SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_051377698.1 NCBI__GCF_000482785.1:WP_051377698.1 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 11 hits to proteins with known functional sites (download)

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)
58% identity, 97% coverage: 5:348/353 of query aligns to 2:336/1227 of P13009

query
sites
P13009

S

S

D

S

L

K

A

V

A

E

R

Q

L

L

A

R

D

A

A

Q

M

L

S

N

R

E

R

R

I

I

L

L

I

V

L

L

D

D

G

G

A

G

M

M

G

G

T

T

M

M

I

I

Q

Q

R

S

Y

Y

K

R

L

L

D

N

E

E

A

A

A

D

Y

F

R

R

G

G

A

E

R

R

F

F

A

A

D

D

W

W

Q

-

P

P

A

C

D

D

L

L

A

-

P

-

G

-

K

-

Q

-

L

-

F

-

L

-

K

K

G

G

N

N

D

D

L

L

V

V

L

L

T

S

Q

K

P

P

E

E

V

V

I

I

A

A

E

A

I

I

H

H

G

N

K

A

Y

Y

L

F

A

E

A

A

G

G

A

A

D

D

I

I

E

E

T

T

N

N

T

T

F

F

G

N

A

S

T

T

S

T

V

I

A

A

Q

M

A

A

D

D

Y

Y

H

Q

M

M

A

E

D

S

L

L

A

S

Y

A

E

E

M

I

N

N

L

F

A

A

R

K

L

L

A

A

R

R

A

A

E

C

C

A

D

D

K

E

Y

W

S

T

-

A

-

R

T

T

A

P

D

E

K

K

P

P

R

R

F

Y

V

V

A

A

G

G

A

V

L

L

G

G

P

P

T

T

P

N

K

R

T

T

A

A

S

S

I

I

S

S

P

P

D

D

V

V

N

N

D

D

P

P

G

A

A

F

R

R

N

N

V

I

S

T

F

F

D

D

E

G

L

L

V

V

A

A

Y

Y

H

R

E

E

Q

S

A

T

R

K

G

A

L

L

W

V

D

E

G

G

A

A

D

D

L

L

F

I

L

L

V

I

E

E

T

T

I

V

F

F

D

D

T

T

L

L

N

N

A

A

K

K

A

A

L

V

F

F

A

A

I

V

D

K

Q

T

L

E

F

F

E

E

E

A

R

L

G

G

A

V

T

E

L

L

P

P

I

I

M

M

I

I

S

S

G

G

T

T

V

I

T

T

D

D

A

A

S

S

G

G

R

R

I

T

L

L

S

S

G

G

Q

Q

T

T

V

T

A

E

A

A

F

F

W

Y

H

N

S

S

V

L

R

R

H

H

A

A

R

E

P

A

I

L

T

T

I

F

G

G

L

L

N

N

C
|
C

A

A

L

L

G

G

A

P

A

D

L

E

M

L

R

R

P

Q

Y

Y

I

V

A

Q

E

E

L

L

S

S

K

R

I

I

A

A

D

E

T

C

R

Y

I

V

C

T

V

A

Y

H

P

P

N

N

A

A

G

G

L

L

P

P

N

N

P

A

M

F

S

G

D

E

T

-

G

-

F

Y

D

D

E

L

T

D

P

A

D

D

V

T

T

M

S

A

R

K

L

Q

L

I

K

R

E

E

F

W

A

A

E

Q

A

A

G

G

F

F

V

L

N

N

I

I

A

V

G

G

C
|
C

G

G

T

T

P

P

E

Q

H

H

I

I

A

A

I

M

A

S

Q

R

A

A

V

V

A

E

T

G

V

L

T

A

P

P

R

R

R

K

V

L

P

P

D

E

L

I

C247 (= C257) binding Zn(2+)
C310 (= C322) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
C311 (= C323) binding Zn(2+); mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
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

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)
58% identity, 94% coverage: 15:346/353 of query aligns to 26:347/1265 of Q99707

