SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012568279.1 NCBI__GCF_000016185.1:WP_012568279.1 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 17 hits to proteins with known functional sites (download)

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)
50% identity, 80% coverage: 26:215/237 of query aligns to 20:210/215 of P0AB87

query
sites
P0AB87

L

L

G

G

I

L

N

N

Q

Q

G

G

R
x
T

S
x
A

G
|
G

N
|
N

V

V

S

S

V

V

R

R

T

Y

A

Q

Q

D

G

G

F

M

L

L

V

I

T

T

P

P

S
x
T

G
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G

V

I

A

P

Y

Y

E

E

A

K

M

L

T

T

P

E

D

S

M

H

L

I

V

V

P

F

V

I

T

D

L

G

D

N

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G

G

K

Y

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E

G

E

D

G

L

K

R

L

P

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S
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S

E
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E

W

W

R

R

L

F

H

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R

M

D

A

I

A

Y

Y

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Q

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E

D

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G

N

A

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H
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H

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H

S

A

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A

H

A

C

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T

A

A

L

V

A

S

C

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L

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I

P

P

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A

F

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Y
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Y

M

M

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I

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M

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A

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K

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G

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L

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I

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Y

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N

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L

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E

K

K

A

A

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G

T26 (≠ R32) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ S33) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 34:35) binding substrate
N29 (= N35) 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 49:50) binding substrate
S71 (= S77) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 77:78) binding substrate
E73 (= E79) 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 (= H98) binding Zn(2+)
H94 (= H100) binding Zn(2+)
Y113 (= Y119) 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 (= F137) 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 (= H161) binding Zn(2+)
F206 (= F211) mutation to 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.
Y209 (= Y214) Plays a key role in the stabilization of the transition state and positioning the aldehyde component; mutation to 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.

Sites not aligning to the query:

207:215 mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
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)
50% identity, 80% coverage: 26:215/237 of query aligns to 20:210/210 of 2fuaA

query
sites
2fuaA

L

L

G

G

I

L

N

N

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Q

G

G

R

T

S

A

G

G

N

N

V

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S

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G

active site: E73 (= E79), H92 (= H98), H94 (= H100), Y113 (= Y119), A117 (≠ M123), H155 (= H161), Y209 (= Y214)
binding cobalt (ii) ion: E73 (= E79), H92 (= H98), H94 (= H100), H155 (= H161)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
49% identity, 80% coverage: 26:214/237 of query aligns to 20:209/209 of 1dzuP

query
sites
1dzuP

L

L

G

G

I

L

N

N

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Q

G

G

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A

S

A

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G

N

N

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D

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P

E

D

A

A

G

N

A

A

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H
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H

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N

H
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H

S

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T

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A

H

A

C

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T

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A

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F

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Y

binding zinc ion: E73 (= E79), H92 (= H98), H94 (= H100), H155 (= H161)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
50% identity, 78% coverage: 26:211/237 of query aligns to 20:206/206 of 4fuaA

query
sites
4fuaA

L

L

G

G

I

L

N

N

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Q

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G

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G

N
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N

V

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Q

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F

active site: E73 (= E79), H92 (= H98), H94 (= H100), Y113 (= Y119), A117 (≠ M123), H155 (= H161)
binding phosphoglycolohydroxamic acid: G28 (= G34), N29 (= N35), T43 (≠ S49), S71 (= S77), S72 (= S78), E73 (= E79), H92 (= H98), H94 (= H100), H155 (= H161)
binding zinc ion: H92 (= H98), H94 (= H100), H155 (= H161)

7x78A L-fuculose 1-phosphate aldolase (see paper)
49% identity, 78% coverage: 26:211/237 of query aligns to 20:203/203 of 7x78A

query
sites
7x78A

L

L

G

G

I

L

N

N

Q

-

G

-

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S

A

G

G

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N

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S

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A

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Q

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D

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D

D

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K

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K

F

F

binding magnesium ion: E70 (= E79), H89 (= H98), H91 (= H100), H152 (= H161)
binding sulfate ion: N26 (= N35), T40 (≠ S49), H61 (≠ Y70), Q63 (≠ G72), S68 (= S77), S69 (= S78)

