠ I105), T179 (≠ G141), T181 (≠ S143), L183 (= L145), M184 (≠ L146), T185 (≠ S147), A208 (≠ I172), G210 (= G174), G211 (= G175), G212 (≠ Y176)

Sites not aligning to the query:

binding 5-hydroxybenzimidazolylcob(iii)amide: 228, 229, 230, 231

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)
28% identity, 81% coverage: 5:180/216 of query aligns to 43:216/258 of Q46EH4

query
sites
Q46EH4

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T

E

K

K

A

P

P

I

V

M

L

L

G

T

I

G

S

T

V

A

L

L

L

M

S

T

F

T

C

T

V

M

S

Y

A

A

V

F

K

K

K

E

V

V

V

N

D

D

L

M

L

L

V

L

E

E

S

N

G

G

L

I

R

K

D

-

Q

-

V

I

K

P

I

F

I

A

V

C

G

G

Y

G

P

A

V

V

N

N

E

Q

H129 (≠ G91) mutation to K: Does not affect cobalamin-binding.
H136 (= H98) mutation H->G,K: Abolishes cobalamin-binding.

Sites not aligning to the query:

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

8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8 (see paper)
29% identity, 91% coverage: 21:216/216 of query aligns to 22:216/507 of 8sseA

query
sites
8sseA

V

L

K

E

E

E

Y

A

L

L

S

K

K

A

G

G

V

H

S

K

P

P

L

L

K

D

V

L

V

I

E

N

-

G

L

P

C

L

Q

L

Q

A

G

G

V

M

E

K

V

E

V

V

G

G

K

D

R

L

Y

F

C

G

N

A

G

G

E

K

Y

M

Y

Q

L

L

S

P

D

F

L

V

I

L

M

Q

S

A

E

A

E

E

I

V

L

M

K

K

E

R

V

A

M

V

V

A

I

Y

L

L

E

E

P

P

L

H

I

M

T

E

S

K

D

E

I

-

P

-

S

G

N

K

G

G

M

-

T

T

I

L

I

V

L

L

G

A

T

T

I

V

E

K

G

G

D

D

I

V

H
|
H

D

D

L

I

G
|
G

K

K

N

N

I

L

I
x
V

H

D

Y

I

M

I

L

L

K

S

S

N

G

G

F

Y

K

R

V

V

D

N

L

L

G

G

V

I

D

K

V

V

S

P

P

I

E

E

T

E

F

I

V

L

Q

K

A

A

V

V

N

E

Q

A

T

H

K

K

A

P

P

H

V

A

L

V

G

G

I

M

S
|
S

V

G

L

L

L
|
L

S
x
V

F

K

C

S

V

T

S

L

A

V

V

M

K

K

K

E

V

N

V

L

D

E

L

Y

L

M

V

R

E

D

S

R

G

G

L

Y

R

-

D

-

Q

T

V

L

K

P

I

V

I
|
I

V

L

G
|
G

Y
x
A

P

A

-

L

-

T

-

R

-

S

-

Y

V

V

N

E

E

E

I

L

V

R

K

A

D

I

Y

Y

T

P

G

N

V

V

D

-

Y

Y

T

A

N

E

D

D

I

A

T

F

K

E

L

G

F

L

E

R

I

L

C

M

Q

E

M

E

L

L

K

T

D

G

E

H

L

A

P

P

I

-

P

P

E

E

E

L

T

T

S

R

binding cobalamin: H97 (= H98), G100 (= G101), V104 (≠ I105), S142 (= S143), L145 (= L146), V146 (≠ S147), I169 (= I172), G171 (= G174), G172 (= G175), A173 (≠ Y176)

Sites not aligning to the query:

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

8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
26% identity, 91% coverage: 14:210/216 of query aligns to 637:837/841 of 8g3hA