query
sites
Q99707

M

L

S

Q

R

K

R

R

I

I

L

M

I

V

L

L

D

D

G

G

A

G

M

M

G

G

T

T

M

M

I

I

Q

Q

R

R

Y

E

K

K

L

L

D

N

E

E

A

E

A

H

Y

F

R

R

G

G

A

Q

R

E

F

F

A

K

D

D

W

H

-

A

Q
x
R

P

P

A

-

D

-

L

-

A

-

P

-

G

-

K

-

Q

-

L

-

F

-

L

L

K

K

G

G

N

N

D

D

L

I

L

L

V

S

L

I

T

T

Q

Q

P

P

E

D

V

V

I

I

A

Y

E

Q

I

I

H

H

G

K

K

E

Y

Y

L

L

A

L

A

A

G

G

A

A

D

D

I

I

E

E

T

T

N

N

T

T

F

F

G

S

A

S

T

T

S

S

V

I

A

A

Q

Q

A

A

D

D

Y

Y

H

G

M

L

A

E

D

H

L

L

A

A

Y

Y

E

R

M

M

N

N

L

M

A

C

A

S

A

A

R

G

L

V

A

A

R

R

-

K

-

A

A

A

E

E

C

E

D

V

K

T

Y

L

S

Q

T

T

A

G

D

I

K

K

P

-

R

R

F

F

V

V

A

A

G

G

A

A

L

L

G

G

P

P

T

T

P

N

K

K

T

T

A

L

S

S

I

V

S

S

P

P

D

S

V

V

N

E

D

R

P

P

G

D

A

Y

R

R

N

N

V

I

S

T

F

F

D

D

E

E

L

L

V

V

A

E

A

A

Y

Y

H

Q

E

E

Q

Q

A

A

R

K

G

G

L

L

W

L

D

D

G

G

A

V

D

D

L

I

F

L

L

L

V

I

E

E

T

T

I

I

F

F

D

D

T

T

L

A

N

N

A

A

K

K

A

A

L

L

F

F

A

A

I

L

D

Q

Q

N

L

L

F

F

E

E

R

K

G

Y

A

A

T

P

L

R

P

P

I

I

M

F

I

I

S

S

G

G

T

T

V

I

T

V

D

D

A

K

S

S

G

G

R

R

I

T

L

L

S

S

G

G

Q

Q

T

T

V

G

A

E

A

G

F

F

W

V

H

I

S

S

V

V

R

S

H

H

A

G

R

E

P

P

I

L

T
x
C

I

I

G

G

L

L

N

N

C

C

A

A

L

L

G

G

A

A

L

E

M

M

R

R

P

P

Y

F

I

I

A

E

E

I

L

I

S

G

K

K

I

C

A

T

D

T

T

A

R

Y

I

V

C

L

V

C

Y

Y

P

P

N

N

A

A

G

G

L

L

P

P

N

N

P

T

M

F

S

G

D

D

T

-

G

-

F

Y

D

D

E

E

T

T

P

P

D

S

V

M

T

M

S

A

R

K

L

H

L

L

K

K

E

D

F

F

A

A

E

M

A

D

G

G

F

L

V

V

N

N

I

I

A

V

G

G

C

C

G

G

T

S

T

T

P

P

E

D

H

H

I

I

A

R

A

E

I

I

A

A

Q

E

A

A

V

V

A

K

T

N

V

C

T

K

P

P

R

R

R

V

V

P

P

P

R61 (≠ Q49) natural variant: R -> K
C255 (≠ T252) to Y: in dbSNP:rs1140598

Sites not aligning to the query:

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.

4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
53% identity, 94% coverage: 15:346/353 of query aligns to 10:307/611 of 4cczA

query
sites
4cczA

M

L

S

Q

R

K

R

R

I

I

L

M

I

V

L

L

D

D

G

G

A

G

M

M

G

G

T

T

M

M

I

I

Q

Q

R

R

Y

E

K

K

L

L

D

E

E

E

A

H

A

-

Y

F

R

R

G

G

A

Q

R

E

F

F

A

K

D

D

W

H

-

A

Q

R

P

P

A

-

D

-

L

-

A

-

P

-

G

-

K

-

Q

-

L

-

F

-

L

L

K

K

G

G

N

N

D

D

L

I

L

L

V

S

L

I

T

T

Q

Q

P

P

E

D

V

V

I

I

A

Y

E

Q

I

I

H

H

G

K

K

E

Y

Y

L

L

A

L

A

A

G

-

A

-

D

D

I

I

E

E

T

T

N

N

T

T

F

F

G

S

A

S

T

T

S

S

V

I

A

A

Q

Q

A

A

D

D

Y

Y

H

G

M

L

A

E

D

H

L

L

A

A

Y

Y

E

R

M

M

N

N

L

M

A

C

A

S

A

A

R

G

L

V

A

A

R

R

A

K

E

A

C

A

D

E

K

E

Y

V

S

T

T

L

A

Q

D

T

K

G

-

I

P

K

R

R

F

F

V

V

A

A

G

G

A

A

L

L

G

G

P

P

T

T

P

N

K

K

T

T

A

L

S

S

I

V

S

S

P

P

D

S

V

V

N

E

D

R

P

P

G

D

A

Y

R

R

N

N

V

I

S

T

F

F

D

D

E

E

L

L

V

V

A

E

A

A

Y

Y

H

Q

E

E

Q

Q

A

A

R

K

G

G

L

L

W

L

D

D

G

G

A

V

D

D

L

I

F

L

L

L

V

I

E

E

T

T

I

I

F

F

D

D

T

T

L

A

N

N

A

A

K

K

A

A

L

L

F

F

A

A

I

L

D

Q

Q

N

L

L

F

F

E

E

R

K

G

Y

A

A

T

P

L

R

P

P

I

I

M

F

I

I

S

S

G

G

T

T

V

I

T

V

D

D

A

K

S

S

G

G

R

R

I

T

L

L

S

S

G

G

Q

Q

T

T

V

G

A

E

A

G

F

F

W

V

H

I

S

S

V

V

R

S

H

H

A

G

R

E

P

P

I

L

T

C

I

I

G

G

L

L

N

N

C

C

A

A

L

L

G

G

A

A

L

E

M

M

R

R

P

P

Y

F

I

I

A

E

E

I

L

I

S

G

K

K

I

C

A

T

D

T

T

A

R

Y

I

V

C

L

V

C

Y

Y

P

P

N

N

A

A

G

G

L

-

P

-

N

-

P

-

M

-

S

-

D

-

T

-

G

-

F

-

D

-

E

-

T

-

P

-

D

-

V

-

T

-

S

-

R

-

L

-

K

-

E

-

F

F

A

A

E

M

A

D

G

G

F

L

V

V

N

N

I

I

A

V

G

G

C

C

G

G

T

S

T

T

P

P

E

D

H

H

I

I

A

R

A

E

I

I

A

A

Q

E

A

A

V

V

A

K

T

N

V

C

T

K

P

P

R

R

R

V

V

P

P

P

Sites not aligning to the query:

