SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_048082184.1 NCBI__GCF_000745485.1:WP_048082184.1 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 15 hits to proteins with known functional sites (download)

Q58813 L-fuculose phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
39% identity, 94% coverage: 1:187/199 of query aligns to 1:175/181 of Q58813

query
sites
Q58813

M

M

D

D

K

K

N

K

L

Q

I

F

I

I

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K

G

-

L

-

V

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N25 (= N29) mutation to L: It shows a 3-fold increase of the affinity for dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of the affinity for DL-glyceraldehyde compared to the wild-type.; mutation to T: It shows a 5-fold decrease of the affinity for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.

P0DTQ0 5-deoxy-D-ribulose 1-phosphate aldolase; 5-deoxyribose disposal aldolase; EC 4.1.2.- from Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73) (see paper)
40% identity, 83% coverage: 21:186/199 of query aligns to 21:184/213 of P0DTQ0

query
sites
P0DTQ0

G

G

L

L

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T

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G

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Y

E76 (= E78) binding Mn(2+)
H95 (= H97) binding Mn(2+)
H97 (= H99) binding Mn(2+)
H157 (= H159) binding Mn(2+)

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
40% identity, 83% coverage: 21:186/199 of query aligns to 21:184/207 of 6btgA

query
sites
6btgA

G

G

L

L

V

T

P

K

G

G

K

T

S

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G

G

N

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active site: E76 (= E78), H95 (= H97), H97 (= H99), Y116 (≠ G118), H157 (= H159)
binding manganese (ii) ion: E76 (= E78), H95 (= H97), H97 (= H99), H157 (= H159)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
31% identity, 100% coverage: 1:199/199 of query aligns to 1:193/209 of 1dzuP

query
sites
1dzuP

M

M

D

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N

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binding zinc ion: E73 (= E78), H92 (= H97), H94 (= H99), H155 (= H159)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
31% identity, 100% coverage: 1:199/199 of query aligns to 1:193/206 of 4fuaA

query
sites
4fuaA

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M

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G

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E

L

L

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K

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D

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A

A

F

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A

M

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K

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H
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G

G

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A

A

A

C

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N

L

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E

K

A

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L

L

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D

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V

active site: E73 (= E78), H92 (= H97), H94 (= H99), Y113 (vs. gap), A117 (≠ G118), H155 (= H159)
binding phosphoglycolohydroxamic acid: G28 (= G28), N29 (= N29), T43 (≠ S47), S71 (= S76), S72 (≠ M77), E73 (= E78), H92 (= H97), H94 (= H99), H155 (= H159)
binding zinc ion: H92 (= H97), H94 (= H99), H155 (= H159)

P0AB87 L-fuculose phosphate aldolase; D-ribulose-phosphate aldolase; L-fuculose-1-phosphate aldolase; EC 4.1.2.17 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 100% coverage: 1:199/199 of query aligns to 1:193/215 of P0AB87

query
sites
P0AB87

M

M

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A

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Y

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D

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M

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A

G

A

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A

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I

N

E

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C

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x
F

S

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A

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P

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G

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E

E

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K

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V

A

A

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A

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L

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K

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N

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H
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G

G

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A

A

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E

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N

L

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A

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L

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A

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Y

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V

T26 (≠ K26) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ S27) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 28:29) binding substrate
N29 (= N29) mutation to L: Loss of aldolase activity; when associated with A-71.; mutation to Q: Strong decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
TG 43:44 (≠ SG 47:48) binding substrate
S71 (= S76) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (≠ SM 76:77) binding substrate
E73 (= E78) active site, Proton donor/acceptor; binding Zn(2+); mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
H92 (= H97) binding Zn(2+)
H94 (= H99) binding Zn(2+)
Y113 (vs. gap) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to F: Slowly inactivated. Has a preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-209.
F131 (≠ Y132) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to A: Has a slight preference for the D-aldehyde and shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with W-206.
H155 (= H159) binding Zn(2+)

Sites not aligning to the query:

206 F→W: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P). Loss of aldolase activity; when associated with A-131.
207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
209 Plays a key role in the stabilization of the transition state and positioning the aldehyde component; Y→F: Slowly inactivated and unable to discriminate between the enantiomers. Shows an inversion of the diastereoselectivity. Loss of aldolase activity; when associated with Q-73 and F-113.
211:215 mutation Missing: Decrease of aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).

