SitesBLAST

4djfA Crystal structure of folate-bound corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr), co-crystallized with folate and ti(iii) citrate reductant (see paper)
31% identity, 82% coverage: 23:283/320 of query aligns to 3:260/262 of 4djfA

query
sites
4djfA

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binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E26), M11 (≠ T31), F12 (vs. gap), D75 (= D100), N96 (= N121), D160 (= D185), S198 (= S221), N199 (= N222), R207 (= R230)
binding calcium ion: G222 (= G245), D224 (≠ T247)
binding co-methylcobalamin: V168 (≠ A193), Q202 (≠ F225), N203 (≠ G226)

4djeA Crystal structure of folate-bound corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr), co-crystallized with folate (see paper)
31% identity, 82% coverage: 23:283/320 of query aligns to 3:260/262 of 4djeA

query
sites
4djeA

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binding cobalamin: V168 (≠ A193), N203 (≠ G226)
binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E26), M11 (≠ T31), F12 (vs. gap), D75 (= D100), N96 (= N121), D160 (= D185), G196 (= G219), S198 (= S221), N199 (= N222), R207 (= R230)
binding calcium ion: G222 (= G245), D224 (≠ T247)

4djdA Crystal structure of folate-free corrinoid iron-sulfur protein (cfesp) in complex with its methyltransferase (metr) (see paper)
31% identity, 82% coverage: 23:283/320 of query aligns to 3:260/262 of 4djdA

query
sites
4djdA

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binding calcium ion: G222 (= G245), D224 (≠ T247)

2e7fA 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.2 angsrom resolution (see paper)
31% identity, 82% coverage: 23:283/320 of query aligns to 3:260/262 of 2e7fA

query
sites
2e7fA

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binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E6 (= E26), M11 (≠ T31), F12 (vs. gap), D75 (= D100), N96 (= N121), D160 (= D185), G196 (= G219), S198 (= S221), N199 (= N222), Q202 (≠ F225), R207 (= R230), I227 (= I250)
binding calcium ion: G222 (= G245), D224 (≠ T247)

Q46389 5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase; 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase; MeTr; EC 2.1.1.258 from Moorella thermoacetica (Clostridium thermoaceticum) (see 2 papers)
31% identity, 82% coverage: 23:283/320 of query aligns to 3:260/262 of Q46389

query
sites
Q46389

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K

M

K

E

I

L

V

V

E

A

R

A

A

A

A

D

D

E

F

F

G

G

I

L

P

P

A

M

H

E

D

D

I

L

V

Y

V

I

D
|
D

P

P

L

L

V

I

M

L

P

P

I

A

G

N

A

V

L

A

G

Q

D

D

A

H

G

A

R

P

Q

E

V

V

F

L

A

K

L

T

L

L

R

Q

L

I

R
x
K

-

M

-

L

E

A

E

D

L

P

K

A

V

P

N

K

T

T

T

V

C

L

G

G

L

L

S

S

N
|
N

I

V

S

S

F
x
Q

G

N

L

C

P

Q

H

N

R
|
R

H

P

G

L

I

I

N

N

A

R

G

T

F

F

I

L

P

A

M

M

V

A

I

M

G

A

A

C

G
|
G

M

L

T
x
D

S

A

A

A

I

I

M

A

N

D

P

A

C

C

R

D

P

E

Q

A

E

L

M

I

E

E

A

T

V

A

H

A

A

T

A

A

N

E

V

I

L

L

N

L

G

N

T

Q

D

T

A

V

N

Y

C

C

T

D

Y

S

W

F

I

V

K

K

K

M

Y

F

R

K

N96 (= N121) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
D160 (= D185) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
K184 (≠ R209) binding Ca(2+)
N199 (= N222) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate; mutation to A: 20-fold decreased affinity for methyltetrahydrofolate and nearly abolished catalytic activity.
Q202 (≠ F225) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
R207 (= R230) binding (6S)-5-methyl-5,6,7,8-tetrahydrofolate
G222 (= G245) binding Ca(2+); binding Ca(2+)
D224 (≠ T247) binding Ca(2+); binding Ca(2+)