query
sites
8g3hA

E

E

E

G

K

K

T

R

I

V

N

G

L

L

V

-

K

E

E

E

Y

D

L

L

S

A

K

E

G

A

V

L

S

G

P

R

L

M

K

R

V

P

V

L

E

E

L

I

C

I

Q

N

-

G

-

P

-

L

Q

E

G

A

V

M

E

K

V

E

V

V

G

G

K

E

R

L

Y
x
F

C

G

N

A

G

G

E

K

Y

M

Y

Q

L

L

S

P

D

F

L
x
V

I

L

M

Q

S

A

E

A

E

E

I

V

L

M

K
|
K

E

Q

V

A

M

V

V

A

I

Y

L

L

E

E

P

P

L

H

I

M

T

E

S

K

D

K

I

G

P

E

S

G

N

K

G

G

M

-

T

K

I

L

I

V

L

L

G

A

T

T

I

V

E

K

G
|
G

D

D

I
x
V

H
|
H

D
|
D

L
x
I

G
|
G

K

K

N

N

I

L

I
x
V

H

D

Y

I

M

I

L

L

K

T

S

N

G

G

F

Y

K

T

V

V

V

Y

D

N

L

L

G

G

V

I

D

K

V

V

S

P

P

I

E

E

T

E

F

M

V

L

Q

K

A

A

V

V

N

D

Q

E

T

V

K

K

A

P

P

H

V

A

L

L

G

G

I
x
M

S
|
S

V

G

L
|
L

L

L

S
x
V

F

K

C

S

V

T

S

Q

A

V

V

M

K

K

K

E

V

N

V

L

D

E

L

Y

L

M

V

R

E

A

S

R

G

G

L

Y

R

-

D

-

Q

T

V

L

K

P

I

V

I
|
I

V
x
L

G
|
G

Y
x
A

P

A

-

L

-

T

-

R

-

A

-

Y

V

V

N

E

E

E

I

L

V

R

K

S

D

I

Y

Y

T

P

G

E

V

V

D

-

Y

Y

Y
|
Y

T
x
A

N
x
E

D
|
D

I

A

T

F

K

E

L

G

F

L

E

A

I

L

C

M

Q

E

M

E

L

L

K

T

D

G

E

H

L

R

P

P

binding cobalamin: F675 (≠ Y49), V685 (≠ L59), K693 (= K67), G720 (= G95), V722 (≠ I97), H723 (= H98), D724 (= D99), I725 (≠ L100), G726 (= G101), V730 (≠ I105), M767 (≠ I142), S768 (= S143), L770 (= L145), V772 (≠ S147), I795 (= I172), L796 (≠ V173), G797 (= G174), G798 (= G175), A799 (≠ Y176), Y818 (= Y191), A819 (≠ T192), E820 (≠ N193), D821 (= D194)

Sites not aligning to the query:

binding cobalamin: 328, 330, 331

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)
26% identity, 82% coverage: 31:208/216 of query aligns to 704:899/1265 of Q99707

query
sites
Q99707

P

P

L

L

K

N

V

I

E

E

-

G

L

P

C

L

Q

M

Q

N

G

G

V

M

E

K

V

I

V

V

G

G

K

D

R

L

Y

F

C

G

N

A

G

G

E

K

Y

M

Y

F

L

L

S

P

D

Q

L

V

I

I

M

K

S

S

E

A

E

R

I

V

L

M

K

K

E

K

V

A

M

V

V

G

I

H

L

L

E

I

P

P

L

F

-

M

-

E

-

K

-

E

-

R

-

E

-

T

-

R

-

V

-

L

-

N

-

G

-

T

I

V

T

E

S

E

D

E

I

D

P

P

S

Y

N

Q

G

G

M

-

T

T

I

I

I

V

L

L

G

A

T

T

I

V

E

K

G

G

D

D

I

V

H

H

D

D

L

I

G

G

K

K

N

N

I

I

I

V

H

G

Y

V

M

V

L

L

K

G

S

C

S

N

G

N

F

F

K

R

V

V

V

I

D

D

L

L

G

G

V

V

D

M

V

T

S

P

P

C

E

D

T

K

F

I

V

L

Q

K

A

A

V

A

N

L

Q

D

T

H

K

K

A

A

P

D

V

I

L

I

G

G

I

L

S

S

V

G

L

L

L

I

S

T

F

P

C

S

V

L

S

D

A

E

V

M

K

I

K

F

V

V

V

A

D

K

L

E

L

M

V

E

E

R

S

L

G

A

L

I

R

R

D

-

Q

-

V

I

K

P

I

L

V

I

G

G

Y

A

P

T

V

T

N

S

-

K

-

T

-

H

-

T

-

A

-

V

E

K

I

I

V

A

K

P

D

R

Y

Y

T

S

G

A

V

P

D

V

Y

I

Y

H

T

V

N

L

D

D

I

A

T

S

K

K

L

S

F

V

E

V

I

V

C

C

Q

S

M

Q

L

L

K

L

D

D

E

E

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.

