SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010964255.1 NCBI__GCF_000008765.1:WP_010964255.1 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 10 hits to proteins with known functional sites (download)

4g09A The crystal structure of the c366s mutant of hdh from brucella suis in complex with a substituted benzyl ketone (see paper)
49% identity, 93% coverage: 32:430/431 of query aligns to 23:422/432 of 4g09A

query
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active site: Q253 (= Q261), H256 (= H264), E321 (= E329), H322 (= H330), D355 (= D363), H414 (= H422)
binding (3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one: P126 (= P133), A130 (= A137), Y132 (= Y139), S134 (= S141), H256 (= H264), E321 (= E329), H322 (= H330), D355 (= D363), Y356 (= Y364), H362 (= H370)
binding zinc ion: H256 (= H264), D307 (≠ S315), D310 (≠ R318), D355 (= D363)

6an0A Crystal structure of histidinol dehydrogenase from elizabethkingia anophelis
43% identity, 96% coverage: 19:431/431 of query aligns to 17:429/433 of 6an0A

query
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active site: Q260 (= Q261), H263 (= H264), E327 (= E329), H328 (= H330), D361 (= D363), H420 (= H422)
binding histidine: E103 (≠ Q105), N104 (= N106), K105 (≠ S107), R118 (= R120), E119 (≠ T121), A120 (≠ V122), K390 (= K392)
binding zinc ion: H263 (= H264), D361 (= D363)

1karA L-histidinol dehydrogenase (hisd) structure complexed with histamine (inhibitor), zinc and NAD (cofactor) (see paper)
41% identity, 98% coverage: 7:429/431 of query aligns to 3:423/431 of 1karA

query
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1karA

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R

active site: Q256 (= Q261), H259 (= H264), E323 (= E329), H324 (= H330), D357 (= D363), H416 (= H422)
binding histamine: S137 (= S141), H259 (= H264), D357 (= D363), Y358 (= Y364), H364 (= H370)
binding zinc ion: H259 (= H264), D357 (= D363)

1kahA L-histidinol dehydrogenase (hisd) structure complexed with l-histidine (product), zn and NAD (cofactor) (see paper)
41% identity, 98% coverage: 7:429/431 of query aligns to 3:423/431 of 1kahA