Sites not aligning to the query:

binding sulfate ion: 5, 8

4c25A L-fuculose 1-phosphate aldolase (see paper)
38% identity, 85% coverage: 10:211/237 of query aligns to 7:210/212 of 4c25A

query
sites
4c25A

A

S

G

D

A

V

R

K

A

Q

A

E

L

L

L

I

R

K

A

Y

A

G

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A

K

L

L

N

V

A

E

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T

G

D

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T

Q

K

G

G

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S
x
G

G

G

N

N

V

L

S

S

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V

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F

-

D

R

R

T

E

A

K

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Q

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E

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D

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D

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H

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H

S

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C

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Y

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K

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A

Y

G

G

A

A

Q

T

N

L

L

E

L

K

N

A

A

L

F

D

N

L

I

A

V

V

E

E

E

V

V

E

E

A

Y

L

C

A

A

R

K

Q

I

Y

Y

W

C

H

L

A

A

R

K

S

N

L

F

G

G

E

E

P

P

V

V

I

V

L

L

S

P

E

D

A

E

E

E

M

M

A

E

E

L

V

M

T

A

R

E

R

K

F

F

active site: E79 (= E79), H98 (= H98), H100 (= H100), Y119 (= Y119), H160 (= H161)
binding zinc ion: G30 (≠ S33), H98 (= H98), H100 (= H100), H160 (= H161)

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)
37% identity, 86% coverage: 13:216/237 of query aligns to 7:212/213 of P0DTQ0

query
sites
P0DTQ0

R

R

A

E

L

I

L

V

R

A

A

Y

A

G

Q

K

A

K

L

M

N

I

A

S

L

S

G

G

I

L

N

T

Q

K

G

G

R

T

S

G

G

G

N

N

V

I

S

S

V

I

-

F

R

N

T

R

A

E

Q

Q

G

G

F

L

L

V

-

A

V

I

T

S

P

P

S

S

G

G

V

L

A

E

Y

Y

E

Y

A

E

M

T

T

K

P

P

D

E

M

D

L

V

V

V

P

I

V

L

T

N

L

L

D

D

G

G

G

E

-

V

Y

I

R

E

G

G

D

E

L

R

R

K

P

P

S

S

E
|
E

W

L

R

D

L

M

H

H

R

L

D

I

I

Y

Y

Y

R

R

H

K

R

R

P

E

E

D

A

I

G

N

A

A

V

L

V

V

H
|
H

V

T

H
|
H

S

S

T

P

A

Y

A

A

T

K

A

T

L

I

A

A

C

S

L

L

R

G

L

W

R

E

I

L

P

P

A

A

F

V

H

S

Y

Y

M

L

V

I

A

A

M

F

A

A

G

G

G

-

T

P

S

N

I

V

E

R

L

C

A

A

D

P

Y

Y

A

E

T

T

F

F

G

G

T

T

Q

K

E

Q

L

L

S

A

D

D

A

A

M

A

L

F

A

E

A

G

L

M

G

I

P

D

R

R

A

A

C

V

L

L

A

A

N

N

H
|
H

G

G

Q

L

I

I

A

A

Y

G

G

A

A

N

T

N

L

I

E

K

K

M

A

A

L

F

D

T

L

V

A

A

V

E

E

E

V

I

E

E

A

F

L

C

A

A

R

Q

Q

I

Y

Y

W

Y

H

Q

A

T

R

K

S

S

L

I

G

G

E

E

P

P

V

K

I

L

L

L

S

P

E

E

A

D

E

E

M

M

A

E

E

N

V

L

T

A

R

K

F

F

A

E

A

G

Y

Y

G

G

K

Q

E76 (= E79) binding Mn(2+)
H95 (= H98) binding Mn(2+)
H97 (= H100) binding Mn(2+)
H157 (= H161) binding Mn(2+)

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
37% identity, 84% coverage: 13:211/237 of query aligns to 7:207/207 of 6btgA