2fuaA L-fuculose 1-phosphate aldolase crystal form t with cobalt (see paper)
31% identity, 100% coverage: 1:199/199 of query aligns to 1:193/210 of 2fuaA

query
sites
2fuaA

M

M

D

E

K

R

N

N

L

K

I

L

I

A

K

R

G

Q

L

I

V

I

D

D

T

T

S

C

H

L

Y

E

V

M

Y

T

K

R

K

L

G

G

L

L

V

N

P

Q

G

G

K

T

S

A

G

G

N

N

I

V

S

S

C

V

R

R

F

-

Y

Y

E

Q

E

D

G

G

I

M

S

-

K

-

V

-

A

L

I

I

T

T

R

P

S

T

G

G

I

I

A

P

K

Y

R

E

N

K

V

L

E

T

S

E

D

S

D

H

I

I

I

V

I

F

I

I

D

D

M

G

D

N

G

G

N

K

M

H

L

E

E

E

G

G

D

-

K

K

K

L

P

P

S

S

M

S

E
|
E

T

W

F

R

L

F

H

H

L

M

G

A

I

A

Y

Y

R

Q

E

S

R

R

N

P

D

D

I

A

N

N

S

A

I

V

V

V

H
|
H

S

N

H
|
H

S

A

P

V

F

H

A

C

T

T

G

A

F

V

S

S

M

I

S

L

G

N

K

R

K

S

L

I

K

P

R

A

L

I

E

H

-
x
Y

-

M

-

I

-

A

G
x
A

F

A

G

G

P

G

I

N

E

S

T

I

P

P

Y

C

I

A

P

P

Y

Y

V

A

K

T

Y

F

S

-

A

-

P

-

G

G

S

T

G

R

E

E

L

L

A

S

K

E

D

H

T

V

A

A

F

L

M

A

M

L

K

K

D

N

N

R

D

K

A

A

V

T

V

L

L

L

K

Q

N

H

H
|
H

G

G

T

L

V

I

A

A

A

C

G

E

V

V

N

N

L

L

D

E

E

K

A

A

T

L

L

W

L

L

A

A

E

H

F

E

I

V

E

E

D

V

I

L

A

A

K

Q

I

L

Q

-

Y

Y

I

L

A

T

H

-

T

T

L

L

S

A

L

I

N

T

S

D

D

P

I

V

S

P

V

V

active site: E73 (= E78), H92 (= H97), H94 (= H99), Y113 (vs. gap), A117 (≠ G118), H155 (= H159)
binding cobalt (ii) ion: E73 (= E78), H92 (= H97), H94 (= H99), H155 (= H159)

Sites not aligning to the query:

active site: 209

4c25A L-fuculose 1-phosphate aldolase (see paper)
34% identity, 84% coverage: 22:188/199 of query aligns to 25:189/212 of 4c25A