8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
31% identity, 77% coverage: 6:252/320 of query aligns to 317:569/841 of 8g3hA

query
sites
8g3hA

V

V

A

A

S

S

A

L

T

Y

R

Q

E

A

I

V

I

P

I

L

G

R

F
x
Q

D

E

Q
x
T

P
x
S

F

L

C

L

V

L

I

V

G

G

E

E

R

R

I

L

N

N

P

A

T

T

G

G

R

S

K

K

K

R

L

F

A

R

A

E

E

L

M

L

I

F

E

A

G

G

N

D

F

L

D

E

T

G

V

I

I

L

R

A

D

L

A

A

L

Q

E

E

Q

Q

V

V

A

A

A

E

G

G

A

A

T

H

M

V

L

L

D

D

V

L

N

S

A

V

G

A

V

W

T

T

A

G

V

R

D

D

P

-

N

-

A

-

T

-

E

E

P

L

G

E

L

D

L

M

V

K

Q

R

T

V

L

L

E

S

I

K

V

L

Q

A

N

T

L

G

V

V

D

T

V

V

P

P

L

F

S

M

I

V

D

D

S

S

S

T

V

S

S

P

A

E

A

V

I

M

E

E

A

E

A

A

L

L

K

K

V

R

A

L

K

P

G

G

R

R

P

A

L

I

V

L

N

N

S

S

V

A

T

N

G

L

E

E

E

D

-

G

-

L

E

E

K

K

L

F

E

D

A

R

I

V

L

A

P

S

L

L

I

A

K

K

K

A

Y

H

N

G

V

A

P

A

V

L

V

V

A

A

I

L

S

A

N

I

D

D

E

E

T

E

G

G

I

M

S

A

M

K

D

T

P

R

D

V

V

K

R

K

F

V

A

E

V

V

A

A

K

L

K

R

I

M

V

Y

E

E

R

R

A

L

A

T

D

E

-

H

F

H

G

G

I

L

P

R

A

P

H

E

D

D

I

L

V

L

V

F

D

D

P

L

L

L

V

T

M

F

P

P

I

I

G

T

A

Q

L

-

G

G

D

D

A

E

-

E

-

T

-

R

-

P

-

L

G

A

R

R

Q

E

V

T

F

L

A

L

L

A

L

L

R

E

L

L

R

R

E

E

E

R

L

L

K

P

-

G

V

V

N

G

T

F

T

V

C

L

G

G

L

V

S

S

N

N

I

V

S

S

F

F

G

G

L

L

-

K

-

P

P

K

H

A

R

R

H

R

G

V

I

L

N

N

A

S

G

V

F

F

I

L

P

D

M

E

V

A

I

R

G

K

A

K

G

G

M

L

T

T

S

A

A

A

I

I

M

V

N

D

binding cobalamin: Q328 (≠ F17), T330 (≠ Q19), S331 (≠ P20)

Sites not aligning to the query:

binding cobalamin: 675, 685, 693, 720, 722, 723, 724, 725, 726, 730, 767, 768, 770, 772, 795, 796, 797, 798, 799, 818, 819, 820, 821

4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
31% identity, 73% coverage: 21:252/320 of query aligns to 331:573/611 of 4cczA