binding (6s)-5,6,7,8-tetrahydrofolate: 336, 342, 344, 430, 458, 497, 536, 538, 539, 542, 545, 551

8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
37% identity, 92% coverage: 14:337/353 of query aligns to 8:301/841 of 8g3hA

query
sites
8g3hA

A

A

M

L

S

S

R

Q

R

R

I

V

L

L

I

V

L

F

D

D

G

G

A

A

M

M

G

G

T

T

M

E

I

L

Q

Q

R

K

Y

-

K

-

L

-

D

-

E

-

A

-

Y

-

R

-

G

-

A

-

R

-

F

-

A

R

D

D

W

L

Q

T

P

P

A

E

D

D

L

Y

A

-

P

-

G

G

K

E

Q

E

L

A

F

Y

L

Y

K

-

G

G

N

C

N

P

D

E

L

V

L

L

V

N

L

R

T

T

Q

R

P

P

E

D

V

V

I

V

A

R

E

E

I

I

H

H

G

L

K

S

Y

Y

L

L

A

E

A

A

G

G

A

A

D

E

I

V

I

I

E

E

T

T

N

N

T

S

F

F

G

G

A

A

T

L

S

R

V

H

A

V

Q

L

A

A

D

E

Y

Y

H

G

M

L

A

G

D

E

L

E

A

A

Y

E

E

E

M

L

N

A

L

Y

A

R

A

A

R

R

L

I

A

A

R

K

A

E

E

A

C

A

D

E

K

P

Y

Y

S

G

T

A

A

-

D

-

K

-

P

-

R

-

F

F

V

V

A

A

G

G

A

A

L

L

G

G

P

P

T

G

P

T

K

K

T

L

A

V

S

S

I

L

S

G

P

-

D

-

V

-

N

-

D

-

P

-

G

-

A

-

R

-

N

Q

V

I

S

S

F

W

D

E

E

E

L

L

V

F

A

S

A

A

Y

Y

H

K

E

E

Q

A

A

V

R

R

G

G

L

L

W

V

D

R

G

G

A

V

D

D

L

L

F

I

L

L

V

L

E

E

T

T

I

A

F

Q

D

D

T

I

L

L

N

Q

A

V

K

R

A

C

A

A

L

V

F

L

A

A

I

A

D

R

Q

E

L

A

F

M

E

A

E

E

R

L

G

G

A

V

T

E

L

L

P

P

I

L

M

Q

I

V

S

Q

G

V

T

T

V

F

T

-

D

E

A

A

S

T

G

G

R

T

I

M

L

L

S

V

G

G

Q

T

T

D

V

E

A

Q

A

A

F

A

W

L

H

A

S

A

V

L

R

E

H

S

A

L

R

P

P

I

I

D

T

V

I

V

G

G

L

M

N

N

C

C

A

A

L

T

G

G

A

P

A

D

L

L

M

M

R

D

P

A

Y

K

I

I

A

R

E

Y

L

F

S

A

K

Q

I

E

A

S

D

T

T

R

R

F

I

V

C

A

V

C

Y

L

P

P

N

N

A

A

G

G

L

L

P

P

-

R

N

N

P

E

M

G

S

G

D

R

T

V

G

V

F

Y

D

D

E

L

T

T

P

P

D

E

V

E

T

L

S

A

R

R

L

W

L

H

K

L

E

K

F

F

A

V

E

T

A

E

G

Y

F

G

V

V

N

N

I

A

A

V

G

G

C

C

G

G

T

T

T

G

P

P

E

E

H

H

I

I

A

R

A

K

I

V

A

A

Q

E

A

A

V

V

Sites not aligning to the query:

binding cobalamin: 328, 330, 331, 675, 685, 693, 720, 722, 723, 724, 725, 726, 730, 767, 768, 770, 772, 795, 796, 797, 798, 799, 818, 819, 820, 821