query
sites
4c25A

L

L

V

T

P

K

G

G

K

T

S
x
G

G

G

N

N

I

L

S

S

C

V

R

F

F

D

Y

R

E

E

E

K

G

Q

I

L

S

-

K

-

V

M

A

A

I

I

T

T

R

P

S

S

G

G

I

I

A

D

K

F

R

F

N

E

V

I

E

K

S

E

D

S

D

D

I

I

I

V

I

M

D

D

M

I

D

N

G

G

N

N

M

V

L

V

E

E

G

G

D

E

K

R

K

L

P

P

S

S

M

S

E
|
E

T

W

F

Y

L

M

H

H

L

L

G

I

I

Q

Y

Y

R

Q

E

T

R

R

N

D

D

D

I

I

N

D

S

A

I

I

V

I

H
|
H

S

A

H
|
H

S

T

P

T

F

Y

A

A

T

T

G

V

F

L

S

A

M

C

S

L

G

R

K

E

K

P

L

L

K

P

R

A

L

S

E

H

G
x
Y

F

M

G

I

P

A

I

V

E

A

T

G

P

K

Y

D

I

V

P

R

Y

V

V

A

K

E

Y

Y

S

A

A

T

P

Y

G

G

S

T

G

K

E

E

L

L

A

A

K

V

D

N

T

A

A

A

F

K

M

A

M

M

K

E

D

G

N

R

D

R

A

A

V

V

V

L

L

L

K

A

N

N

H
|
H

G

G

T

I

V

L

A

A

A

G

G

A

V

Q

N

N

L

L

D

L

E

N

A

A

T

F

L

N

L

I

A

V

E

E

F

E

I

V

E

E

D

Y

I

C

A

A

K

K

I

I

Q

Y

Y

C

I

L

A

A

active site: E79 (= E78), H98 (= H97), H100 (= H99), Y119 (≠ G118), H160 (= H159)
binding zinc ion: G30 (≠ S27), H98 (= H97), H100 (= H99), H160 (= H159)

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
27% identity, 92% coverage: 1:184/199 of query aligns to 2:186/207 of 6voqA

query
sites
6voqA

M

M

D

T

K

E

N

Q

L

Q

I

L

I

R

K

E

G

E

L

M

V

V

D

Q

T

I

S

G

H

A

Y

S

V

L

Y

F

K

S

K

R

G

G

L

Y

V

A

P

T

G

G

K

S

S

A

G

G

N

N

I

L

S

S

C

L

R

L

F

L

Y

P

E

D

E

-

G

-

I

-

S

G

K

N

V

L

A

L

I

A

T

T

R

P

S

T

G

G

I

A

A

C

K

L

R

G

N

E

V

L

E

Q

S

A

D

Q

D

R

I

L

I

S

I

V

D

T

M

L

D

Q

G

G

N

E

M

W

L

I

E

S

G

G

D

D

K

K

K

-

P

P

S

S

M

K

E
|
E

T

V

F

T

L

F

H

H

L

R

G

A

I

V

Y

Y

R

L

E

H

R

N

N

P

D

A

I

C

N

K

S

A

I

I

V

V

H
|
H

S

L

H
|
H

S

S

P

H

F

Y

A

L

T

T

G

A

F

L

S

S

M

C

S

-

G

-

K

-

L

-

K

-

R

-

L

L

E

Q

G

G

F

L

G

D

P

P

I

H

E

N

-

C

-

I

-

R

-

P

-

F

T

T

P

P

Y
|
Y

I

V

-

V

-

M

-

R

-

V

-

G

-

D

-

V

P

P

Y

V

V

V

K

P

Y

Y

S

Y

A

R

P

P

G

G

S

D

G

D

E

R

L

I

A

A

K

Q

D

A

T

L

A

A

F

G

M

L

M

A

K

P

D

R

N

Y

D

N

A

A

V

F

V

L

L

L

K

A

N

N

H
|
H

G

G

T

P

V

V

A

V

A

T

G

G

V

S

N

S

L

L

D

R

E

E

A

A

T

T

L

N

A

T

E

E

F

E

I

L

E

E

D

E

I

T

A

A

K

R

I

L

active site: E75 (= E78), H94 (= H97), H96 (= H99), Y121 (= Y126), H161 (= H159)
binding zinc ion: E75 (= E78), H94 (= H97), H96 (= H99), H161 (= H159)

8il8A Crystal structure of pyruvic oxime dioxygenase (pod) from alcaligenes faecalis
30% identity, 83% coverage: 25:189/199 of query aligns to 21:185/230 of 8il8A