query
sites
6btgA

R

R

A

E

L

I

L

V

R

A

A

Y

A

G

Q

K

A

K

L

M

N

I

A

S

L

S

G

G

I

L

N

T

Q

K

G

G

R

T

S

G

G

G

N

N

V

I

S

S

V

I

-

F

R

N

T

R

A

E

Q

Q

G

G

F

L

L

V

-

A

V

I

T

S

P

P

S

S

G

G

V

L

A

E

Y

Y

E

Y

A

E

M

T

T

K

P

P

D

E

M

D

L

V

V

V

P

I

V

L

T

N

L

L

D

D

G

G

G

E

-

V

Y

I

R

E

G

G

D

E

L

R

R

K

P

P

S

S

E
|
E

W

L

R

D

L

M

H

H

R

L

D

I

I

Y

Y

Y

R

R

H

K

R

R

P

E

E

D

A

I

G

N

A

A

V

L

V

V

H
|
H

V

T

H
|
H

S

S

T

P

A

Y

A

A

T

K

A

T

L

I

A

A

C

S

L

L

R

G

L

W

R

E

I

L

P

P

A

A

F

V

H

S

Y
|
Y

M

L

V

I

A

A

M

F

A

A

G

G

G

-

T

P

S

N

I

V

E

R

L

C

A

A

D

P

Y

Y

A

E

T

T

F

F

G

G

T

T

Q

K

E

Q

L

L

S

A

D

D

A

A

M

A

L

F

A

E

A

G

L

M

G

I

P

D

R

R

A

A

C

V

L

L

A

A

N

N

H
|
H

G

G

Q

L

I

I

A

A

Y

G

G

A

A

N

T

N

L

I

E

K

K

M

A

A

L

F

D

T

L

V

A

A

V

E

E

E

V

I

E

E

A

F

L

C

A

A

R

Q

Q

I

Y

Y

W

Y

H

Q

A

T

R

K

S

S

L

I

G

G

E

E

P

P

V

K

I

L

L

L

S

P

E

E

A

D

E

E

M

M

A

E

E

N

V

L

T

A

R

K

F

F

active site: E76 (= E79), H95 (= H98), H97 (= H100), Y116 (= Y119), H157 (= H161)
binding manganese (ii) ion: E76 (= E79), H95 (= H98), H97 (= H100), H157 (= H161)

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
34% identity, 75% coverage: 8:185/237 of query aligns to 3:185/207 of 6voqA

query
sites
6voqA

S

T

E

E

A

Q

G

Q

A

L

R

R

A

E

L

M

L

V

R

Q

A

I

A

G

Q

A

A

S

L

L

N

F

A

S

L

R

G

G

I

Y

N

A

Q

T

G

G

R

S

S

A

G

G

N

N

V

L

S

S

V

L

R

L

T

L

A

P

Q

D

G

G

-

N

F

L

L

L

V

A

T

T

P

P

S

T

G

G

V

A

A

C

Y

L

E

G

A

E

M

L

T

Q

P

A

D

Q

M

R

L

L

V

S

P

V

V

V

T

T

L

L

D

Q

G

G

G

E

Y

W

R

I

G

S

D

G

L

D

R

K

P

P

S

S

S

K

E
|
E

W

V

R

T

L

F

H

H

R

R

D

A

I

V

Y

Y

R

L

H

H

R

N

P

P

E

A

A

C

G

K

A

A

V

I

V

V

H
|
H

V

L

H
|
H

S

S

T

H

A

Y

A

L

T

T

A

A

L

L

A

S

C

C

L

L

R

Q

L

G

R

L

I

D

P

P

-

H

-

N

-

C

-

I

-

R

A

P

F

F

H

T

Y

P

M
x
Y

V

V

A

V

M

M

A

R

G

V

G

G

T

-

S

D

I

V

E

P

L

V

A

V

D

P

Y

Y

A

Y

T

R

F

P

G

G

T

D

Q

D

E

R

L

I

S

A

D

Q

A

A

M

-

L

L

A

A

A

G

L

L

G

A

P

P

R

R

-

Y

R

N

A

A

C

F

L

L

A

A

N

N

H
|
H

G

G

Q

P

I

V

A

V

Y

T

G

G

A

S

T

S

L

L

E

R

K

E

A

A

L

T

D

N

L

N

A

T

V

E

E

E

V

L

E

E

A

E

L

T

A

A

R

R

active site: E75 (= E79), H94 (= H98), H96 (= H100), Y121 (≠ M120), H161 (= H161)
binding zinc ion: E75 (= E79), H94 (= H98), H96 (= H100), H161 (= H161)

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)
30% identity, 66% coverage: 31:186/237 of query aligns to 21:169/181 of Q58813