query
sites
1kahA

I

I

I

I

Q

D

D

W

G

N

S

S

L

C

D

T

G

A

E

E

K

Q

Y

Q

F

R

Q

Q

S

L

L

L

K

M

E

R

R

P

Q

A

G

I

K

S

E

A

N

S

A

E

E

S

I

I

I

T

K

R

T

T

V

V

K

N

F

D

I

I

I

L

D

D

N

N

V

V

K

K

E

A

N

R

G

G

D

D

K

E

A

A

L

L

I

R

E

E

Y

Y

T

S

S

A

K

K

F

F

D

D

K

K

V

T

E

T

L

V

Q

T

S

A

I

L

E

K

V

V

T

S

K

A

E

E

E

E

I

I

K

A

A

A

A

A

Y

S

S

E

K

R

V

L

E

S

N

D

D

E

F

L

I

K

C

Q

A

A

L

M

K

A

T

V

A

A

K

V

E

K

N

N

I

I

E

E

E

T

Y

F

H

H

S

T

K

A

Q

Q

V

K

Q

L

N

P

S

P

Y

V

V

D

I

V

T

E

K

T

E

Q

N

P

G

G

I

V

V

R

M

C

G

Q

R

Q

T

V

V

T

R

R

G

P

L

V

D

A

K

S

V

V

G

G

I

L

Y

Y

V

I

P

P

G

G

G

G

T

S

A

A

A

P

Y
x
L

P

F

S

S

S

T

V

V

I

L

M

M

N

L

A

A

V

T

P

P

A

A

K

S

V

I

A

A

G

G

V

C

N

K

K

K

I

V

I

V

M

L

T

C

T

S

P

P

P

P

M

P

K

-

D

-

G

-

F

-

V

I

N

A

P

D

S

E

I

I

L

L

V

Y

A

A

A

A

D

Q

L

L

A

C

G

G

V

V

D

Q

K

D

I

V

Y

F

K

N

V

V

G

G

G

G

A

A

Q

Q

A

A

I

I

A

A

A

A

L

L

A

A

F

F

G

G

T

T

E

E

T

S

I

V

D

P

K

K

V

V

D

D

K

K

I

I

V

F

G

G

P

P

G

G

N

N

I

A

F

F

V

V

A

T

M

E

A

A

K

K

K

R

S

Q

V

V

Y

S

G

Q

F

R

V

L

D

D

-

G

-

A

-

A

I

I

D

D

M

M

I

P

A

A

G

G

P

P

S

S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

S

T

G

G

A

N

T

P

P

K

D

F

F

I

V

A

A

A

S

D

D

L

L

M

L

S

S

Q
|
Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

I

L

L

V

L

T

T

T

P

S

A

K

A

E

D

L

M

I

A

G

R

K

R

V

V

I

A

E

E

E

A

I

V

K

E

L

R

Q

Q

V

L

E

A

G

E

L

L

S

P

R

R

K

A

E

E

I

T

I

A

L

R

E

Q

A

A

L

L

R

-

N

N

F

A

G

S

A

R

I

L

I

I

L

V

V

T

D

K

S

D

I

L

S

A

R

Q

A

C

I

V

E

E

I

I

G

S

N

N

V

Q

V

Y

A

G

P

P

E
|
E

H
|
H

L

L

E

I

I

I

I

Q

T

T

P

R

N

N

P

A

F

R

E

E

Y

L

L

V

N

D

D

S

I

I

K

T

N

S

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

D

Y

W

S

S

P

P

E

E

P

S

L

A

G

G

D
|
D

Y
|
Y

M

A

A

S

G

G

P

T

N

N

H
|
H

V

V

L

L

P

P

T

T

S

Y

G

G

T

Y

A

T

R

A

F

T

S

C

S

S

P

S

L

L

S

G

V

L

D

A

D

D

F

F

V

Q

K

K

K

R

S

M

S

T

Y

V

L

Q

Y

E

Y

L

S

S

E

K

K

E

A

G

L

F

R

S

N

A

V

L

N

A

D

S

K

T

V

I

V

E

K

T

I

L

A

A

E

A

T

A

E
|
E

G

R

L
|
L

T

T

A

A

H
|
H

A

K

N

N

S

A

I

V

K

T

V

L

R

R

active site: Q256 (= Q261), H259 (= H264), E323 (= E329), H324 (= H330), D357 (= D363), H416 (= H422)
binding histidine: L135 (≠ Y139), H259 (= H264), H324 (= H330), D357 (= D363), Y358 (= Y364), H364 (= H370), E411 (= E417), L413 (= L419), H416 (= H422)
binding zinc ion: H259 (= H264), D357 (= D363)

1kaeA L-histidinol dehydrogenase (hisd) structure complexed with l- histidinol (substrate), zinc and NAD (cofactor) (see paper)
41% identity, 98% coverage: 7:429/431 of query aligns to 6:426/434 of 1kaeA