1id8A Nmr structure of glutamate mutase (b12-binding subunit) complexed with the vitamin b12 nucleotide (see paper)
36% identity, 41% coverage: 87:175/216 of query aligns to 5:92/137 of 1id8A

query
sites
1id8A

T

T

I

I

I

V

L

L

G

G

T
x
V

I

I

E

G

G

S

D
|
D

I

C

H
|
H

D

A

L

V

G

G

K

N

N

K

I

I

I

L

H

D

Y

H

M

S

L

F

K

T

S

N

S

A

G

G

F

F

K

N

V

V

D

N

L

I

G

G

V

V

D

L

V

S

S

S

P

Q

E

E

T

D

F

F

V

I

Q

N

A

A

V

A

N

I

Q

E

T

T

K

K

A

A

P

D

V

L

L

I

G

C

I

V

S
|
S

V

S

L
|
L

L

Y

S

G

F

Q

C

G

V

E

S

I

A

D

V

C

K

K

K

G

V

L

V

R

D

E

L

K

L

C

V

D

E

E

S

A

G

G

L

L

R

K

D

G

Q

-

V

I

K

K

I

L

I

F

V

V

G
|
G

G

G

active site: V10 (≠ T92), D14 (= D96), H16 (= H98)
binding phosphoric acid mono-[5-(5,6-dimethyl-benzoimidazol-1-yl)-4-hydroxy-2-hydroxymethyl-tetrahydro-furan-3-yl] ester: S61 (= S143), L63 (= L145), G91 (= G174)

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

Q59268 2-methyleneglutarate mutase; Alpha-methyleneglutarate mutase; EC 5.4.99.4 from Eubacterium barkeri (Clostridium barkeri) (see paper)
31% identity, 44% coverage: 82:175/216 of query aligns to 469:562/614 of Q59268

query
sites
Q59268

P

P

S

T

N

R

G

P

M

E

T

K

I

I

I

V

L

L

G

A

T

T

I

V

E

G

G

A

D
|
D

I

A

H
|
H

D

V

L

N

G

G

K

I

N

N

I

V

I

I

H

R

Y

E

M

A

L

F

K

Q

S

D

S

A

G

G

F

Y

K

D

V

V

D

Y

L

L

G

R

V

G

D

M

V

N

S

L

P

P

E

E

T

S

F

V

V

A

Q

E

A

V

V

A

N

A

Q

E

T

V

K

G

A

A

P

D

V

A

L

V

G

G

I

V

S

S

V

N

L

L

S

G

F

L

C

G

V

M

S

E

A

L

V

F

K

P

K

R

V

V

V

S

D

K

L

R

L

L

V

E

E

E

S

L

G

G

L

L

R

R

D

D

Q

K

V

M

K

V

I

V

I

C

V

A

G

G

D483 (= D96) mutation to N: Activity reduced 2000-fold.
H485 (= H98) mutation to Q: Loss of activity.

Sites not aligning to the query:

464 H→Q: No effect on activity.

1i9cA Glutamate mutase from clostridium cochlearium: complex with adenosylcobalamin and substrate (see paper)
39% identity, 27% coverage: 87:145/216 of query aligns to 5:63/137 of 1i9cA

query
sites
1i9cA

T

T

I

I

I

V

L

L

G

G

T
x
V

I

I

E

G

G
x
S

D
|
D

I
x
C

H
|
H

D
x
A

L

V

G
|
G

K

N

N

K

I

I

I
x
L

H

D

Y

H

M

A

L

F

K

T

S

N

S

A

G

G

F

F

K

N

V

V

D

N

L

I

G

G

V

V

D

L

V

S

S

P

P

Q

E

E

T

N

F

F

V

I

Q

K

A

A

V

A

N

I

Q

E

T

T

K

K

A

A

P

D

V

A

L

I

G

L

I

V

S
|
S

V

S

L
|
L

active site: V10 (≠ T92), D14 (= D96), H16 (= H98)
binding cobalamin: S13 (≠ G95), D14 (= D96), C15 (≠ I97), H16 (= H98), A17 (≠ D99), G19 (= G101), L23 (≠ I105), S61 (= S143), L63 (= L145)