3bofA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima complexed with zn2+ and homocysteine (see paper)
28% identity, 94% coverage: 11:342/353 of query aligns to 7:292/560 of 3bofA

query
sites
3bofA

L

V

A

S

D

K

A

L

M

L

S

S

R

E

R

R

I

V

L

L

I

L

L

L

D

D

G

G

A

A

M

Y

G

G

T

T

M

E

I

F

Q

M

R

K

Y

Y

K

G

L

Y

D

D

E

D

A

L

A

-

Y

-

R

-

G

-

A

-

R

-

F

-

A

-

D

-

W

-

Q

-

P

P

A

E

D

E

L

L

A

N

P

-

G

-

K

-

Q

-

L

-

F

-

L

-

K

-

G

-

N

-

D

-

L

-

V

-

L

I

T

K

Q

A

P

P

E

D

V

V

I

V

A

L

E

K

I

V

H

H

G

R

K

S

Y

Y

L

I

A

E

A

S

G

G

A

S

D

D

I

V

I

I

E

L

T

T

N

N

T

T

F

F

G

G

A

A

T

T

S

R

V

M

A

K

Q

L

A

R

D

K

Y

H

H

G

M

L

A

E

D

D

L

K

A

L

Y

D

E

P

M

I

N

V

L

R

A

N

A

A

A

V

R

R

L

I

A

A

R

R

A

-

E

-

C

-

D

-

K

-

Y

-

S

-

T

R

A

A

D

A

K

G

P

E

R

K

F

L

V

V

A

F

G

G

A

D

L

I

G

G

P

P

T

T

P

G

K

E

T

L

A

P

S

Y

I

-

S

-

P

-

D

-

V

-

N

-

D

-

P

P

G

L

A

G

R

S

N

T

V

L

S

-

F

F

D

E

E

E

L

F

V

Y

A

E

A

N

Y

F

H

R

E

E

Q

T

A

V

R

E

G

I

L

M

W

V

D

E

G

E

G

G

A

V

D

D

L

G

F

I

L

I

V

F

E

E

T

T

I

F

F

S

D

D

T

I

L

L

N

E

A

L

K

K

A

A

L

V

F

L

A

A

I

A

D

R

Q

E

L

V

F

S

E

R

E

D

R

-

G

-

A

-

T

-

L

-

P

V

I

F

M

L

I

I

S

A

G

H

T

M

V

T

T

F

D

D

A

E

S

K

G

G

R

R

I

S

L

L

S

T

G

G

Q

T

T

D

V

P

A

A

A

N

F

F

W

A

H

I

S

T

V

F

R

D

H

E

A

L

R

D

P

I

I

D

T

A

I

L

G

G

L

I

N

N

C
|
C

A

S

L

L

G

G

A

P

A

E

L

E

M

I

R

L

P

P

Y

I

I

F

A

Q

E

E

L

L

S

S

K

Q

I

Y

A

T

D

D

T

K

R

F

I

L

C

V

V

V

Y

E

P

P

N

N

A

A

G

G

L

-

P

-

N

K

P

P

M

I

S

V

D

E

T

N

G

G

-

K

-

T

-

V

F

Y

D

P

E

L

T

K

P

P

D

H

V

D

T

F

S

A

R

V

L

H

L

I

K

D

E

S

F

Y

A

Y

E

E

A

L

G

G

F

-

V

V

N

N

I

I

A

F

G

G

C
|
C

C

C

G

G

T

T

P

P

E

E

H

H

I

V

A

K

A

L

I

F

A

R

Q

K

A

V

V

L

A

G

T

N

V

R

T

K

P

P

binding zinc ion: C207 (= C257), C272 (= C322)

1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
28% identity, 94% coverage: 11:342/353 of query aligns to 7:292/559 of 1q8jA

