SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing H281DRAFT_02075 FitnessBrowser__Burk376:H281DRAFT_02075 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 12 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)
61% identity, 92% coverage: 23:349/356 of query aligns to 8:334/1227 of P13009

query
sites
P13009

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C247 (= C260) binding
C310 (= C325) binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
C311 (= C326) binding ; 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
756:760 binding
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
808 binding
810 S→A: Decreases activity by about 40%.
860 binding
946 binding
1134 binding
1189:1190 binding

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)
57% identity, 98% coverage: 1:349/356 of query aligns to 8:347/1265 of Q99707

query
sites
Q99707

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R61 (= R62) natural variant: R -> K
C255 (≠ T255) to Y: in dbSNP:rs1140598

Sites not aligning to the query:

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.

4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
56% identity, 92% coverage: 23:349/356 of query aligns to 6:307/611 of 4cczA

query
sites
4cczA

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Sites not aligning to the query:

binding (6s)-5,6,7,8-tetrahydrofolate: 336, 339, 342, 343, 344, 409, 430, 458, 497, 536, 538, 539, 542, 545, 551, 571

8g3hA Methionine synthase (see paper)
36% identity, 88% coverage: 27:340/356 of query aligns to 9:301/841 of 8g3hA

query
sites
8g3hA

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R

E

Y

L

F

A

A

K

Q

L

E

C

S

D

T

T

R

Y

F

V

V

S

A

C

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

L

T

P

P

A

E

D

E

T

L

S

A

G

R

L

W

L

H

K

L

E

K

F

F

A

V

E

T

A

E

G

Y

L

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

K

E

A

A

L

V

Sites not aligning to the query:

binding cobalamin: 328, 330, 331, 668, 672, 675, 685, 693, 720, 721, 722, 723, 724, 725, 726, 730, 767, 768, 769, 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)
31% identity, 90% coverage: 26:345/356 of query aligns to 10:292/560 of 3bofA

query
sites
3bofA

L

L

K

S

S

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

R

-

Y

-

R

-

G

-

E

-

R

-

F

-

K

-

D

-

Y

-

G

-

R

-

D

-

I

-

K

-

G

-

N

-

N

P

E

E

L

E

L

L

S

N

I

I

T

K

Q

A

P

P

Q

D

I

V

S

L

E

K

I

V

H

H

E

R

Q

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

T

R

V

M

A

K

Q

L

A

R

D

K

Y

H

G

G

M

L

E

E

A

D

L

K

A

L

V

D

E

P

M

I

N

V

L

R

Q

N

S

A

A

V

K

R

L

I

A

A

R

R

A

R

A

A

C

A

D

G

K

E

Y

-

S

-

T

-

P

-

D

-

K

-

P

-

R

K

F

L

V

V

A

F

G

G

A

D

I

I

G

G

P

P

T

T

P

G

K

E

T

L

A

-

S

-

I

-

S

-

P

-

D

-

V

-

N

-

D

-

P

P

G

Y

A

P

R

L

N

G

V

S

T

T

-

L

F

F

D

E

E

E

L

F

R

Y

A

E

A

N

Y

F

Y

R

E

E

Q

T

A

V

K

E

A

I

L

M

L

V

E

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

L

A

D

R

E

E

L

V

F

-

E

-

N

-

T

-

G

-

E

S

R

R

L

D

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

E

A

A

N

F

F

W

A

N

I

S

T

L

F

R

D

H

E

A

L

K

D

P

I

L

D

T

A

F

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

A

S

K

Q

L

Y

C

T

D

D

T

K

Y

F

V

L

S

V

C

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

L

K

P

P

A

H

D

D

T

F

S

A

G

V

L

H

L

I

K

D

E

S

F

Y

A

Y

E

E

A

L

G

G

L

-

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

K

K

A

V

L

L

A

G

E

N

V

R

K

K

P

P

binding zinc ion: C207 (= C260), C272 (= C325), C273 (= C326)