query
sites
8il8A

G

G

K

L

S

A

G

G

N

Q

I

I

S

S

C

V

R

R

F

S

Y

E

E

R

E

P

G

G

I

-

S

-

K

A

V

Y

A

W

I

T

T

L

R

R

S

F

G

G

I

L

A

G

K

F

R

D

N

E

V

A

E

T

S

P

D

E

D

D

I

F

I

I

I

E

I

V

D

D

M

R

D

D

G

L

N

N

M

T

L

L

E

S

G

G

D

E

K

G

K

M

P

A

S

N

M

P

E

A

T

T

F

R

L

F

H

H

L

L

G

W

I

V

Y

Y

R

E

E

A

R

R

N

P

D

D

I

V

N

N

S

S

I

I

V

I

H
|
H

S

T

H
|
H

S

S

P

P

F

W

A

A

T

T

G

V

F

L

S

A

M

T

S

A

G

R

K

Q

K

P

L

L

K

V

R

I

L

S

E

Q

-

M

G

D

F

M

G

T

P

P

I

L

-

H

-

N

-

D

-

C

-

A

-

F

-

L

-

G

E

E

T

W

P

P

Y

G

I

V

P

P

Y

I

V

-

K

-

Y

-

S

-

A

A

P

D

G

Q

S

E

G

G

E

V

L

I

A

I

K

S

D

K

T

A

A

-

F

-

M

-

M

L

K

G

D

D

N

K

D

R

A

A

V

I

L

L

K

A

N

H

H
|
H

G

G

T

Y

V

L

A

T

A

A

G

G

V

K

N

S

L

C

D

Q

E

E

A

A

T

T

L

Y

L

L

A

S

E

V

F

Y

I

L

E

E

D

R

I

A

A

A

K

R

I

L

Q

Q

Y

V

I

R

A

A

H

Q

binding fe (ii) ion: H91 (= H97), H93 (= H99), H155 (= H159)

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 87% coverage: 19:192/199 of query aligns to 18:204/231 of P08203

query
sites
P08203

K

K

K

H

G

N

L

L

V

V

P

T

G

L

K

T

S

W

G

G

N
|
N

I

V

S

S

C

A

R

V

F

D

Y

R

E

E

E

R

G

G

I

V

S

-

K

-

V

F

A

V

I

I

T
x
K

R

P

S

S

G

G

I

V

A

D

K

Y

R

S

N

V

V

M

E

T

S

A

D

D

I

M

I

V

D

S

M

I

D

E

-

T

G

G

N

E

M

V

L

V

E

E

G

G

D

T

K

K

P

P

S

S

M

S

E
x
D

T

T

F

P

L

T

H

H

L

R

G

L

I

L

Y

Y

R

Q

E

A

R

F

N

P

D

S

I

I

N

G

S

G

I

I

V

V

H
|
H

S

T

H
|
H

S

S

P

R

F

H

A

A

T

T

G

I

F

W

S

A

M

Q

S

A

G

G

K

Q

K

S

L

I

K

P

R

-

L

-

E

-

G

A

F

T

G

G

P
x
T

I

T

E

H

T

A

P
x
D

Y

Y

-

F

-

Y

-

G

-

T

I

I

P

P

Y

C

V

T

K

R

-

K

-

M

Y

T

S

D

A

A

P

E

G

I

S

N

G

G

E

E

L

Y

A
x
E

K

W

D

E

T

T

-

G

-

N

-

V

-

I

-

V

-

E

A

T

F

F

M

E

M

K

K

Q

D

G

N

I

D

D

A

A

-

A

-

Q

-

M

-

P

-

G

V

V

V

L

L

V

K

H

N

S

H
|
H

G

G

T

P

V

F

A

A

A

W

G

G

V

K

N

N

L

A

D

E

E

D

A

A

T

V

L

H

L

N

A

A

E

I

F

V

I

L

E

E

D

E

I

V

A

A

K

Y

I

M

Q

G

Y

I

I

F

A

C

H

R

T

Q

L

L

S

A

N28 (= N29) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ T45) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E78) mutation to N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
H95 (= H97) binding Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H99) binding Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
T116 (≠ P121) mutation T->E,Y: Loss of the epimerase activity due to an increased steric bulk introduced by the mutation which causes a conformational change that is incompatible with catalysis.
D120 (≠ P125) mutation to N: Loss of the epimerase activity.
E142 (≠ A141) mutation to Q: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
H171 (= H159) binding Zn(2+)

Sites not aligning to the query:

218 H→N: Mutant shows a strong decrease of the catalytic efficiency, but it retains considerable epimerase activity. The affinity for L-ribulose 5-phosphate (LRu5P) is relatively unaffected.
229 Y→F: Loss of the epimerase activity.