query
sites
1q8jA

L

V

A

S

D

K

A

L

M

L

S

S

R

E

R

R

I

V

L

L

I

L

L

L

D

D

G

G

A

A

M

Y

G

G

T

T

M

E

I

F

Q

M

R

K

Y

Y

K

G

L

Y

D

D

E

D

A

L

A

-

Y

-

R

-

G

-

A

-

R

-

F

-

A

-

D

-

W

-

Q

-

P

P

A

E

D

E

L

L

A

N

P

-

G

-

K

-

Q

-

L

-

F

-

L

-

K

-

G

-

N

-

D

-

L

-

V

-

L

I

T

K

Q

A

P

P

E

D

V

V

I

V

A

L

E

K

I

V

H

H

G

R

K

S

Y

Y

L

I

A

E

A

S

G

G

A

S

D

D

I

V

I

I

E

L

T

T

N

N

T

T

F

F

G

G

A

A

T

T

S

R

V

M

A

K

Q

L

A

R

D

K

Y

H

H

G

M

L

A

E

D

D

L

K

A

L

Y

D

E

P

M

I

N

V

L

R

A

N

A

A

A

V

R

R

L

I

A

A

R

R

A

-

E

-

C

-

D

-

K

-

Y

-

S

-

T

R

A

A

D

A

K

G

P

E

R

K

F

L

V

V

A

F

G

G

A

D

L

I

G

G

P

P

T

T

P

G

K

E

T

L

A

P

S

Y

I

-

S

-

P

-

D

-

V

-

N

-

D

-

P

P

G

L

A

G

R

S

N

T

V

L

S

-

F

F

D

E

E

E

L

F

V

Y

A

E

A

N

Y

F

H

R

E

E

Q

T

A

V

R

E

G

I

L

M

W

V

D

E

G

E

G

G

A

V

D

D

L

G

F

I

L

I

V

F

E

E

T

T

I

F

F

S

D

D

T

I

L

L

N

E

A

L

K

K

A

A

L

V

F

L

A

A

I

A

D

R

Q

E

L

V

F

S

E

R

E

D

R

-

G

-

A

-

T

-

L

-

P

V

I

F

M

L

I

I

S

A

G

H

T

M

V

T

T

F

D

D

A

E

S

K

G

G

R

R

I

S

L

L

S

T

G

G

Q

T

T

D

V

P

A

A

A

N

F

F

W

A

H

I

S

T

V

F

R

D

H

E

A

L

R

D

P

I

I

D

T

A

I

L

G

G

L

I

N

N

C

C

A

S

L

L

G

G

A

P

A

E

L

E

M

I

R

L

P

P

Y

I

I

F

A

Q

E

E

L

L

S

S

K

Q

I

Y

A

T

D

D

T

K

R

F

I

L

C

V

V

V

Y

E

P

P

N

N

A

A

G

G

L

-

P

-

N

K

P

P

M

I

S

V

D

E

T

N

G

G

-

K

-

T

-

V

F

Y

D

P

E

L

T

K

P

P

D

H

V

D

T

F

S

A

R

V

L

H

L

I

K

D

E

S

F

Y

A

Y

E

E

A

L

G

G

F

-

V

V

N

N

I

I

A

F

G

G

C

C

G

G

T

T

P

P

E

E

H

H

I

V

A

K

A

L

I

F

A

R

Q

K

A

V

V

L

A

G

T

N

V

R

T

K

P

P

Sites not aligning to the query:

binding 5-methyl-5,6,7,8-tetrahydrofolic acid: 320, 390, 411, 473, 505, 508, 511, 516, 536

5dmmA Crystal structure of the homocysteine methyltransferase mmum from escherichia coli, metallated form (see paper)
26% identity, 89% coverage: 19:333/353 of query aligns to 12:284/288 of 5dmmA

query
sites
5dmmA

I

I

L

L

I

L

L

L

D

D

G

G

A

A

M

M

G

A

T

T

M

E

I

L

Q

E

R

A

Y

-

K

-

L

-

D

-

E

-

A

-

Y

-

R

R

G

G

A

C

R

N

F

L

A

A

D

D

W

-

Q

-

P

-

A

-

D

S

L

L

A

W

P

S

G

A

K

K

Q

-

L

-

F

-

L

-

K

-

G

-

N

-

D

-

L

-

L

V

V

L

L

V

T

E

Q

N

P

P

E

E

V

L

I

I

A

R

E

E

I

V

H

H

G

L

K

D

Y

Y

L

Y

A

R

A

A

G

G

A

A

D

Q

I

C

I

A

E

I

T

T

N

A

T

S

F

Y

G

Q

A

A

T

T

S

P

V

A

A

G

Q

F

A

A

D

A

Y

R

H

G

M

L

A

-

D

D

L

E

A

A

Y

Q

E

S

M

K

N

A

L

L

-

I

-

G

A

K

A

S

A

V

R

E

L

L

A

A

R

R

A

K

E

A

C

R

D

E

K

A

Y

Y

S

-

T

L

A

A

D

E

K

N

P

P

R

Q

-

A

-

G

-

T

-

L

F

L

V

V

A

A

G

G

A

S

L

V

G

G

P

P

T

Y

P

-

K

-

T

G

A

A

S

Y

I

L

S

A

P

D

D

G

V

S

N

E

D

Y

P

R

G

G

A
x
D

R

Y

N
x
H

V

C

S

S

F

V

D

E

E

A

L

F

V

Q

A

A

A

F

Y

H

H

R

E

P

Q

R

A

V

R

E

G

A

L

L

W

L

D

D

G

A

G

G

A

A

D

D

L

L

F

L

L

A

V

C

E

E

T

T

I

L

-

P

-

N

F

F

D

S

T

E

L

I

N

E

A

A

K

L

A

A

A

E

L

L

F

L

A

T

I

A

D

-

Q

-

L

-

F

Y

E

P

E

R

R

A

G

R

A

A

T

W

L

F

P

S

I

F

M

T

I

L

S

R

G

D

T

S

V

E

T

H

D

L

A

S

S

D

G

G

R

T

I

P

L

L

S

-

G

-

Q

R

T

D

V

V

A

V

A

A

F

L

W

L

H

A

S

G

V

-

R

-

H

Y

A

P

R

Q

P

V

I

V

T

A

I

L

G

G

L

I

N

N

C
|
C

A

-

L

I

G

A

A

L

A

E

L

N

M

T

R

T

P

A

Y

A

I

L

A

Q

E

H

L

L

S

H

K

G

I

L

A

T

D

V

T

L

R

P

I

L

C

V

V

V

Y

Y

P

P

N

N

A

S

G

G

L

-

P

-

N

-

P

Q

M

L

S

A

D

D

T

-

G

-

F

-

D

-

E

-

T

-

P

-

D

-

V

-

T

-

S

-

R

-

L

Y

L

L

K

P

E

Q

F

W

A

Q

E

A

A

A

G

G

F

-

V

A

N

R

I

L

A

I

G

G

C
|
C

C

C

G

R

T

T

P

P

E

A

H

D

I

I

A

A

I

L

binding zinc ion: D134 (≠ A161), H136 (≠ N163), C225 (= C257), C273 (= C322)