query
sites
4cczA

F

F

C

V

V

N

I

I

G

G

E
|
E

R

R

I

C

N

N

P

V

T

A

G
|
G

R

S

K
x
R

K

K

L

F

A

A

A

K

E

L

M

I

I

M

E

A

G

G

N

N

F

Y

D

E

T

E

V

A

I

L

R

C

D

V

A

A

L

K

E

V

Q

Q

V

V

A

E

A

M

G

G

A

A

T

Q

M

V

L

L

D

D

V

V

N

N

A

M

G

D

V

D

T

G

A

M

V

L

D

D

P

G

N

-

A

-

T

-

E

-

P

P

G

S

L

A

L

M

V

T

Q

R

T

F

L

C

E

N

I

L

V

I

Q

A

-

S

-

E

-

P

N

D

L

I

V

A

D

K

V

V

P

P

L

L

S

C

I

I

D

D

S

S

V

N

S

F

A

A

A

V

I

I

E

E

A

A

A

G

L

L

K

K

V

C

A

C

K

Q

G

G

R

K

P

C

L

I

V

V

N
|
N

S

S

V

I

T

S

-

L

-

K

-

E

G

G

E

E

E

D

K

F

L

L

E

E

A

K

I

A

L

R

P

K

L

-

I

I

K

K

Y

Y

N

G

V

A

P

A

V

M

V

V

A

V

I
x
M

S

A

N

F

D

D

E

E

T

E

G

G

I

Q

S

A

M

T

D

E

P

T

D

D

V

T

R

K

F

I

A

R

V

V

A

C

K

T

K

R

I

A

V

Y

E

H

-

L

R

L

A

V

A

K

D

K

F

L

G

G

I

F

P

N

A

P

H

N

D

D

I

I

V

I

V

F

D
|
D

P

P

L

N

V

I

M

L

P

T

I

I

G

G

A

T

L

-

G

G

D

M

A

E

G

E

R

H

Q

N

V

L

F

Y

A

A

L

I

-

N

-

F

-

I

-

H

-

A

L

T

R

K

R

V

L

I

R

K

E

E

E

T

L

L

-

P

K

G

V

A

N

R

T

I

T

S

C

G

G
|
G

L

L

S
|
S

N
|
N

I

L

S

S

F
|
F

G

S

L

F

P
x
R

H

G

-

M

-

E

-

A

-

I

R
|
R

H

E

G

A

I

M

N

H

A

G

G

V

F

F

I

L

P

Y

M

H

V

A

I

I

G

K

A

S

G

G

M

M

T

D

S

M

A

G

I

I

M

V

N

N

binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E26), G342 (= G32), R344 (≠ K34), N430 (= N121), M458 (≠ I147), D497 (= D185), G536 (= G219), S538 (= S221), N539 (= N222), F542 (= F225), R545 (≠ P228), R551 (= R230)

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, 73% coverage: 21:252/320 of query aligns to 371:613/1265 of Q99707

query
sites
Q99707

F

F

C

V

V

N

I

I

G

G

E

E

R

R

I

C

N

N

P

V

T

A

G
|
G

R
x
S

K
x
R

K

K

L

F

A

A

A

K

E

L

M

I

I

M

E

A

G

G

N

N

F

Y

D

E

T

E

V

A

I

L

R

C

D

V

A

A

L

K

E

V

Q

Q

V

V

A

E

A

M

G

G

A

A

T

Q

M

V

L

L

D

D

V

V

N

N

A

M

G

D

V

D

T

G

A

M

V

L

D

D

P

G

N

-

A

-

T

-

E

-

P

P

G

S

L

A

L

M

V

T

Q

R

T

F

L

C

E

N

I

L

V

I

Q

A

-

S

-

E

-

P

N

D

L

I

V

A

D

K

V

V

P

P

L

L

S

C

I

I

D
|
D

S

S

V

N

S

F

A

A

A

V

I

I

E

E

A

A

A

G

L

L

K

K

V

C

A

C

K

Q

G

G

R

K

P

C

L

I

V

V

N
|
N

S

S

V

I

T

S

-

L

-

K

-

E

G

G

E

E

E

D

K

F

L

L

E

E

A

K

I

A

L

R

P

K

L

-

I

I

K

K

Y

Y

N

G

V

A

P

A

V

M

V

V

A

V

I

M

S

A

N

F

D

D

E

E

T

E

G

G

I

Q

S

A

M

T

D

E

P

T

D

D

V

T

R

K

F

I

A

R

V

V

A

C

K

T

K

R

I

A

V

Y

E

H

-

L

R

L

A

V

A

K

D

K

F

L

G

G

I

F

P

N

A

P

H

N

D

D

I

I

V

I

V

F

D
|
D

P

P

L

N

V

I

M

L

P

T

I

I

G

G

A

T

L

-

G

G

D

M

A

E

G

E

R

H

Q

N

V

L

F

Y

A

A

L

I

-

N

-

F

-

I

-

H

-

A

L

T

R

K

R

V

L

I

R

K

E

E

E

T

L

L

K

P

-

G

V

A

N

R

T

I

T

S

C

G

G

G

L

L

S

S

N
|
N

I

L

S

S

F

F

G

S

L

F

P
x
R

H

G

-

M

-

E

-

A

-

I

R
|
R

H

E

G

A

I

M

N

H

A

G

G

V

F

F

I

L

P

Y

M

H

V

A

I

I

G

K

A

S

G

G

M

M

T

D

S

M

A

G

I

I

M

V

N

N

GSR 382:384 (≠ GRK 32:34) binding (6S)-5,6,7,8-tetrahydrofolate
D449 (= D100) binding (6S)-5,6,7,8-tetrahydrofolate
N470 (= N121) binding (6S)-5,6,7,8-tetrahydrofolate
D537 (= D185) binding (6S)-5,6,7,8-tetrahydrofolate
N579 (= N222) binding (6S)-5,6,7,8-tetrahydrofolate
R585 (≠ P228) binding (6S)-5,6,7,8-tetrahydrofolate
R591 (= R230) binding (6S)-5,6,7,8-tetrahydrofolate

Sites not aligning to the query:

61 natural variant: R -> K
255 C → Y: in dbSNP:rs1140598
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.