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
28% identity, 87% coverage: 19:192/199 of query aligns to 18:204/223 of 1jdiA

query
sites
1jdiA

K

K

K

H

G

N

L

L

V

V

P

T

G

L

K

T

S

W

G

G

N

N

I

V

S

S

C

A

R

V

F

D

Y

R

E

E

E

R

G

G

I

V

S

-

K

-

V

F

A

V

I

I

T

K

R

P

S

S

G

G

I

V

A

D

K

Y

R

S

N

I

V

M

E

T

S

A

D

D

I

M

I

V

D

S

M

I

D

E

-

T

G

G

N

E

M

V

L

V

E

E

G

G

D

A

K

K

P

P

S

S

M

S

E
x
D

T

T

F

P

L

T

H

H

L

R

G

L

I

L

Y

Y

R

Q

E

A

R

F

N

P

D

S

I

I

N

G

S

G

I

I

V

V

H
|
H

S

T

H
|
H

S

S

P

R

F

H

A

A

T

T

G

I

F

W

S

A

M

Q

S

A

G

G

K

Q

K

S

L

I

K

P

R

-

L

-

E

-

G

A

F

T

G

G

P
x
T

I

T

E

H

T

A

P
x
D

Y

Y

-

F

-

Y

-

G

-

T

I

I

P

P

Y

C

V

T

K

R

-

K

-

M

Y

T

S

D

A

A

P

E

G

I

S

N

G

G

E

E

L

Y

A

E

K

W

D

E

T

T

-

G

-

N

-

V

-

I

-

V

-

E

A

T

F

F

M

E

M

K

K

Q

D

G

N

I

D

D

A

A

-

A

-

Q

-

M

-

P

-

G

V

V

V

L

L

V

K

H

N

S

H
|
H

G

G

T

P

V

F

A

A

A

W

G

G

V

K

N

N

L

A

D

E

E

D

A

A

T

V

L

H

L

N

A

A

E

I

F

V

I

L

E

E

D

E

I

V

A

A

K

Y

I

M

Q

G

Y

I

I

F

A

C

H

R

T

Q

L

L

S

A

active site: D76 (≠ E78), H95 (= H97), H97 (= H99), T116 (≠ P121), D120 (≠ P125), H171 (= H159)
binding zinc ion: H95 (= H97), H97 (= H99), H171 (= H159)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
25% identity, 71% coverage: 48:188/199 of query aligns to 63:201/249 of 4xxfA

query
sites
4xxfA

G

G

I

L

A

A

K

F

R

R

N

L

V

M

E

T

S

V

D

S

D

D

I

L

I

I

I

L

I

V

D

N

M

Q

D

E

G

G

N

T

M

V

L

I

-

G

-

K

E

E

G

G

D

R

K

R

K

I

P

V

S

N

M

L

E

A

T
x
G

F

F

L

M

-

I

H

H

L

S

G

A

I

I

Y

H

R

K

E

A

R

R

N

P

D

E

I

V

N

Q

S

A

I

I

V

C

H
|
H

S

S

H
|
H

S

S

P

T

F

Y

A

G

T

K

G

A

F

F

S

S

M

S

S

L

G

G

K

K

K

P

L

L

K

A

R

-

L

-

E

-

G

-

F

-

G

-

P

-

I

I

E

T

T

T

P
x
Q

Y

D

I

S

P

C

Y

A

V

F

K

Y

Y

G

S

D

A

V

P

A

G

L

S

L

G

G

E

D

L

E

A

S

K

G

D

T

T

I

A

A

F

V

M

A

M

L

K

Q

D

Q

N

K

D

K

A

A

V

I

L

L

K

Q

N

N

H
|
H

G

G

T

L

V

L

A

T

A

V

G

G

V

T

N

T

L

I

D

D

E

S

A

A

T

V

L

A

L

W

A

F

E

I

F

M

I

L

E

E

D

K

I

Q

A

C

K

Q

I

V

Q

Q

Y

L

I

L

A

A

active site: G98 (≠ T79), H117 (= H97), H119 (= H99), Q138 (≠ P125), H172 (= H159)
binding zinc ion: H117 (= H97), H119 (= H99), H172 (= H159)