1umyD Bhmt from rat liver (see paper)
23% identity, 76% coverage: 70:338/353 of query aligns to 41:292/381 of 1umyD

query
sites
1umyD

L

V

T

E

Q

H

P

P

E

E

V

A

I

V

A

R

E

Q

I

L

H

H

G

R

K

E

Y

F

L

L

A

R

A

A

G

G

A

S

D

N

I

V

I

M

E

Q

T

T

N

F

T

T

F

F

G

Y

A

A

T

K

S

I

V

S

A

G

Q

Q

A

-

D

-

Y

-

H

-

M

-

A

-

D

-

L

-

A

-

Y

-

E

K

M

V

N

N

L

E

A

A

A

C

R

D

L

I

A

A

R

R

A

Q

E

V

C

A

D

D

K

E

Y

G

S

D

T

A

A

-

D

-

K

-

P

-

R

-

F

L

V

V

A

A

G

G

A

G

L

V

G

S

P

Q

T

T

P

P

K

S

T

Y

A

L

S

S

I

C

S

K

P

S

D

E

V

T

N

-

D

-

P

-

G

-

A

-

R

-

N

-

V

-

S

-

F

-

D

-

E

E

L

V

V

K

A

K

A

I

Y

F

H

H

E

Q

Q

Q

A

L

R

E

G

V

L

F

W

M

D

K

G

K

G

N

A

V

D

D

L

-

F

F

L

L

V

I

E

A

T

E

I

Y

F

F

D

E

T

-

L

-

N

H

A

V

K

E

A

E

A

A

L

V

F

W

A

A

I

V

D

E

Q

A

L

L

F

K

E

T

E

S

R

G

G

K

A

P

T

I

L

A

P

A

I

T

M

M

I

C

S

I

G

G

T

P

V

E

T

G

D

D

A

L

S

H

G

G

R

-

I

V

L

S

S

P

G

G

Q

E

T

C

V

A

A

V

A

-

F

-

W

-

H

-

S

R

V

L

R

V

H

K

A

A

R

G

P

A

I

A

T

I

I

V

G

G

L

V

N

N

C

C

-

H

-

F

-

D

-

P

-

S

-

T

-

S

-

L

-

Q

-

T

-

I

-

K

-

L

-

M

-

K

-

E

A

G

L

L

G

E

A

A

L

R

M

L

R

K

P

A

Y

Y

I

L

A

M

E

S

L

Q

S

P

K

L

I

A

A

Y

D

H

T

T

R

P

I

D

C

C

V

-

Y

-

P

G

N

K

A

Q

G

G

L

F

P

I

N

D

P

-

M

L

S

P

D

E

T

F

G

P

F

F

D

G

E

L

T

E

P

P

D

R

V

V

T

A

S

T

R

R

L

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

F

Y

-

N

-

L

-

G

V

V

N

R

I

Y

A

I

G

G

C
|
C

G

G

T

F

T

E

P

P

E

Y

H

H

I

I

A

R

A

A

I

I

A

A

Q

E

A

E

V

L

A

A

binding zinc ion: C276 (= C322), C277 (= C323)

1lt8A Reduced homo sapiens betaine-homocysteine s-methyltransferase in complex with s-(delta-carboxybutyl)-l-homocysteine (see paper)
24% identity, 76% coverage: 70:338/353 of query aligns to 40:292/348 of 1lt8A