1q8jA Cobalamin-dependent methionine synthase (1-566) from thermotoga maritima (cd2+, hcy, methyltetrahydrofolate complex) (see paper)
31% identity, 90% coverage: 26:345/356 of query aligns to 10:292/559 of 1q8jA

query
sites
1q8jA

L

L

K

S

S

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

R

-

Y

-

R

-

G

-

E

-

R

-

F

-

K

-

D

-

Y

-

G

-

R

-

D

-

I

-

K

-

G

-

N

-

N

P

E

E

L

E

L

L

S

N

I

I

T

K

Q

A

P

P

Q

D

I

V

S

L

E

K

I

V

H

H

E

R

Q

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

T

R

V

M

A

K

Q

L

A

R

D

K

Y

H

G

G

M

L

E

E

A

D

L

K

A

L

V

D

E

P

M

I

N

V

L

R

Q

N

S

A

A

V

K

R

L

I

A

A

R

R

A

R

A

A

C

A

D

G

K

E

Y

-

S

-

T

-

P

-

D

-

K

-

P

-

R

K

F

L

V

V

A

F

G

G

A

D

I

I

G

G

P

P

T

T

P

G

K

E

T

L

A

-

S

-

I

-

S

-

P

-

D

-

V

-

N

-

D

-

P

P

G

Y

A

P

R

L

N

G

V

S

T

T

-

L

F

F

D

E

E

E

L

F

R

Y

A

E

A

N

Y

F

Y

R

E

E

Q

T

A

V

K

E

A

I

L

M

L

V

E

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

L

A

D

R

E

E

L

V

F

-

E

-

N

-

T

-

G

-

E

S

R

R

L

D

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

E

A

A

N

F

F

W

A

N

I

S

T

L

F

R

D

H

E

A

L

K

D

P

I

L

D

T

A

F

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

A

S

K

Q

L

Y

C

T

D

D

T

K

Y

F

V

L

S

V

C

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

L

K

P

P

A

H

D

D

T

F

S

A

G

V

L

H

L

I

K

D

E

S

F

Y

A

Y

E

E

A

L

G

G

L

-

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

K

K

A

V

L

L

A

G

E

N

V

R

K

K

P

P

Sites not aligning to the query:

binding 5-methyl-5,6,7,8-tetrahydrofolic acid: 320, 323, 325, 327, 390, 411, 435, 473, 505, 507, 508, 511, 516, 536

5dmmA Crystal structure of the homocysteine methyltransferase mmum from escherichia coli, metallated form (see paper)
28% identity, 88% coverage: 23:336/356 of query aligns to 3:284/288 of 5dmmA

query
sites
5dmmA

L

L

P

R

A

A

L

L

-

D

K

K

S

Q

R

D

I

I

L

L

I

L

L

L

D

D

G

G

A

A

M

M

G

A

T

T

M

-

I

-

Q

-

R

-

Y

-

K

-

L

-

D

-

E

E

A

L

R

E

Y

A

R

R

G

G

E

C

R

N

F

L

K

A

D

D

Y

S

G

L

R

W

D

S

I

A

K

K

G

-

N

-

E

-

L

-

L

V

S

L

I

V

T

E

Q

N

P

P

Q

E

I

L

I

I

S

R

E

E

I

V

H

H

E

L

Q

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

T

P

V

A

A

G

Q

F

A

A

D

A

Y

R

G

G

M

L

-

D

E

E

A

A

L

Q

A

S

V

K

E

A

M

L

N

I

L

G

Q

K

S

S

A

V

K

E

L

L

A

A

R

R

A

K

A

A

C

R

D

E

K

A

Y

Y

S

-

T

L

P

A

D

E

K

N

P

P

R

Q

-

A

-

G

-

T

-

L

F

L

V

V

A

A

G

G

A

S

I

V

G

G

P

-

T

-

P

P

K

Y

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

T

S

F

V

D

E

E

A

L

F

R

Q

A

A

A

F

Y

H

Y

R

E

P

Q

R

A

V

K

E

A

A

L

L

E

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

-

L

-

D

-

E

-

L

-

F

-

E

-

N

T

T

A

G

Y

E

P

R

R

L

A

P

R

I

A

M

W

I

F

S

S

G

F

T

T

V

L

T

R

D

D

A

-

S

S

G

E

R

H

I

L

L

S

S

D

G

G

Q

T

T

P

V

L

E

R

A

D

F

V

W

V

N

A

S

L

L

L

R

A

-

G

H

Y

A

P

K

Q

P

V

L

V

T

A

F

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

A

H

K

G

L

L

C

T

D

V

T

L

Y

P

V

L

S

V

C

V

Y

Y

P

P

N

N

A

S

G

G

L

-

P

-

N

-

P

-

M

-

S

-

D

-

T

-

G

-

F

-

D

-

E

-

L

-

P

-

A

-

D

Q

T

L

S

A

G

D

L

Y

L

L

K

P

E

Q

F

W

A

Q

E

A

A

A

G

G

L

-

V

A

N

R

I

L

A

I

G

G

C
|
C

G

R

T

T

P

P

E

A

H

D

I

I

A

A

I

L

binding zinc ion: D134 (≠ A164), H136 (≠ N166), C225 (= C260), C273 (= C325), C274 (= C326)