2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
25% identity, 78% coverage: 28:182/199 of query aligns to 29:189/237 of 2z7bA

query
sites
2z7bA

G

G

N

H

I

I

S

S

C

A

R

R

F

D

Y

P

E

E

E

D

G

P

I

A

S

S

K

F

V

F

A

L

I

A

T

Q

R

K

S

-

G

-

I

L

A

A

K

P

R

S

N

L

V

I

E

T

S

V

D

D

I

I

I

Q

I

R

I

F

D

N

M

L

D

D

G

G

N

E

M

T

L

-

E

-

G

S

D

D

K

N

K

R

P

P

S

S

-

Y

M

L

E
|
E

T

R

F

Y

L

I

H

H

L

S

G

E

I

I

Y

Y

R

K

E

T

R

R

N

P

D

D

I

V

N

Q

S

C

I

V

V

L

H
|
H

S

T

H
|
H

S

S

P

P

F

A

A

V

T

L

G

P

F

Y

S

C

M

F

S

V

G

D

K

T

K

P

L

L

K

R

R

P

L

V

E

T

G

H

F

M

G

G

P

A

I

F

E

I

T

G

P

E

Y

S

I

V

P

P

Y

V

V

Y

K

E

Y

I

S

R

A

D

P

K

-

H

-

G

-

D

-

E

-

T

-

D

-

L

-

F

-

G

G

G

S

S

G

P

E

D

L

V

A

C

K

A

D

D

T

I

A

A

F

E

M

S

M

L

K

G

D

S

N

Q

D

T

A

V

V

V

V

L

L

M

K

A

N

R

H
|
H

G

G

T

V

V

V

A

N

A

V

G

G

V

K

N

S

L

V

D

R

E

E

A

V

T

V

L

F

L

R

A

A

E

F

F

Y

I

L

E

E

D

Q

I

E

A

A

binding manganese (ii) ion: E76 (= E78), H95 (= H97), H97 (= H99), H166 (= H159)

Q988D0 3-hydroxy-2-methylpyridine-4,5-dicarboxylate 4-decarboxylase; HMPDdc; EC 4.1.1.51 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see paper)
25% identity, 78% coverage: 28:182/199 of query aligns to 26:186/234 of Q988D0

query
sites
Q988D0

G

G

N

H

I

I

S

S

C

A

R

R

F

D

Y

P

E

E

E

D

G

P

I

A

S

S

K

F

V

F

A

L

I

A

T

Q

R

K

S

-

G

-

I

L

A

A

K

P

R

S

N

L

V

I

E

T

S

V

D

D

I

I

I

Q

I

R

I

F

D

N

M

L

D

D

G

G

N

E

M

T

L

-

E

-

G

S

D

D

K

N

K

R

P

P

S

S

-

Y

M

L

E
|
E

T

R

F

Y

L

I

H

H

L

S

G

E

I

I

Y

Y

R

K

E

T

R

R

N

P

D

D

I

V

N

Q

S

C

I

V

V

L

H
|
H

S

T

H
|
H

S

S

P

P

F

A

A

V

T

L

G

P

F

Y

S

C

M

F

S

V

G

D

K

T

K

P

L

L

K

R

R

P

L

V

E

T

G

H

F

M

G

G

P

A

I

F

E

I

T

G

P

E

Y

S

I

V

P

P

Y

V

V

Y

K

E

Y

I

S

R

A

D

P

K

-

H

-

G

-

D

-

E

-

T

-

D

-

L

-

F

-

G

G

G

S

S

G

P

E

D

L

V

A

C

K

A

D

D

T

I

A

A

F

E

M

S

M

L

K

G

D

S

N

Q

D

T

A

V

V

V

V

L

L

M

K

A

N

R

H
|
H

G

G

T

V

V

V

A

N

A

V

G

G

V

K

N

S

L

V

D

R

E

E

A

V

T

V

L

F

L

R

A

A

E

F

F

Y

I

L

E

E

D

Q

I

E

A

A

E73 (= E78) binding Mn(2+)
H92 (= H97) binding Mn(2+)
H94 (= H99) binding Mn(2+)
H163 (= H159) binding Mn(2+)

Query Sequence

>WP_048082184.1 NCBI__GCF_000745485.1:WP_048082184.1
MDKNLIIKGLVDTSHYVYKKGLVPGKSGNISCRFYEEGISKVAITRSGIAKRNVESDDII
IIDMDGNMLEGDKKPSMETFLHLGIYRERNDINSIVHSHSPFATGFSMSGKKLKRLEGFG
PIETPYIPYVKYSAPGSGELAKDTAFMMKDNDAVVLKNHGTVAAGVNLDEATLLAEFIED
IAKIQYIAHTLSLNSDISV

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