query
sites
1kaeA

I

I

I

I

Q

D

D

W

G

N

S

S

L

C

D

T

G

A

E

E

K

Q

Y

Q

F

R

Q

Q

S

L

L

L

K

M

E

R

R

P

Q

A

G

I

K

S

E

A

N

S

A

E

E

S

I

I

I

T

K

R

T

T

V

V

K

N

F

D

I

I

I

L

D

D

N

N

V

V

K

K

E

A

N

R

G

G

D

D

K

E

A

A

L

L

I

R

E

E

Y

Y

T

S

S

A

K

K

F
|
F

D

D

K

K

V

T

E

T

L

V

Q

T

S

A

I

L

E

K

V

V

T

S

K

A

E

E

E

E

I

I

K

A

A

A

A

A

Y

S

S

E

K

R

V

L

E

S

N

D

D

E

F

L

I

K

C

Q

A

A

L

M

K

A

T

V

A

A

K

V

E

K

N

N

I

I

E

E

E

T

Y

F

H

H

S

T

K

A

Q

Q

V

K

Q

L

N

P

S

P

Y

V

V

D

I

V

T

E

K

T

E

Q

N

P

G

G

I

V

V

R

M

C

G

Q

R

Q

T

V

V

T

R

R

G

P

L

V

D

A

K

S

V

V

G

G

I

L

Y
|
Y

V

I

P
|
P

G

G

G

G

T

S

A

A

A

P

Y

L

P

F

S

S

S

T

V

V

I

L

M

M

N

L

A

A

V

T

P

P

A

A

K

S

V

I

A

A

G

G

V

C

N

K

K

K

I

V

I

V

M

L

T

C

T

S

P
|
P

P

P

M

P

K

-

D

-

G

-

F

-

V

I

N

A

P

D

S

E

I

I

L

L

V

Y

A

A

A

A

D

Q

L

L

A

C

G

G

V

V

D

Q

K

D

I

V

Y

F

K

N

V

V

G

G

G
|
G

A

A

Q

Q

A

A

I

I

A

A

A

A

L

L

A

A

F

F

G

G

T

T

E

E

T

S

I

V

D

P

K

K

V

V

D

D

K

K

I

I

V

F

G

G

P
|
P

G
|
G

N
|
N

I

A

F
|
F

V

V

A

T

M

E

A

A

K

K

K

R

S

Q

V

V

Y

S

G

Q

F

R

V

L

D

D

-

G

-

A

-

A

I

I

D

D

M

M

I

P

A

A

G

G

P

P

S

S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

S

T

G

G

A

N

T

P

P

K

D

F

F

I

V

A

A

A

S

D

D

L

L

M

L

S

S

Q
|
Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

I

L

L

V

L

T

T

T

P

S

A

K

A

E

D

L

M

I

A

G

R

K

R

V

V

I

A

E

E

E

A

I

V

K

E

L

R

Q

Q

V

L

E

A

G

E

L

L

S

P

R

R

K

A

E

E

I

T

I

A

L

R

E

Q

A

A

L

L

R

-

N

N

F

A

G

S

A

R

I

L

I

I

L

V

V

T

D

K

S

D

I

L

S

A

R

Q

A

C

I

V

E

E

I

I

G

S

N

N

V

Q

V

Y

A

G

P

P

E
|
E

H
|
H

L

L

E

I

I

I

I

Q

T

T

P

R

N

N

P

A

F

R

E

E

Y

L

L

V

N

D

D

S

I

I

K

T

N

S

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

D

Y

W

S

S

P

P

E

E

P

S

L

A

G

G

D
|
D

Y
|
Y

M

A

A

S

G

G

P

T

N

N

H
|
H

V

V

L

L

P

P

T

T

S

Y

G

G

T

Y

A

T

R

A

F

T

S

C

S

S

P

S

L

L

S

G

V

L

D

A

D

D

F

F

V

Q

K

K

K

R

S

M

S

T

Y

V

L

Q

Y

E

Y

L

S

S

E

K

K

E

A

G

L

F

R

S

N

A

V

L

N

A

D

S

K

T

V

I

V

E

K

T

I

L

A

A

E

A

T

A

E

E

G

R

L

L

T

T

A

A

H
|
H

A

K

N

N

S

A

I

V

K

T

V

L

R

R

active site: Q259 (= Q261), H262 (= H264), E326 (= E329), H327 (= H330), D360 (= D363), H419 (= H422)
binding L-histidinol: H262 (= H264), H327 (= H330), D360 (= D363), Y361 (= Y364), H367 (= H370)
binding nicotinamide-adenine-dinucleotide: F58 (= F59), Y130 (= Y131), P132 (= P133), P162 (= P163), G186 (= G191), P209 (= P214), G210 (= G215), N211 (= N216), F213 (= F218), H262 (= H264)
binding zinc ion: Q259 (= Q261), H262 (= H264), D360 (= D363)

P06988 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Escherichia coli (strain K12) (see 2 papers)
41% identity, 98% coverage: 7:429/431 of query aligns to 6:426/434 of P06988