5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
30% identity, 73% coverage: 21:252/320 of query aligns to 2:239/282 of 5vooA

query
sites
5vooA

F

L

C

F

V

L

I

V

G

G

E
|
E

R
|
R

I

L

N

N

P

A

T

T

G
|
G

R
x
S

K
|
K

K

R

L

F

A

R

A

E

E

M

M

L

I

F

E

A

G

R

N

D

F

L

D

E

T

G

V

I

I

L

R

A

D

L

A

A

L

R

E

E

Q

Q

V

V

A

E

G

G

A

A

T

H

M

A

L

L

D

D

V

L

N

S

A

V

G

A

V

W

T

T

A

G

V

R

D

D

P

-

N

-

A

-

T

-

E

E

P

L

G

E

L

D

L

L

V

R

Q

W

T

L

L

L

E

P

I

H

V

L

Q

A

N

T

L

A

V

L

D

T

V

V

P

P

L

V

S

M

I

V

D
|
D

S

S

S

T

V

S

S

P

A

E

A

A

I

M

E

E

A

L

A

A

L

L

K

K

V

Y

A

L

K

P

G

G

R

R

P

V

L

L

V

L

N
|
N

S

S

V

A

T

N

G

L

E

E

E

D

-

G

-

L

E

E

K

R

L

F

E

D

A

R

I

V

L

A

P

S

L

L

I

A

K

K

K

A

Y

H

N

G

V

A

P

A

V

L

V

V

A

V

I

L

S

A

N

I

D

D

E

E

T

K

G

G

I

M

S

A

M

K

D

T

P

R

D

E

V

E

R

K

F

V

A

R

V

V

A

A

K

L

K

R

I

M

V

Y

E

E

R

R

A

L

A

T

D

E

-

H

F

H

G

G

I

L

P

R

A

P

H

E

D

D

I

L

V

L

V

F

D
|
D

P

L

L

L

V

T

M

F

P

P

I

I

G

T

A

Q

L

-

G

G

D

D

A

E

-

E

-

S

-

R

-

P

-

L

G

A

R

K

Q

E

V

T

F

L

A

L

L

A

L

M

R

E

L

L

R

R

E

E

E

R

L

L

K

P

-

G

V

V

N

G

T

F

T

V

C

L

G
|
G

L

V

S

S

N
|
N

I

V

S

S

F
|
F

G

G

L

L

P

K

-

P

-

R

H

A

R
|
R

H

R

G

V

I

L

N

N

A

S

G

V

F

F

I

L

P

D

M

E

V

A

I

R

G

K

A

R

G

G

M

L

T

T

S

A

A

A

I
|
I

M

V

N

D

binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E26), R8 (= R27), G13 (= G32), S14 (≠ R33), K15 (= K34), D77 (= D100), N98 (= N121), D165 (= D185), G204 (= G219), N207 (= N222), F210 (= F225), R217 (= R230), I237 (= I250)

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)
29% identity, 74% coverage: 15:252/320 of query aligns to 350:598/1227 of P13009