query
sites
1lt8A

L

V

T

E

Q

H

P

P

E

E

V

A

I

V

A

R

E

Q

I

L

H

H

G

R

K

E

Y

F

L

L

A

R

A

A

G

G

A

S

D

N

I

V

I

M

E

Q

T

T

N

F

T

T

F
|
F

G

-

A

-

T

-

S

-

V

-

A

-

Q

-

A

-

D

-

Y

Y

H

A

M

S

A

E

D

D

L

K

A

G

Y

Q

E

E

M

V

N

N

L

E

A

A

R

D

L

I

A

A

R

R

A

Q

E

V

C

A

D

D

K

E

Y

G

S

D

T

A

A

-

D

-

K

-

P

-

R

-

F

L

V

V

A

A

G

G

A

G

L

V

G

S

P

Q

T

T

P

P

K

S

T

Y

A

L

S

S

I

A

S

K

P

S

D

E

V

T

N

-

D

-

P

-

G

-

A

-

R

-

N

-

V

-

S

-

F

-

D

-

E

E

L

V

V

K

A

K

A

V

Y

F

H

L

E

Q

Q

Q

A

L

R

E

G

V

L

F

W

M

D

K

G

K

G

N

A

V

D

D

L

-

F

F

L

L

V

I

E

A

T
x
E

I
x
Y

F

F

D

E

T

-

L

-

N

H

A

V

K

E

A

E

A

A

L

V

F

W

A

A

I

V

D

E

Q

T

L

L

F

I

E

A

E

S

R

G

G

K

A

P

T

V

L

A

P

A

I

T

M

M

I

A

S

I

G

G

T

P

V

E

T

G

D

D

A

L

S

H

G

G

R

-

I

V

L

P

S

P

G

G

Q

E

T

A

V

A

A

V

A

-

F

-

W

-

H

-

S

R

V

L

R

V

H

K

A

A

R

G

P

A

I

S

T

I

I

I

G

G

L

V

N

N

C
|
C

A

H

L

F

G

D

-

P

-

T

-

I

-

S

-

L

-

K

-

T

A

V

A

K

L

L

M

M

R

K

P

E

Y

G

I

L

-

E

-

A

A

A

E

Q

L

L

S

K

K

A

I

H

A

L

D

M

T

S

R

Q

I

P

C

L

V

A

Y

Y

-

H

-

T

P

P

N

D

A

A

G

N

L

K

P

Q

N

G

-

F

-
x
I

P

D

M

L

S

P

D

E

T
x
F

G

P

F

F

D

G

E

L

T

E

P

P

D

R

V

V

T

A

S

T

R

R

L

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

F

Y

-

N

-

L

-

G

V

V

N

R

I

Y

A

I

G

G

C
|
C

G

G

T

F

T

E

P

P

E

Y

H

H

I

I

A

R

A

A

I

I

A

A

Q

E

A

E

V

L

A

A

binding s-(d-carboxybutyl)-l-homocysteine: F66 (= F96), E136 (≠ T192), Y137 (≠ I193), C194 (= C257), I239 (vs. gap), F244 (≠ T294), C276 (= C322), C277 (= C323)
binding zinc ion: C194 (= C257), C277 (= C323)

Sites not aligning to the query:

binding s-(d-carboxybutyl)-l-homocysteine: 18, 19, 20, 34

O09171 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Rattus norvegicus (Rat) (see 2 papers)
23% identity, 76% coverage: 70:338/353 of query aligns to 50:315/407 of O09171

query
sites
O09171

L

V

T

E

Q

H

P

P

E

E

V

A

I

V

A

R

E

Q

I

L

H

H

G

R

K

E

Y

F

L

L

A

R

A

A

G

G

A

S

D

N

I

V

I

M

E

Q

T
|
T

N
x
F

T

T

F

F

G
x
Y

A

A

T

S

S

E

-

D

-

K

-

L

V

E

A

N

Q

R

A

G

D

N

Y

Y

H

V

M

A

A

E

D

K

L

I

A

S

-

G

Y

Q

E

K

M

V

N

N

L

E

A

A

A

C

R

D

L

I

A

A

R

R

A

Q

E

V

C

A

D

D

K

E

Y

G

S

D

T

A

A

-

D

-

K

-

P

-

R

-

F

L

V

V

A
|
A

G

G

A

G

L

V

G

S

P

Q

T

T

P

P

K

S

T

Y

A

L

S

S

I

C

S

K

P

S

D

E

V

T

N

-

D

-

P

-

G

-

A

-

R

-

N

-

V

-

S

-

F

-

D

-

E

E

L

V

V

K

A

K

A

I

Y

F

H

H

E

Q

Q

Q

A

L

R

E

G

V

L

F

W

M

D

K

G

K

G

N

A

V

D

D

L

-

F

F

L

L

V

I

E

A

T
x
E

I

Y

F

F

D

E

T

-

L

-

N

H

A

V

K

E

A

E

A

A

L

V

F

W

A

A

I

V

D

E

Q

A

L

L

F

K

E

T

E

S

R

G

G

K

A

P

T

I

L

A

P

A

I
x
T

M

M

I
x
C

S

I

G

G

T

P

V

E

T

G

D

D

A

L

S

H

G

G

R

-

I

V

L

S

S

P

G

G

Q

E

T

C

V

A

A

V

A

-

F

-

W

-

H

-

S

R

V

L

R

V

H

K

A

A

R

G

P

A

I

A

T

I

I

V

G

G

L

V

N

N

C

C

-

H

-

F

-

D

-

P

-

S

-

T

-

S

-

L

-

Q

-

T

-

I

-

K

-

L

-

M

-

K

-

E

A

G

L

L

G

E

A

A

L

R

M

L

R

K

P

A

Y

Y

I

L

A

M

E

S

L

H

S

A

K

L

I

A

A

Y

D

H

T

T

R

P

I

D

C

C

V

-

Y

-

P

G

N

K

A

Q

G

G

L

F

P

I

N

D

P

-

M

L

S

P

D

E

T

F

G

P

F

F

D

G

E

L

T

E

P

P

D

R

V

V

T

A

S

T

R

R

L

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

F

Y

-

N

-

L

-

G

V

V

N

R

I

Y

A

I

G

G

C

C

G

G

T

F

T

E

P

P

E

Y

H

H

I

I

A

R

A

A

I

I

A

A

Q

E

A

E

V

L

A

A

T73 (= T93) mutation to G: Decreases the catalytic efficiency.
F74 (≠ N94) mutation to A: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine.
Y77 (≠ G97) mutation to A: Decreases the catalytic efficiency.
A119 (= A140) mutation to G: Decreases the catalytic efficiency.
E159 (≠ T192) mutation E->G,K: Loss of catalytic activity.
T184 (≠ I219) mutation to G: Decreases the catalytic efficiency.
C186 (≠ I221) mutation C->A,S: Decreases the catalytic efficiency. Increases the affinity for L-homocysteine.