query
sites
P06988

I

I

I

I

Q

D

D

W

G

N

S

S

L

C

D

T

G

A

E

E

K

Q

Y

Q

F

R

Q

Q

S

L

L

L

K

M

E

R

R

P

Q

A

G

I

K

S

E

A

N

S

A

E

E

S

I

I

I

T

K

R

T

T

V

V

K

N

F

D

I

I

I

L

D

D

N

N

V

V

K

K

E

A

N

R

G

G

D

D

K

E

A

A

L

L

I

R

E

E

Y

Y

T

S

S

A

K

K

F

F

D

D

K

K

V

T

E

T

L

V

Q

T

S

A

I

L

E

K

V

V

T

S

K

A

E

E

E

E

I

I

K

A

A

A

A

A

Y

S

S

E

K

R

V

L

E

S

N

D

D

E

F

L

I

K

C

Q

A

A

L

M

K

A

T

V

A

A

K

V

E

K

N

N

I

I

E

E

E

T

Y

F

H

H

S

T

K

A

Q

Q

V

K

Q

L

N

P

S

P

Y

V

V

D

I

V

T

E

K

T

E

Q

N

P

G

G

I

V

V

R

M

C

G

Q

R

Q

T

V

V

T

R

R

G

P

L

V

D

A

K

S

V

V

G

G

I

L

Y
|
Y

V

I

P

P

G

G

G

G

T

S

A

A

A

P

Y

L

P

F

S

S

S

T

V

V

I

L

M

M

N

L

A

A

V

T

P

P

A

A

K

S

V

I

A

A

G

G

V

C

N

K

K

K

I

V

I

V

M

L

T

C

T

S

P

P

P

P

M

P

K

-

D

-

G

-

F

-

V

I

N

A

P

D

S

E

I

I

L

L

V

Y

A

A

A

A

D

Q

L

L

A

C

G

G

V

V

D

Q

K

D

I

V

Y

F

K

N

V

V

G

G

G

G

A

A

Q
|
Q

A

A

I

I

A

A

A

A

L

L

A

A

F

F

G

G

T

T

E

E

T

S

I

V

D

P

K

K

V

V

D

D

K

K

I

I

V

F

G

G

P

P

G

G

N
|
N

I

A

F

F

V

V

A

T

M

E

A

A

K

K

K

R

S

Q

V

V

Y

S

G

Q

F

R

V

L

D

D

-

G

-

A

-

A

I

I

D

D

M

M

I

P

A

A

G

G

P

P

S

S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

S

T

G

G

A

N

T

P

P

K

D

F

F

I

V

A

A

A

S

D

D

L

L

M

L

S

S

Q
|
Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

I

L

L

V

L

T

T

T

P

S

A

K

A

E

D

L

M

I

A

G

R

K

R

V

V

I

A

E

E

E

A

I

V

K

E

L

R

Q

Q

V

L

E

A

G

E

L

L

S

P

R

R

K

A

E

E

I

T

I

A

L

R

E

Q

A

A

L

L

R

-

N

N

F

A

G

S

A

R

I

L

I

I

L

V

V

T

D

K

S

D

I

L

S

A

R

Q

A

C

I

V

E

E

I

I

G

S

N

N

V

Q

V

Y

A

G

P

P

E

E

H

H

L

L

E

I

I

I

I

Q

T

T

P

R

N

N

P

A

F

R

E

E

Y

L

L

V

N

D

D

S

I

I

K

T

N

S

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

D

Y

W

S

S

P

P

E

E

P

S

L

A

G

G

D
|
D

Y

Y

M

A

A

S

G

G

P

T

N

N

H

H

V

V

L

L

P

P

T

T

S

Y

G

G

T

Y

A

T

R

A

F

T

S

C

S

S

P

S

L

L

S

G

V

L

D

A

D

D

F

F

V

Q

K

K

K

R

S

M

S

T

Y

V

L

Q

Y

E

Y

L

S

S

E

K

K

E

A

G

L

F

R

S

N

A

V

L

N

A

D

S

K

T

V

I

V

E

K

T

I

L

A

A

E

A

T

A

E

E

G

R

L

L

T

T

A

A

H
|
H

A

K

N

N

S

A

I

V

K

T

V

L

R

R

Y130 (= Y131) binding NAD(+)
Q188 (= Q193) binding NAD(+)
N211 (= N216) binding NAD(+)
Q259 (= Q261) binding Zn(2+)
H262 (= H264) binding Zn(2+)
D360 (= D363) binding Zn(2+)
H419 (= H422) binding Zn(2+)

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

P10370 Histidinol dehydrogenase; HDH; EC 1.1.1.23 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
42% identity, 92% coverage: 33:429/431 of query aligns to 32:426/434 of P10370