query
sites
P13009

I

I

G

G

F

E

D

D

Q

S

P

L

F

F

C

V

V

N

I

V

G

G

E

E

R

R

I

T

N

N

P

V

T

T

G

G

R

S

K

A

K

K

L

F

A

K

A

R

E

L

M

I

I

K

E

E

G

E

N

K

F

Y

D

S

T

E

V

A

I

L

R

D

D

V

A

A

L

R

E

Q

Q

Q

V

V

A

E

A

N

G

G

A

A

T

Q

M

I

L

I

D

D

V

I

N

N

A

M

G

D

V

E

T

G

A

M

V

L

D

D

P

A

N

E

A

A

T

A

E

-

P

-

G

-

L

-

L

M

V

V

Q

R

T

F

L

L

E

N

I

L

V

I

Q

A

-

G

-

E

-

P

N

D

L

I

V

A

D

R

V

V

P

P

L

I

S

M

I

I

D

D

S

S

V

K

S

W

A

D

A

V

I

I

E

E

A

K

A

G

L

L

K

K

V

C

A

I

K

Q

G

G

R

K

P

G

L

I

V

V

N

N

S

S

V

I

T

S

G

-

E

M

E

K

E

E

K

G

L

V

E

D

A

A

I

F

L

I

-

H

-

A

P

K

L

L

I

L

K

R

Y

Y

N

G

V

A

P

A

V

V

A

V

I

M

S

A

N

F

D

D

E

E

T

Q

G

G

I

-

S

-

M

-

D

Q

P

A

D

D

V

T

R

R

F

-

A

A

V

R

A

K

K

I

K

E

I

I

V

C

E

R

R

R

A

A

-

Y

-

K

-

I

-

L

-

T

A

E

D

E

F

V

G

G

I

F

P

P

A

P

H

E

D

D

I

I

V

I

V

F

D

D

P

P

L

N

V

I

M

F

P

A

I

V

G

A

A

T

-

G

-

I

-

E

L

H

G

N

D

N

A

Y

G

A

R

Q

Q

D

V

F

F

I

A

G

L

A

L

C

R

E

R

D

L

I

R

K

E

R

E

E

L

L

-

P

K

H

V

A

N

L

T

I

T

S

C

G

G

G

L

V

S

S

N

N

I

V

S

S

F

F

G

S

L

F

-

R

-

G

-

N

-

D

P

P

H

V

R

R

H

E

G

A

I

I

N

H

A

A

G

V

F

F

I

L

P

Y

M

Y

V

A

I

I

G

R

A

N

G

G

M

M

T

D

S

M

A

G

I

I

M

V

N

N

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.
694 binding methylcob(III)alamin
756:760 binding methylcob(III)alamin
757 D→E: Decreases activity by about 70%.; D→N: Decreases activity by about 45%.
759 binding axial binding residue; H→G: Loss of catalytic activity.
804 binding methylcob(III)alamin
808 binding methylcob(III)alamin
810 S→A: Decreases activity by about 40%.
860 binding methylcob(III)alamin
946 binding S-adenosyl-L-methionine
1134 binding S-adenosyl-L-methionine
1189:1190 binding S-adenosyl-L-methionine

3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
31% identity, 73% coverage: 21:253/320 of query aligns to 4:247/287 of 3k13C