query
sites
Q58813

G

G

R

S

S

G

G

G

N
|
N

V

V

S

S

V

V

R

K

T

E

A

G

Q

D

G

K

F

I

L

Y

V

L

T

T

P

P

S

T

G

G

V

S

A

I

Y

L

E

G

A

F

M

L

T

K

P

E

D

D

M

D

L

I

V

A

P

E

V

M

T

D

L

L

D

D

G

G

G

N

-

V

Y

I

R

K

G

G

D

-

L

-

R

K

P

P

S

T

S

S

E

E

W

K

R

N

L

L

H

H

R

L

D

M

I

I

Y

Y

R

R

H

K

R

R

P

N

E

D

A

I

G

N

A

A

V

I

H

H

V

T

H

H

S

S

T

L

A

I

A

S

T

T

A

F

L

L

A

S

C

T

L

I

R

N

L

K

R

E

I

I

-

E

-

L

-

T

P

P

A

E

F

G

H

K

Y

I

M

F

V

L

A

K

M

K

A

I

G

G

G

-

T

-

S

-

I

-

E

-

L

Y

A

V

D

D

Y

Y

A

Y

T

E

F

A

G

G

T

S

Q

L

E

K

L

L

S

A

D

E

A

E

M

-

L

-

A

T

A

A

L

K

G

R

P

D

R

E

R

D

A

V

C

I

L

I

L

L

A

K

N

N

H

H

G

G

Q

V

I

V

A

C

Y

L

G

G

A

K

T

D

L

L

E

-

K

-

A

-

L

I

D

D

L

A

A

Y

V

I

E

K

V

V

E

E

A

V

L

L

A

E

R

E

Q

Q

N25 (= N35) 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.

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
31% identity, 64% coverage: 34:184/237 of query aligns to 27:194/231 of P08203

query
sites
P08203

G

G

N
|
N

V

V

S

S

V

A

-

V

-

D

R

R

T

E

A

R

Q

G

G

V

F

F

L

V

V

I

T
x
K

P

P

S

S

G

G

V

V

A

D

Y

Y

E

S

A

V

M

M

T

T

P

A

D

D

M

D

L

M

V

V

P

V

V

V

T

S

L

I

D

E

G

T

G

G

-

E

-

V

Y

V

R

E

G

G

D

T

L

K

R

K

P

P

S

S

E
x
D

W

T

R

P

L

T

H

H

R

R

D

L

I

L

Y

Y

R

Q

H

A

R

F

P

P

E

S

A

I

G

G

A

G

V

I

V

V

H
|
H

V

T

H
|
H

S

S

T

R

A

H

A

A

T

T

A

I

L

W

A

A

C

Q

L

A

R

G

L

Q

R

S

I

I

P

P

A

A

F

-

H

-

Y

-

M

-

V

-

A

-

M

-

A

-

G

-

T

T

S

G

I
x
T

E

T

L

H

A

A

D
|
D

Y

Y

A

F

T

-

F

Y

G

G

T

T

-

I

-

P

-

C

-

T

Q

R

E

K

L

M

S

T

D

D

A

A

M

E

L

I

-

N

-

G

-

E

-

Y

-
x
E

-

W

-

E

-

T

-

G

-

N

-

V

-

I

-

V

-

E

-

T

-

F

-

E

-

K

-

Q

-

G

-

I

-

D

A

A

L

Q

G

M

P

P

R

-

A

G

C

V

L

L

L

V

A

H

N

S

H
|
H

G

G

Q

P

I

F

A

A

Y

W

G

G

A

K

T

N

L

A

E

E

K

D

A

A

L

V

D

H

L

N

A

A

V

I

E

V

V

L

E

E

A

E

L

V

A

A

N28 (= N35) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ T47) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E79) 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 (= H98) binding Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H100) 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 (≠ I129) 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 (= D133) mutation to N: Loss of the epimerase activity.
E142 (vs. gap) 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 (= H161) 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)
31% identity, 64% coverage: 34:184/237 of query aligns to 27:194/223 of 1jdiA

query
sites
1jdiA

G

G

N

N

V

V

S

S

V

A

-

V

-

D

R

R

T

E

A

R

Q

G

G

V

F

F

L

V

V

I

T

K

P

P

S

S

G

G

V

V

A

D

Y

Y

E

S

A

I

M

M

T

T

P

A

D

D

M

D

L

M

V

V

P

V

V

V

T

S

L

I

D

E

G

T

G

G

-

E

-

V

Y

V

R

E

G

G

D

A

L

K

R

K

P

P

S

S

E
x
D

W

T

R

P

L

T

H

H

R

R

D

L

I

L

Y

Y

R

Q

H

A

R

F

P

P

E

S

A

I

G

G

A

G

V

I

V

V

H
|
H

V

T

H
|
H

S

S

T

R

A

H

A

A

T

T

A

I

L

W

A

A

C

Q

L

A

R

G

L

Q

R

S

I

I

P

P

A

A

F

-

H

-

Y

-

M

-

V

-

A

-

M

-

A

-

G

-

T

T

S

G

I
x
T

E

T

L

H

A

A

D
|
D

Y

Y

A

F

T

-

F

Y

G

G

T

T

-

I

-

P

-

C

-

T

Q

R

E

K

L

M

S

T

D

D

A

A

M

E

L

I

-

N

-

G

-

E

-

Y

-

E

-

W

-

E

-

T

-

G

-

N

-

V

-

I

-

V

-

E

-

T

-

F

-

E

-

K

-

Q

-

G

-

I

-

D

A

A

L

Q

G

M

P

P

R

-

A

G

C

V

L

L

L

V

A

H

N

S

H
|
H

G

G

Q

P

I

F

A

A

Y

W

G

G

A

K

T

N

L

A

E

E

K

D

A

A

L

V

D

H

L

N

A

A

V

I

E

V

V

L

E

E

A

E

L

V

A

A

active site: D76 (≠ E79), H95 (= H98), H97 (= H100), T116 (≠ I129), D120 (= D133), H171 (= H161)
binding zinc ion: H95 (= H98), H97 (= H100), H171 (= H161)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
25% identity, 76% coverage: 27:205/237 of query aligns to 37:216/249 of 4xxfA