query
sites
P10370

I

I

I

T

K

R

T

T

V

V

K

S

F

D

I

I

I

L

D

D

N

N

V

V

K

K

E

T

N

R

G

G

D

D

K

D

A

A

L

L

I

R

E

E

Y

Y

T

S

S

A

K

K

F

F

D

D

K

K

V

T

E

E

L

V

Q

T

S

A

I

L

E

R

V

V

T

T

K

P

E

E

E

E

I

I

K

A

A

A

A

A

Y

G

S

A

K

R

V

L

E

S

N

D

D

E

F

L

I

K

C

Q

A

A

L

M

K

T

T

A

A

A

K

V

E

K

N

N

I

I

E

E

E

T

Y

F

H
|
H

S

S

K

A

Q

Q

V

T

Q

L

N

P

S

P

Y

V

V

D

I

V

T

E

K

T

E

Q

N

P

G

G

I

V

V

R

M
x
C

G

Q

R

Q

T

V

V

T

R

R

G

P

L

V

D

S

K

S

V

V

G

G

I

L

Y

Y

V

I

P

P

G

G

G

G

T

S

A

A

A

P

Y

L

P

F

S

S

S

T

V

V

I

L

M

M

N

L

A

A

V

T

P

P

A

A

K

R

V

I

A

A

G

G

V
x
C

N

Q

K

K

I

V

I

V

M

L

T

C

T

S

P

P

P

P

M

P

K

-

D

-

G

-

F

-

V

I

N

A

P

D

S

E

I

I

L

L

V

Y

A

A

A

A

D

Q

L

L

A

C

G

G

V

V

D

Q

K

E

I

I

Y

F

K

N

V

V

G

G

G

G

A

A

Q

Q

A

A

I

I

A

A

A

A

L

L

A

A

F

F

G

G

T

S

E

E

T

S

I

V

D

P

K

K

V

V

D

D

K

K

I

I

V

F

G

G

P

P

G

G

N

N

I

A

F

F

V

V

A

T

M

E

A

A

K

K

K

R

S

Q

V

V

Y

S

G

Q

F

R

V

L

D

D

-

G

-

A

-

A

I

I

D

D

M

M

I

P

A

A

G

G

P

P

S

S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

S

T

G

G

A

N

T

P

P

K

D

F

F

I

V

A

A

A

S

D

D

L

L

M

L

S

S

Q

Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

I

L

L

V

L

T

T

T

P

S

D

K

A

E

D

L

I

I

A

G

R

K

K

V

V

I

A

E

E

E

A

I

V

K

E

L

R

Q

Q

V

L

E

A

G

E

L

L

S

P

R

R

K

A

E

D

I

T

I

A

L

R

E

Q

A

A

L

L

R

-

N

S

F

A

G

S

A

R

I

L

I

I

L

V

V

T

D

K

S

D

I

L

S

A

R

Q

A

C

I

V

E

A

I

I

G

S

N

N

V

Q

V

Y

A

G

P

P

E

E

H
|
H

L

L

E

I

I

I

I

Q

T

T

P

R

N

N

P

A

F

R

E

D

Y

L

L

V

N

D

D

A

I

I

K

T

N

S

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

D

Y

W

S

S

P

P

E

E

P

S

L

A

G

G

D

D

Y

Y

M

A

A

S

G

G

P

T

N

N

H
|
H

V

V

L

L

P

P

T

T

S

Y

G

G

T

Y

A

T

R

A

F

T

S

C

S

S

P

S

L

L

S

G

V

L

D

A

D

D

F

F

V

Q

K

K

K

R

S

M

S

T

Y

V

L

Q

Y

E

Y

L

S

S

E

K

K

A

A

G

L

F

R

S

N

A

V

L

N

A

D

S

K

T

V

I

V

E

K

T

I

L

A

A

E

A

T

A

E

E

G

R

L

L

T

T

A

A

H
|
H

A

K

N

N

S

A

I

V

K

T

V

L

R

R

H99 (= H100) mutation to N: Slight decrease in activity.
C117 (≠ M118) mutation C->A,S: Almost no change in activity.
C154 (≠ V155) mutation C->A,S: Almost no change in activity.
H262 (= H264) mutation to N: 7000-fold decrease in activity.
H327 (= H330) mutation to N: 500-fold decrease in activity.
H367 (= H370) mutation to N: Slight decrease in activity.
H419 (= H422) mutation to Q: 20-fold decrease in activity.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed

5vldF Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidine and NAD+ (see paper)
40% identity, 95% coverage: 21:431/431 of query aligns to 17:428/435 of 5vldF