Sites not aligning to the query:

7 K→A: Has no effect on tetramer assembly or catalytic efficiency.
8 K→A: Has no effect on tetramer assembly. Decreases the catalytic efficiency.
10 K→A: Has no effect on tetramer assembly. Decreases the catalytic efficiency. Alters nucleocytoplasmic distribution.
11 R→A: Has no effect on tetramer assembly.
21 mutation E->A,K: Decreases the catalytic efficiency. Increases the affinity for L-homocysteine.
26 mutation D->A,I: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine.

Q93088 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Homo sapiens (Human) (see 4 papers)
23% identity, 76% coverage: 70:338/353 of query aligns to 50:315/406 of Q93088

query
sites
Q93088

L

V

T

E

Q

H

P

P

E

E

V

A

I

V

A

R

E

Q

I

L

H

H

G

R

K

E

Y

F

L

L

A

R

A

A

G

G

A

S

D

N

I

V

I

M

E

Q

T

T

N

F

T

T

F

F

G

Y

A

A

T

S

S

E

-

D

-

K

-

L

V

E

A

N

Q

R

A

G

D

N

Y

Y

H

V

M

L

A

E

D

K

L

I

A

S

-

G

Y

Q

E

E

M

V

N

N

L

E

A

A

A

C

R

D

L

I

A

A

R

R

A

Q

E

V

C

A

D

D

K

E

Y

G

S

D

T

A

A

-

D

-

K

-

P

-

R

-

F

L

V

V

A

A

G

G

A

G

L

V

G

S

P

Q

T

T

P

P

K

S

T

Y

A

L

S

S

I

C

S

K

P

S

D

E

V

T

N

-

D

-

P

-

G

-

A

-

R

-

N

-

V

-

S

-

F

-

D

-

E

E

L

V

V

K

A

K

A

V

Y

F

H

L

E

Q

Q

Q

A

L

R

E

G

V

L

F

W

M

D

K

G

K

G

N

A

V

D

D

L

-

F

F

L

L

V

I

E

A

T

E

I

Y

F

F

D

E

T

-

L

-

N

H

A

V

K

E

A

E

A

A

L

V

F

W

A

A

I

V

D

E

Q

T

L

L

F

I

E

A

E

S

R

G

G

K

A

P

T

V

L

A

P

A

I

T

M

M

I

C

S

I

G

G

T

P

V

E

T

G

D

D

A

L

S

H

G

G

R

-

I

V

L

P

S

P

G

G

Q

E

T

C

V

A

A

V

A

R

F

L

W

-

H

-

S

-

V

V

R

K

H

A

A

G

R

A

P

S

I

I

T

-

I

I

G

G

L

V

N
|
N

C
|
C

-

H

-

F

-

D

-

P

-

T

-

I

-

S

-

L

-

K

-

T

-

V

-

K

-

L

-

M

-

K

-

E

A

G

L

L

G

E

A

A

L
x
R

M

L

R

K

P

A

Y

H

I

L

A

M

E

S

L

Q

S

P

K

L

I

A

A

Y

D

H

T

T

R

P

I

D

C

C

V

-

Y

-

P

N

N

K

A

Q

G

G

L

F

P

I

N

D

P

-

M

L

S

P

D

E

T

F

G

P

F

F

D

G

E

L

T

E

P

P

D

R

V

V

T

A

S

T

R

R

L

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

F

Y

-

N

-

L

-

G

V

V

N

R

I

Y

A

I

G

G

C
|
C

G

G

T

F

T
x
E

P

P

E

Y

H
|
H

I

I

A

R

A

A

I

I

A

A

Q

E

A

E

V

L

A

A

N216 (= N256) mutation N->A,C: Decreases the catalytic efficiency.
C217 (= C257) binding Zn(2+); mutation C->A,S,H: Impairs zinc ion binding. Loss of catalytic activity.
R239 (≠ L263) to Q: may decrease risk for coronary artery disease; dbSNP:rs3733890
C299 (= C322) binding Zn(2+); mutation C->A,S: Impairs zinc ion binding. Loss of catalytic activity.
C300 (= C323) binding Zn(2+); mutation C->A,S: Impairs zinc ion binding. Loss of catalytic activity.
E303 (≠ T326) mutation to A: Has no significant effect on catalytic activity.
H306 (= H329) mutation to A: Has no significant effect on catalytic activity.

Query Sequence

>WP_051377698.1 NCBI__GCF_000482785.1:WP_051377698.1
MTATSDLAARLADAMSRRILILDGAMGTMIQRYKLDEAAYRGARFADWQPADLAPGKQLF
LKGNNDLLVLTQPEVIAEIHGKYLAAGADIIETNTFGATSVAQADYHMADLAYEMNLAAA
RLARAECDKYSTADKPRFVAGALGPTPKTASISPDVNDPGARNVSFDELVAAYHEQARGL
WDGGADLFLVETIFDTLNAKAALFAIDQLFEERGATLPIMISGTVTDASGRILSGQTVAA
FWHSVRHARPITIGLNCALGAALMRPYIAELSKIADTRICVYPNAGLPNPMSDTGFDETP
DVTSRLLKEFAEAGFVNIAGGCCGTTPEHIAAIAQAVATVTPRRVPDLEQTAT

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