Sites not aligning to the query:

binding cobalamin: 64, 65, 91, 92, 93, 95, 96, 121

E3PY95 D-ornithine 4,5-aminomutase subunit beta; D-ornithine aminomutase E component; OAM-E; EC 5.4.3.5 from Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii) (see 2 papers)
31% identity, 60% coverage: 60:189/216 of query aligns to 577:713/740 of E3PY95

query
sites
E3PY95

I

I

M

N

S

S

E

L

E

V

I

I

L

P

K

P

E

E

V

P

M

E

V

I

I

L

L

S

E

E

P

D

L

E

I

I

T

R

S

E

D

D

I

I

P

E

S

K

N

T

G

P

M

L

T

K

I

I

I

V

L

A

G

A

T

T

I

V

E

G

G

E

D

D

I
x
E

H
|
H

D
x
S

L

V

G

G

K

L

-

R

-

E

-

V

-

I

N

D

I

I

I
x
K

H

H

Y

G

M

G

L

I

K

E

S

K

S

Y

G

G

F

V

K

E

V

V

V

H

D

Y

L

L

G

G

V

T

D

S

V

V

S

P

P

V

E

E

T

K

F

L

V

V

Q

D

A

A

V

A

N

I

Q

E

T

L

K

K

A

A

P

D

V

A

L

I

G

L

I

A

S
|
S

V
x
T

L
x
I

S
|
S

-
x
H

-

D

F

I

C

H

V

Y

S

K

A

N

V

M

K

K

K

R

V

I

V

H

D

E

L

L

L

A

V

V

E

E

S

K

G

G

L

I

R

R

D

D

Q

K

V

I

K

M

I

I

I

G

V

C

G

G

Y

T

P

Q

V

V

N

T

E

P

I

E

V

V

K

A

D

V

Y

K

T

Q

G

G

V

V

D

D

EHS 614:616 (≠ IHD 97:99) binding adenosylcob(III)alamin
H615 (= H98) binding axial binding residue; mutation to G: Loss of corrinoid-binding ability.
K626 (≠ I105) modified: N6-(pyridoxal phosphate)lysine
STIISH 664:669 (≠ SVLLS- 143:147) binding adenosylcob(III)alamin

Sites not aligning to the query:

81 binding substrate
182 binding substrate

3koyA Crystal structure of ornithine 4,5 aminomutase in complex with ornithine (aerobic) (see paper)
30% identity, 55% coverage: 71:189/216 of query aligns to 579:704/728 of 3koyA

query
sites
3koyA

V

I

I

L

L

S

E

E

P

D

L

E

I

I

T

R

S

E

D

D

I

I

P

E

S

K

N

T

G

P

M

L

T

K

I

I

I

V

L

A

G

A

T

T

I

V

E

G

G

E

D

D

I
x
E

H
|
H

D
x
S

L
x
V

G

G

K

L

-

R

-

E

-
x
V

-

I

N

D

I

I

I
x
K

H

H

Y

G

M

G

L

I

K

E

S

K

S

Y

G

G

F

V

K

E

V

V

V

H

D

Y

L

L

G

G

V

T

D

S

V

V

S

P

P

V

E

E

T

K

F

L

V

V

Q

D

A

A

V

A

N

I

Q

E

T

L

K

K

A

A

P

D

V

A

L

I

G

L

I

A

S
|
S

V

T

L

I

L
x
I

S
|
S

-

H

-

D

F

I

C

H

V

Y

S

K

A

N

V

M

K

K

K

R

V

I

V

H

D

E

L

L

L

A

V

V

E

E

S

K

G

G

L

I

R

R

D

D

Q

K

V

I

K

M

I

I

I

G

V

C

G
|
G

Y
x
T

P

Q

V

V

N

T

E

P

I

E

V

V

K

A

D

V

Y

K

T

Q

G

G

V

V

D

D

active site: K617 (≠ I105)
binding cobalamin: E605 (≠ I97), H606 (= H98), S607 (≠ D99), V608 (≠ L100), V613 (vs. gap), S655 (= S143), I658 (≠ L146), S659 (= S147), G689 (= G174), G690 (= G175), T691 (≠ Y176)

Sites not aligning to the query:

active site: 183, 218, 290
binding cobalamin: 112, 483, 707, 710, 711
binding (E)-N~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-ornithine: 77, 105, 109, 110, 156, 158, 178, 183, 188, 218, 219, 290, 292