query
sites
5vldF

S

S

L

L

K

K

E

S

R

R

Q

P

G

R

K

I

E

D

N

F

A

S

E

S

I

V

I

F

K

D

T

I

V

V

K

N

F

P

I

I

I

V

D

D

N

D

V

V

K

H

E

A

N

H

G

G

D

D

K

A

A

A

L

V

I

K

E

Q

Y

Y

T

T

S

S

K

K

F
|
F

D
|
D

K

K

V

V

E

D

L

L

Q

E

S

N

I

I

-

V

-

E

-

L

-

V

-

S

-

D

-

L

-

P

-

D

E

P

V

V

T

L

K

D

E

P

E

A

I

I

K

K

A

E

A

A

Y

F

S

D

K

-

V

-

E

-

N

-

D

-

F

-

I

-

C

-

A

-

L

-

K

-

T

V

A

A

K

Y

E

S

N

N

I

I

E

Y

E

A

Y

F

H

H

S

A

K

A

Q

Q

V

K

Q

S

N

P

S

E

Y

K

V

S

I

V

T

E

K

N

E

M

N

K

G

G

I

V

V

Q

M

C

G

K

R

R

T

V

V

A

R

R

G

S

L

I

D

N

K

S

V

V

G

G

I

L

Y
|
Y

V

V

P
|
P

G

G

G
|
G

T
|
T

A

A

A

V

Y

L

P

P

S
|
S

S

T

V

A

I

L

M

M

N

L

A

A

V

V

P

P

A

A

K

Q

V

I

A

A

G

G

V

C

N

K

K

T

I

I

I

V

M

L

T

A

T

N

P

P

P

P

M

T

K

R

D

D

G

G

F

T

V

T

N

C

P

K

S

E

I

V

L

L

V

Y

A

C

A

A

D

K

L

K

A

A

G

G

V

V

D

T

K

H

I

L

Y

L

K

K

V

A

G

G

G

G

A

A

Q
|
Q

A

A

I

I

A

S

A

A

L

M

A

A

F

W

G

G

T

T

E

E

T

T

I

C

D

P

K

K

V

V

D

E

K

K

I

I

V

F

G

G

P
|
P

G
|
G

N
|
N

I

Q

F
x
Y

V

V

A

T

M

A

A

A

K

K

-

M

-

I

-

L

K

Q

S

N

V

S

Y

E

G

A

F

M

V

V

D

S

I

I

D

D

M

M

I

P

A
|
A

G
|
G

P

P

S
|
S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

K

T

H

G

A

N

I

P

P

K

S

F

H

I

V

A

A

A

A

D

D

L

L

M

L

S

S

Q
|
Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

V

L

L

V

V

T

I

T

A

S

G

K

D

E

G

L

V

I

D

G

Q

K

N

V

A

I

I

-

Q

E

E

E

E

I

V

K

S

L

K

Q

Q

V

C

E

Q

G

S

L

L

S

P

R

R

K

G

E

E

I

F

I

A

L

A

E

K

A

A

L

L

R

S

N

H

F

-

G

S

A

F

I

I

I

V

L

H

V

A

D

R

S

D

I

M

S

L

R

E

A

A

I

I

E

T

I

F

G

S

N

N

V

M

V

Y

A

A

P

P

E
|
E

H
|
H

L

L

E

I

I

I

I

N

T

V

P

K

N

D

P

A

F

E

E

K

Y

W

L

E

N

S

D

F

I

I

K

E

N

N

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

S

Y

W

S

T

P

P

E

E

P

S

L

V

G

G

D
|
D

Y
|
Y

M

A

A

S

G

G

P

T

N

N

H
|
H

V
|
V

L
|
L

P

P

T

T

S

Y

G

G

T

Y

A

A

R

R

F

M

S

Y

S

S

P

G

L

V

S

S

V

L

D

D

D

S

F

F

V

L

K

K

K

Y

S

I

S

T

Y

V

L

Q

Y

S

Y

L

S

T

E

E

K

E

A

G

L

L

R

R

N

K

V

L

N

G

D

P

K

Y

V

V

V

E

K

T

I

M

A

A

E

E

T

V

E
|
E

G

G

L

L

T

E

A

A

H
|
H

A

K

N

R

S

A

I

V

K

T

V

L

R

R

F

L

K

Q

active site: Q258 (= Q261), H261 (= H264), E326 (= E329), H327 (= H330), D360 (= D363), H419 (= H422)
binding histidine: S135 (= S141), S236 (= S239), Q258 (= Q261), H261 (= H264), E326 (= E329), H327 (= H330), D360 (= D363), Y361 (= Y364), H367 (= H370), E414 (= E417), H419 (= H422)
binding nicotinamide-adenine-dinucleotide: F55 (= F59), D56 (= D60), Y125 (= Y131), P127 (= P133), G129 (= G135), T130 (= T136), Q187 (= Q193), P208 (= P214), G209 (= G215), N210 (= N216), Y212 (≠ F218), A233 (= A236), G234 (= G237), S236 (= S239), H261 (= H264), E326 (= E329), H367 (= H370), V368 (= V371), L369 (= L372)
binding zinc ion: Q258 (= Q261), H261 (= H264), D360 (= D363)

5vlbA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with imidazole (see paper)
40% identity, 95% coverage: 21:431/431 of query aligns to 16:427/434 of 5vlbA