Q93088 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Homo sapiens (Human) (see 4 papers)
24% identity, 76% coverage: 72:341/356 of query aligns to 49:315/406 of Q93088

query
sites
Q93088

S

A

I

V

T

E

Q

H

P

P

Q

E

I

A

I

V

S

R

E

Q

I

L

H

H

E

R

Q

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

T

E

V

D

A

K

-

L

-

E

-

N

Q

R

A

G

D

N

Y

Y

G

V

M

L

E

E

A

K

L

I

A

S

-

G

V

Q

E

E

M

V

N

N

L

E

Q

A

S

A

A

C

K

D

L

I

A

A

R

R

A

Q

A

V

C

A

D

D

K

E

Y

G

S

D

T

A

P

-

D

-

K

-

P

-

R

-

F

L

V

V

A

A

G

G

A

G

I

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

-

T

-

F

-

D

-

E

E

L

V

R

K

A

K

A

V

Y

F

Y

L

E

Q

Q

Q

A

L

K

E

A

V

L

F

L

M

E

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

L

V

D

E

E

T

L

L

F

I

E

A

N

S

T

G

G

K

E

P

R

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

E

-

A

-

F

-

W

-

N

V

S

R

L

L

R

V

H

K

A

A

K

G

P

A

L

S

T

I

F

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

A

-

E

E

L

A

A

A

K
x
R

L

L

C

-

D

K

T

A

Y

H

V

L

S

M

C

S

Y

Q

P

P

N

L

A

A

G

Y

L

H

P

T

N

P

P

D

M

C

S

N

D

K

T

Q

G

G

F

F

D

I

E

D

L

L

P

P

A

E

D

F

T

P

S

F

G

G

L

L

-

E

-

P

-

R

-

V

-

A

-

T

-

R

-

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

L

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

K

E

A

E

L

L

A

A

N216 (= N259) mutation N->A,C: Decreases the catalytic efficiency.
C217 (= C260) binding ; mutation C->A,S,H: Impairs zinc ion binding. Loss of catalytic activity.
R239 (≠ K276) to Q: may decrease risk for coronary artery disease; dbSNP:rs3733890
C299 (= C325) binding ; mutation C->A,S: Impairs zinc ion binding. Loss of catalytic activity.
C300 (= C326) binding ; mutation C->A,S: Impairs zinc ion binding. Loss of catalytic activity.
E303 (≠ T329) mutation to A: Has no significant effect on catalytic activity.
H306 (= H332) mutation to A: Has no significant effect on catalytic activity.

O09171 Betaine--homocysteine S-methyltransferase 1; EC 2.1.1.5 from Rattus norvegicus (Rat) (see 2 papers)
24% identity, 76% coverage: 72:341/356 of query aligns to 49:315/407 of O09171