3koxA Crystal structure of ornithine 4,5 aminomutase in complex with 2,4- diaminobutyrate (anaerobic) (see paper)
30% identity, 55% coverage: 71:189/216 of query aligns to 579:704/728 of 3koxA

query
sites
3koxA

V

I

I

L

L

S

E

E

P

D

L

E

I

I

T

R

S

E

D

D

I

I

P

E

S

K

N

T

G

P

M

L

T

K

I

I

I

V

L

A

G

A

T

T

I

V

E

G

G

E

D

D

I
x
E

H
|
H

D
x
S

L
x
V

G
|
G

K

L

-

R

-

E

-

V

-

I

N

D

I

I

I
x
K

H

H

Y

G

M

G

L

I

K

E

S

K

S

Y

G

G

F

V

K

E

V

V

V

H

D

Y

L

L

G

G

V

T

D

S

V

V

S

P

P

V

E

E

T

K

F

L

V

V

Q

D

A

A

V

A

N

I

Q

E

T

L

K

K

A

A

P

D

V

A

L

I

G

L

I
x
A

S
|
S

V

T

L
x
I

L

I

S
|
S

-

H

-

D

F

I

C

H

V

Y

S

K

A

N

V

M

K

K

K

R

V

I

V

H

D

E

L

L

L

A

V

V

E

E

S

K

G

G

L

I

R

R

D

D

Q

K

V

I

K

M

I

I

I

G

V

C

G
|
G

Y
x
T

P

Q

V

V

N

T

E

P

I

E

V

V

K

A

D

V

Y

K

T

Q

G

G

V

V

D

D

active site: K617 (≠ I105)
binding cobalamin: E605 (≠ I97), H606 (= H98), S607 (≠ D99), V608 (≠ L100), G609 (= G101), A654 (≠ I142), S655 (= S143), I657 (≠ L145), S659 (= S147), G689 (= G174), G690 (= G175), T691 (≠ Y176)

Sites not aligning to the query:

active site: 183, 218, 290
binding cobalamin: 112, 483, 707, 708, 710, 711
binding (2S)-2-amino-4-{[(1Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}butanoic acid: 77, 105, 108, 110, 156, 158, 183, 188, 218, 219, 290

3kowB Crystal structure of ornithine 4,5 aminomutase backsoaked complex (see paper)
30% identity, 55% coverage: 71:189/216 of query aligns to 579:704/728 of 3kowB

query
sites
3kowB

V

I

I

L

L

S

E

E

P

D

L

E

I

I

T

R

S

E

D

D

I

I

P

E

S

K

N

T

G

P

M

L

T

K

I

I

I

V

L

A

G

A

T

T

I

V

E

G

G

E

D

D

I
x
E

H
|
H

D
x
S

L
x
V

G
|
G

K
x
L

-

R

-

E

-

V

-

I

N

D

I

I

I
x
K

H

H

Y

G

M

G

L

I

K

E

S

K

S

Y

G

G

F

V

K

E

V

V

V

H

D

Y

L

L

G

G

V

T

D

S

V

V

S

P

P

V

E

E

T

K

F

L

V

V

Q

D

A

A

V

A

N

I

Q

E

T

L

K

K

A

A

P

D

V

A

L

I

G

L

I

A

S

S

V

T

L
x
I

L

I

S

S

-

H

-

D

F

I

C

H

V

Y

S

K

A

N

V

M

K

K

K

R

V

I

V

H

D

E

L

L

L

A

V

V

E

E

S

K

G

G

L

I

R

R

D

D

Q

K

V

I

K

M

I

I

I

G

V

C

G
|
G

Y
x
T

P

Q

V

V

N

T

E

P

I

E

V

V

K

A

D

V

Y

K

T

Q

G

G

V

V

D

D

active site: K617 (≠ I105)
binding cobalamin: E605 (≠ I97), H606 (= H98), S607 (≠ D99), V608 (≠ L100), G609 (= G101), L610 (≠ K102), I657 (≠ L145), G689 (= G174), G690 (= G175), T691 (≠ Y176)

Sites not aligning to the query:

active site: 183, 218, 290
binding cobalamin: 707, 711
binding pyridoxal-5'-phosphate: 105, 110, 156, 158, 178, 183, 188, 218, 219

Query Sequence

>WP_015944299.1 NCBI__GCF_000021925.1:WP_015944299.1
MDDQLLNALADLDEEKTINLVKEYLSKGVSPLKVVELCQQGVEVVGKRYCNGEYYLSDLI
MSEEILKEVMVILEPLITSDIPSNGMTIILGTIEGDIHDLGKNIIHYMLKSSGFKVVDLG
VDVSPETFVQAVNQTKAPVLGISVLLSFCVSAVKKVVDLLVESGLRDQVKIIVGGYPVNE
IVKDYTGVDYYTNDITKLFEICQMLKDELPIPEETS

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