query
sites
5vlbA

S

S

L

L

K

K

E

S

R

R

Q

P

G

R

K

I

E

D

N

F

A

S

E

S

I

V

I

F

K

D

T

I

V

V

K

N

F

P

I

I

I

V

D

D

N

D

V

V

K

H

E

A

N

H

G

G

D

D

K

A

A

A

L

V

I

K

E

Q

Y

Y

T

T

S

S

K

K

F

F

D

D

K

K

V

V

E

D

L

L

Q

E

S

N

I

I

-

V

-

E

-

L

-

V

-

S

-

D

-

L

-

P

-

D

E

P

V

V

T

L

K

D

E

P

E

A

I

I

K

K

A

E

A

A

Y

F

S

D

K

-

V

-

E

-

N

-

D

-

F

-

I

-

C

-

A

-

L

-

K

-

T

V

A

A

K

Y

E

S

N

N

I

I

E

Y

E

A

Y

F

H

H

S

A

K

A

Q

Q

V

K

Q

S

N

P

S

E

Y

K

V

S

I

V

T

E

K

N

E

M

N

K

G

G

I

V

V

Q

M

C

G

K

R

R

T

V

V

A

R

R

G

S

L

I

D

N

K

S

V

V

G

G

I

L

Y

Y

V

V

P

P

G

G

G

G

T

T

A

A

A

V

Y

L

P

P

S

S

S

T

V

A

I

L

M

M

N

L

A

A

V

V

P

P

A

A

K

Q

V

I

A

A

G

G

V

C

N

K

K

T

I

I

I

V

M

L

T

A

T

N

P

P

P

P

M

T

K

R

D

D

G

G

F

T

V

T

N

C

P

K

S

E

I

V

L

L

V

Y

A

C

A

A

D

K

L

K

A

A

G

G

V

V

D

T

K

H

I

L

Y

L

K

K

V

A

G

G

G

G

A

A

Q

Q

A

A

I

I

A

S

A

A

L

M

A

A

F

W

G

G

T

T

E

E

T

T

I

C

D

P

K

K

V

V

D

E

K

K

I

I

V

F

G

G

P

P

G

G

N

N

I

Q

F

Y

V

V

A

T

M

A

A

A

K

K

-

M

-

I

-

L

K

Q

S

N

V

S

Y

E

G

A

F

M

V

V

D

S

I

I

D

D

M

M

I

P

A

A

G

G

P

P

S

S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

K

T

H

G

A

N

I

P

P

K

S

F

H

I

V

A

A

A

A

D

D

L

L

M

L

S

S

Q
|
Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

V

L

L

V

V

T

I

T

A

S

G

K

D

E

G

L

V

I

D

G

Q

K

N

V

A

I

I

-

Q

E

E

E

E

I

V

K

S

L

K

Q

Q

V

C

E

Q

G

S

L

L

S

P

R

R

K

G

E

E

I

F

I

A

L

A

E

K

A

A

L

L

R

S

N

H

F

-

G

S

A

F

I

I

I

V

L

H

V

A

D

R

S

D

I

M

S

L

R

E

A

A

I

I

E

T

I

F

G

S

N

N

V

M

V

Y

A

A

P

P

E
|
E

H
|
H

L

L

E

I

I

I

I

N

T

V

P

K

N

D

P

A

F

E

E

K

Y

W

L

E

N

S

D

F

I

I

K

E

N

N

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

S

Y

W

S

T

P

P

E

E

P

S

L

V

G

G

D
|
D

Y

Y

M

A

A

S

G

G

P

T

N

N

H

H

V

V

L

L

P

P

T

T

S

Y

G

G

T

Y

A

A

R

R

F

M

S

Y

S

S

P

G

L

V

S

S

V

L

D

D

D

S

F

F

V

L

K

K

K

Y

S

I

S

T

Y

V

L

Q

Y

S

Y

L

S

T

E

E

K

E

A

G

L

L

R

R

N

K

V

L

N

G

D

P

K

Y

V

V

V

E

K

T

I

M

A

A

E

E

T

V

E

E

G

G

L

L

T

E

A

A

H
|
H

A

K

N

R

S

A

I

V

K

T

V

L

R

R

F

L

K

Q

active site: Q257 (= Q261), H260 (= H264), E325 (= E329), H326 (= H330), D359 (= D363), H418 (= H422)
binding imidazole: H260 (= H264), D359 (= D363)
binding zinc ion: H260 (= H264), D359 (= D363)

5vlcA Crystal structure of medicago truncatula l-histidinol dehydrogenase in complex with l-histidinol (see paper)
40% identity, 95% coverage: 21:431/431 of query aligns to 17:425/431 of 5vlcA