query
sites
O09171

S

A

I

V

T

E

Q

H

P

P

Q

E

I

A

I

V

S

R

E

Q

I

L

H

H

E

R

Q

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

T

E

V

D

A

K

Q

L

A

E

D

N

Y

R

G

G

M

N

E

-

A

-

L

-

A

Y

V

V

E

A

M

E

N

K

L

I

Q

S

S

G

A

Q

K

K

L

V

A

N

R

E

A

A

C

C

D

D

-

I

-

A

K

R

Y

Q

S

V

T

A

P

D

D

E

K

G

P

D

R

A

F

L

V

V

A
|
A

G

G

A

G

I

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

-

T

-

F

-

D

-

E

E

L

V

R

K

A

K

A

I

Y

F

Y

H

E

Q

Q

Q

A

L

K

E

A

V

L

F

L

M

E

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

L

V

D

E

E

A

L

L

F

K

E

T

N

S

T

G

G

K

E

P

R

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

E

-

A

-

F

-

W

-

N

V

S

R

L

L

R

V

H

K

A

A

K

G

P

A

L

A

T

I

F

V

G

G

L

V

N

N

C

C

A

H

L

F

G

D

A

P

A

S

-

T

-

S

-

L

-

Q

-

T

-

I

-

K

L

L

M

M

R

K

P

E

Y

G

I

L

A

-

E

E

L

A

A

A

K

R

L

L

C

-

D

K

T

A

Y

Y

V

L

S

M

C

S

Y

H

P

A

N

L

A

A

G

Y

L

H

P

T

N

P

P

D

M

C

S

G

D

K

T

Q

G

G

F

F

D

I

E

D

L

L

P

P

A

E

D

F

T

P

S

F

G

G

L

L

-

E

-

P

-

R

-

V

-

A

-

T

-

R

-

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

L

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

K

E

A

E

L

L

A

A

T73 (= T96) mutation to G: Decreases the catalytic efficiency.
F74 (≠ N97) mutation to A: Decreases the catalytic efficiency. Decreases the affinity for glycine betaine.
Y77 (≠ G100) mutation to A: Decreases the catalytic efficiency.
A119 (= A143) mutation to G: Decreases the catalytic efficiency.
E159 (≠ T195) mutation E->G,K: Loss of catalytic activity.
T184 (≠ I222) mutation to G: Decreases the catalytic efficiency.
C186 (≠ I224) 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.

1lt8A Reduced homo sapiens betaine-homocysteine s-methyltransferase in complex with s-(delta-carboxybutyl)-l-homocysteine (see paper)
24% identity, 76% coverage: 72:341/356 of query aligns to 39:292/348 of 1lt8A

query
sites
1lt8A

S

A

I

V

T

E

Q

H

P

P

Q

E

I

A

I

V

S

R

E

Q

I

L

H

H

E

R

Q

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

-

V

-

A

-

Q

-

A

-

D

-

Y
|
Y

G

A

M

S

E

E

A

D

L

K

A

G

V

Q

E

E

M

V

N

N

L

E

Q

A

S

A

A

A

K

D

L

I

A

A

R

R

A

Q

A

V

C

A

D

D

K

E

Y

G

S

D

T

A

P

-

D

-

K

-

P

-

R

-

F

L

V

V

A

A

G

G

A

G

I

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

-

T

-

F

-

D

-

E

E

L

V

R

K

A

K

A

V

Y

F

Y

L

E

Q

Q

Q

A

L

K

E

A

V

L

F

L

M

E

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

L

V

D

E

E

T

L

L

F

I

E

A

N

S

T

G

G

K

E

P

R

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

E

-

A

-

F

-

W

-

N

V

S

R

L

L

R

V

H

K

A

A

K

G

P

A

L

S

T

I

F

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

A

-

E

E

L

A

A

A

K

Q

L

L

C

-

D

K

T

A

Y

H

V

L

S

M

C

S

Y

Q

P

P

N

L

A

A

G

Y

L

H

P

T

N

P

P

D

M

A

S

N

D

K

T

Q

G

G

F

F

D
x
I

E

D

L

L

P

P

A

E

D
x
F

T

P

S

F

G

G

L

L

-

E

-

P

-

R

-

V

-

A

-

T

-

R

-

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

L

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

K

E

A

E

L

L

A

A

binding s-(d-carboxybutyl)-l-homocysteine: F66 (= F99), Y67 (= Y109), E136 (≠ T195), Y137 (≠ I196), C194 (= C260), I239 (≠ D300), F244 (≠ D305), C276 (= C325), C277 (= C326)
binding zinc ion: C194 (= C260), C277 (= C326)

Sites not aligning to the query:

binding s-(d-carboxybutyl)-l-homocysteine: 17, 18, 19, 20, 34

1umyD Bhmt from rat liver (see paper)
24% identity, 76% coverage: 72:341/356 of query aligns to 40:292/381 of 1umyD