query
sites
3k13C

F

F

C

V

V

N

I

I

G

G

E
|
E

R

R

I

C

N

N

P

V

T

A

G
|
G

R

S

K
x
R

K

K

L

F

A

L

A

R

E

L

M

V

I

N

E

E

G

K

N

K

F

Y

D

D

T

E

V

A

I

L

R

S

D

I

A

A

L

R

E

Q

Q

Q

V

V

A

E

A

D

G

G

A

A

T

L

M

V

L

I

D

D

V

V

N

N

A

M

G

D

V

D

T

G

A

L

V

L

D

D

P

A

N

R

A

-

T

T

E

E

P

M

G

T

L

T

L

F

V

L

Q

N

T

L

L

I

E

M

I

S

V

E

Q

P

N

E

L

I

V

A

D

R

V

V

P

P

L

V

S

M

I

I

D

D

S

S

V

K

S

W

A

E

A

V

I

I

E

E

A

A

A

G

L

L

K

K

V

C

A

L

K

Q

G

G

R

K

P

S

L

I

V

V

N
|
N

S

S

V

I

T

S

-

L

-

K

-

E

G

G

E

E

E

V

K

F

L

L

E

E

A

H

I

A

L

-

P

R

L

I

I

I

K

K

K

Q

Y

Y

N

G

V

A

P

A

V

T

V

V

A

V

I

M

S

A

N

F

D

D

E

E

T

K

G

G

I

Q

S

A

M

D

D

T

P

A

D

A

V

R

R

K

F

I

A

E

V

V

A

C

K

E

K

R

I

A

V

Y

E

R

R

L

A

L

A

V

D

D

-

K

F

V

G

G

I

F

P

N

A

P

H

H

D

D

I

I

V

I

V

F

D
|
D

P

P

L

N

V

V

M

L

P

A

I

V

G

-

A

A

L

T

G

G

D

I

A

E

G

E

R

H

Q

N

V

N

F

Y

A

A

L

V

-

D

-

F

-

I

-

E

-

A

L

T

R

G

R

W

L

I

R

R

E

K

E

N

L

L

-

P

K

G

V

A

N

H

T

V

T

S

C

G

G
|
G

L

V

S
|
S

N
|
N

I

L

S

S

F

F

G

S

L

F

P
x
R

H

G

-

N

-

Y

-

I

R
|
R

H

E

G

A

I

M

N

H

A

A

G

V

F

F

I

L

P

Y

M

H

V

A

I

I

G

Q

A

Q

G

G

M

M

T

D

S

M

A

G

I
|
I

M

V

N

N

P

P

binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E9 (= E26), G15 (= G32), R17 (≠ K34), N103 (= N121), D170 (= D185), G209 (= G219), S211 (= S221), N212 (= N222), R218 (≠ P228), R224 (= R230), I244 (= I250)

6pz2A Crystal structure of folp (dihydropteroate synthase) from colstridium difficile in the presence of pteroic acid
29% identity, 52% coverage: 44:210/320 of query aligns to 29:194/263 of 6pz2A

query
sites
6pz2A

N

N

F

L

D

D

T

I

V

A

I

I

R

Q

D

H

A

A

L

K

E

D

Q

M

V

V

A

D

A

Q

G

G

A

A

T

D

M

I

L

I

D

D

V

L

N

G

A

G

-

E

-

S

-
x
T

-

R

-
x
P

G

G

V

H

T

S

A

Y

V

V

D

D

P

S

N

D

A

E

T

-

E

E

P

L

G

R

L

R

L

V

V

I

Q

P

T

V

L

I

E

K

I

K

V

L

Q

K

N

Q

L

E

V

L

D

D

V

I

P

P

L

I

S

S

I

I

D

D

S

T

S

Y

V

K

S

A

A

D

A

V

I

A

E

E

A

E

A

A

L

L

K

K

V

L

A

-

K

-

G

G

R

V

P

T

L

M

V

V

N
|
N

S

D

V
|
V

T

W

G

G

E

-

E

L

E

R

K

K

L

D

E

K

A

N

I

M

L

A

P

S

L

V

I

I

K

G

K

K

Y

Y

N

D

V

A

P

E

V

V

V

C

A

I

I
x
M

S

H

N

N

D

-

E

Q

T

D

G

G

I

T

S

N

M

Y

D

D

P

K

D

D

V

I

R

M

F

E

A

S

V

I

A

K

-

D

-

F

K

K

K

V

I

S

V

I

E

E

R

M

A

A

A

M

D

S

F

C

G

G

I

V

P

K

A

K

H

E

D

K

I

I

V

V

V

L

D
|
D

P

P

L

G

V

V

M

-

P

-

I

-

G

-

A
x
G

L
x
F

G

G

D

K

A

D

G

F

R

E

Q

Q

V

N

F

I

A

E

L

V

L

L

R

R

L

L

R

N

E

E

binding pteroic acid: T55 (vs. gap), P57 (vs. gap), N108 (= N121), V110 (= V123), M133 (≠ I147), D173 (= D185), G177 (≠ A193), F178 (≠ L194)

Sites not aligning to the query:

binding pteroic acid: 205, 209, 210, 243

Query Sequence

>WP_106718068.1 NCBI__GCF_003010935.1:WP_106718068.1
MTRTIVASATREIIIGFDQPFCVIGERINPTGRKKLAAEMIEGNFDTVIRDALEQVAAGA
TMLDVNAGVTAVDPNATEPGLLVQTLEIVQNLVDVPLSIDSSVSAAIEAALKVAKGRPLV
NSVTGEEEKLEAILPLIKKYNVPVVAISNDETGISMDPDVRFAVAKKIVERAADFGIPAH
DIVVDPLVMPIGALGDAGRQVFALLRRLREELKVNTTCGLSNISFGLPHRHGINAGFIPM
VIGAGMTSAIMNPCRPQEMEAVHAANVLNGTDANCTYWIKKYRDHQPAAPGVAASVSVPA
DSAGGGRRRGGREARRGVAS

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