query
sites
5vlcA

S

S

L

L

K

K

E

S

R

R

Q

-

G

-

K

-

E

P

N

R

A

I

E

S

I

V

I

F

K

D

T

I

V

V

K

N

F

P

I

I

I

V

D

D

N

D

V

V

K

H

E

A

N

H

G

G

D

D

K

A

A

A

L

V

I

K

E

Q

Y

Y

T

T

S

S

K

K

F

F

D

D

K

K

V

V

E

D

L

L

Q

E

S

N

I

I

-

V

-

E

-

L

-

V

-

S

-

D

-

L

-

P

-

D

E

P

V

V

T

L

K

D

E

P

E

A

I

I

K

K

A

E

A

A

Y

F

S

D

K

-

V

-

E

-

N

-

D

-

F

-

I

-

C

-

A

-

L

-

K

-

T

V

A

A

K

Y

E

S

N

N

I

I

E

Y

E

A

Y

F

H

H

S

A

K

A

Q

Q

V

K

Q

S

N

P

S

E

Y

K

V

S

I

V

T

E

K

N

E

M

N

K

G

G

I

V

V

Q

M

C

G

K

R

R

T

V

V

A

R

R

G

S

L

I

D

N

K

S

V

V

G

G

I

L

Y

Y

V

V

P

P

G

G

G

G

T

T

A

A

A

V

Y

L

P

P

S

S

S

T

V

A

I

L

M

M

N

L

A

A

V

V

P

P

A

A

K

Q

V

I

A

A

G

G

V

C

N

K

K

T

I

I

I

V

M

L

T

A

T

N

P

P

P

P

M

T

K

R

D

D

G

G

F

T

V

T

N

C

P

K

S

E

I

V

L

L

V

Y

A

C

A

A

D

K

L

K

A

A

G

G

V

V

D

T

K

H

I

L

Y

L

K

K

V

A

G

G

G

G

A

A

Q

Q

A

A

I

I

A

S

A

A

L

M

A

A

F

W

G

G

T

T

E

E

T

T

I

C

D

P

K

K

V

V

D

E

K

K

I

I

V

F

G

G

P

P

G

G

N

N

I

Q

F

Y

V

V

A

T

M

A

A

A

K

K

-

M

-

I

-

L

K

Q

S

N

V

S

Y

E

G

A

F

M

V

V

D

S

I

I

D

D

M

M

I

P

A

A

G

G

P

P

S

S

E

E

I

V

L

L

V

V

I

I

S

A

D

D

E

K

T

H

G

A

N

I

P

P

K

S

F

H

I

V

A

A

A

A

D

D

L

L

M

L

S

S

Q
|
Q

A

A

E

E

H
|
H

D

G

T

P

L

D

A

S

S

Q

S

V

I

V

L

L

V

V

T

I

T

A

S

G

K

D

E

G

L

V

I

D

G

Q

K

N

V

A

I

I

-

Q

E

E

E

E

I

V

K

S

L

K

Q

Q

V

C

E

Q

G

S

L

L

S

P

R

R

K

G

E

E

I

F

I

A

L

A

E

K

A

A

L

L

R

S

N

H

F

-

G

S

A

F

I

I

I

V

L

H

V

A

D

R

S

D

I

M

S

L

R

E

A

A

I

I

E

T

I

F

G

S

N

N

V

M

V

Y

A

A

P

P

E
|
E

H
|
H

L

L

E

I

I

I

I

N

T

V

P

K

N

D

P

A

F

E

E

K

Y

W

L

E

N

S

D

F

I

I

K

E

N

N

A

A

G

G

S

S

I

V

F

F

L

L

G

G

S

S

Y

W

S

T

P

P

E

E

P

S

L

V

G

G

D
|
D

Y
|
Y

M

A

A

S

G

G

P

T

N

N

H
|
H

V

V

L

L

P

P

T

T

S

Y

G

G

T

Y

A

A

R

R

F

M

S

Y

S

S

P

G

L

V

S

S

V

L

D

D

D

S

F

F

V

L

K

K

K

Y

S

I

S

T

Y

V

L

Q

Y

S

Y

L

S

T

E

E

K

E

A

G

L

L

R

R

N

K

V

L

N

G

D

P

K

Y

V

V

V

E

K

T

I

M

A

A

E

E

T

V

E
|
E

G

G

L

L

T

E

A

A

H
|
H

A

K

N

R

S

A

I

V

K

T

V

L

R

R

F

L

K

Q

active site: Q255 (= Q261), H258 (= H264), E323 (= E329), H324 (= H330), D357 (= D363), H416 (= H422)
binding L-histidinol: H258 (= H264), E323 (= E329), H324 (= H330), D357 (= D363), Y358 (= Y364), H364 (= H370), E411 (= E417), H416 (= H422)
binding zinc ion: Q255 (= Q261), H258 (= H264), D357 (= D363)

Query Sequence

>WP_010964255.1 NCBI__GCF_000008765.1:WP_010964255.1
MEDIIRIIQDGSLDGEKYFQSLKERQGKENAEIIKTVKFIIDNVKENGDKALIEYTSKFD
KVELQSIEVTKEEIKAAYSKVENDFICALKTAKENIEEYHSKQVQNSYVITKENGIVMGR
TVRGLDKVGIYVPGGTAAYPSSVIMNAVPAKVAGVNKIIMTTPPMKDGFVNPSILVAADL
AGVDKIYKVGGAQAIAALAFGTETIDKVDKIVGPGNIFVAMAKKSVYGFVDIDMIAGPSE
ILVISDETGNPKFIAADLMSQAEHDTLASSILVTTSKELIGKVIEEIKLQVEGLSRKEII
LEALRNFGAIILVDSISRAIEIGNVVAPEHLEIITPNPFEYLNDIKNAGSIFLGSYSPEP
LGDYMAGPNHVLPTSGTARFSSPLSVDDFVKKSSYLYYSEKALRNVNDKVVKIAETEGLT
AHANSIKVRFK

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