query
sites
1umyD

S

A

I

V

T

E

Q

H

P

P

Q

E

I

A

I

V

S

R

E

Q

I

L

H

H

E

R

Q

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

T

I

V

S

A

G

Q

Q

A

-

D

-

Y

-

G

-

M

-

E

-

A

-

L

-

A

-

V

-

E

-

M

-

N

-

L

-

Q

-

S

-

A

-

K

K

L

V

A

N

R

E

A

A

C

C

D

D

-

I

-

A

K

R

Y

Q

S

V

T

A

P

D

D

E

K

G

P

D

R

A

F

L

V

V

A

A

G

G

A

G

I

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

-

T

-

F

-

D

-

E

E

L

V

R

K

A

K

A

I

Y

F

Y

H

E

Q

Q

Q

A

L

K

E

A

V

L

F

L

M

E

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

L

V

D

E

E

A

L

L

F

K

E

T

N

S

T

G

G

K

E

P

R

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

E

-

A

-

F

-

W

-

N

V

S

R

L

L

R

V

H

K

A

A

K

G

P

A

L

A

T

I

F

V

G

G

L

V

N

N

C

C

A

H

L

F

G

D

A

P

A

S

-

T

-

S

-

L

-

Q

-

T

-

I

-

K

L

L

M

M

R

K

P

E

Y

G

I

L

A

-

E

E

L

A

A

A

K

R

L

L

C

-

D

K

T

A

Y

Y

V

L

S

M

C

S

Y

Q

P

P

N

L

A

A

G

Y

L

H

P

T

N

P

P

D

M

C

S

G

D

K

T

Q

G

G

F

F

D

I

E

D

L

L

P

P

A

E

D

F

T

P

S

F

G

G

L

L

-

E

-

P

-

R

-

V

-

A

-

T

-

R

-

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

L

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

K

E

A

E

L

L

A

A

binding zinc ion: C276 (= C325), C277 (= C326)

Sites not aligning to the query:

binding zinc ion: 380, 381

4m3pA Betaine-homocysteine s-methyltransferase from homo sapiens complexed with homocysteine (see paper)
23% identity, 76% coverage: 72:341/356 of query aligns to 40:284/370 of 4m3pA

query
sites
4m3pA

S

A

I

V

T

E

Q

H

P

P

Q

E

I

A

I

V

S

R

E

Q

I

L

H

H

E

R

Q

E

Y

F

L

L

A

R

A

A

G

G

A

S

D

N

I

V

I

M

E
x
Q

T

T

N

F

T

T

F

F

G

Y

A

S

T

G

T

Q

V

-

A

-

Q

-

A

-

D

-

Y

-

G

-

M

-

E

-

A

-

L

-

A

-

V

-

E

E

M

V

N

N

L

E

Q

A

S

A

A

C

K

D

L

I

A

A

R

R

A

Q

A

V

C

A

D

D

K

E

Y

G

S

D

T

A

P

-

D

-

K

-

P

-

R

-

F

L

V

V

A

A

G

G

A

G

I

V

G

S

P

Q

T

T

P

P

K

K

T

S

A

E

S

T

I

-

S

-

P

-

D

-

V

-

N

-

D

-

P

-

G

-

A

-

R

-

N

-

V

-

T

-

F

-

D

-

E

E

L

V

R

K

A

K

A

V

Y

F

Y

L

E

Q

Q

Q

A

L

K

E

A

V

L

F

L

M

E

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

L

V

D

E

E

T

L

L

F

I

E

A

N

S

T

G

G

K

E

P

R

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

E

-

A

-

F

-

W

-

N

V

S

R

L

L

R

V

H

K

A

A

K

G

P

A

L

S

T

I

F

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

A

-

E

E

L

A

A

A

K

Q

L

L

C

-

D

K

T

A

Y

H

V

L

S

M

C

S

Y
x
Q

P

P

N

L

A

A

G

Y

L

H

P

T

N

P

P

D

M

C

S

N

D

K

T

Q

G

G

F

F

D

I

E

D

L

L

P

P

A

E

D

F

T

P

S

F

G

G

L

L

-

E

-

P

-

R

-

V

-

A

-

T

-

R

-

W

-

D

L

I

K

Q

E

K

F

Y

A

A

E

R

A

E

G

A

L

Y

-

N

-

L

-

G

V

V

N

R

I

Y

A

I

G

G

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

K

E

A

E

L

L

A

A

binding potassium ion: Q63 (≠ E95), Q216 (≠ Y285), G267 (= G324)
binding zinc ion: C186 (= C260), C268 (= C325), C269 (= C326)

Sites not aligning to the query:

binding potassium ion: 17, 18

Query Sequence

>H281DRAFT_02075 FitnessBrowser__Burk376:H281DRAFT_02075
MNQPAQTAKPVRPELAYTRGTALPALLKSRILILDGAMGTMIQRYKLDEARYRGERFKDY
GRDIKGNNELLSITQPQIISEIHEQYLAAGADIIETNTFGATTVAQADYGMEALAVEMNL
QSAKLARAACDKYSTPDKPRFVAGAIGPTPKTASISPDVNDPGARNVTFDELRAAYYEQA
KALLEGGADLFLVETIFDTLNAKAALFALDELFENTGERLPIMISGTVTDASGRILSGQT
VEAFWNSLRHAKPLTFGLNCALGAALMRPYIAELAKLCDTYVSCYPNAGLPNPMSDTGFD
ELPADTSGLLKEFAEAGLVNIAGGCCGTTPEHIAAIAKALAEVKPRKWPTQYRDAA

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