query
sites
4xxfA

G

G

I

F

N

D

Q

H

G

T

R

V

S

A

G

G

N

H

V

L

S

T

V

V

R

R

T

D

A

P

Q

E

G

N

-

K

-

H

F

F

L

W

V

V

T

N

P

P

S

F

G

G

V

L

A

A

Y

F

E

R

A

L

M

M

T

T

P

V

D

S

M

D

L

L

V

I

P

L

V

V

T

N

L

Q

D

E

G

G

G

T

Y

V

R

I

G

G

D

G

L

G

R

K

P

E

S

G

-

R

-

I

-

V

-

N

-

L

S

A

E
x
G

W

F

R

M

L

I

H

H

R

S

D

A

I

I

Y

H

R

K

H

A

R

R

P

P

E

E

A

V

G

Q

A

A

V

I

V

C

H
|
H

V

S

H
|
H

S

S

T

T

A

Y

A

G

T

K

A

A

L

F

A

S

C

S

L

L

R

G

L

K

R

P

I

L

P

-

A

-

F

-

H

-

Y

-

M

-

V

-

A

A

M

I

A

T

G

T

G
x
Q

T

D

S

S

I

C

E

A

L

F

-

Y

A

G

D

D

Y

V

A

A

T

L

F

L

G

G

T

D

Q

E

E

-

L

-

S

S

D

G

A

T

M

I

L

A

A

V

A

A

L

L

G

Q

P

Q

R

K

A

A

C

I

L

I

L

L

A

Q

N

N

H
|
H

G

G

Q

L

I

L

A

T

Y

V

G

G

A

T

T

T

L

I

E

D

K

S

A

A

L

V

D

A

L

W

A

F

V

I

E

M

V

L

E

E

A

K

L

Q

A

C

R

Q

Q

V

Y

Q

W

L

H

L

A

A

R

D

S

A

L

A

G

G

E

Q

P

T

V

I

I

P

L

I

S

D

E

E

A

P

E

Q

M

A

A

A

active site: G98 (≠ E79), H117 (= H98), H119 (= H100), Q138 (≠ G126), H172 (= H161)
binding zinc ion: H117 (= H98), H119 (= H100), H172 (= H161)

8il8A Crystal structure of pyruvic oxime dioxygenase (pod) from alcaligenes faecalis
27% identity, 65% coverage: 31:185/237 of query aligns to 21:179/230 of 8il8A

query
sites
8il8A

G

G

R

L

S

A

G

G

N

Q

V

I

S

S

V

V

R

R

T

S

A

E

Q

R

-

P

-

G

G

A

F

Y

L

W

V

T

T

L

P

R

S

F

G

G

V

L

A

G

Y

F

E

D

A

E

M

A

T

T

P

P

D

E

M

D

L

F

V

I

P

E

V

V

-

D

-

R

-

D

-

L

-

N

T

T

L

L

D

S

G

G

G

-

Y

-

R

E

G

G

D

M

L

A

R

N

P

P

S

A

S

T

E

-

W

-

R

R

L

F

H

H

R

L

D

W

I

V

Y

Y

R

E

H

A

R

R

P

P

E

D

A

V

G

N

A

S

V

I

H
|
H

V

T

H
|
H

S

S

T

P

A

W

A

A

T

T

A

V

L

L

A

A

C

T

L

A

R

R

L

Q

R

P

I

L

P

V

A

I

F

S

H

Q

Y

M

M

D

V

M

A

T

M

P

A

L

G

H

G

N

T

D

S

C

I

A

E

F

L

L

A

G

D

E

Y

W

A

P

T

G

F

V

G

P

T

I

Q

A

E

D

L

Q

S

E

D

G

A

V

M

I

L

I

A

S

-

K

A

A

L

L

G

G

P

D

R

K

R

R

A

A

C

I

L

I

L

L

A

A

N

H

H
|
H

G

G

Q

Y

I

L

A

T

Y

A

G

G

A

K

T

S

L

C

E

Q

K

E

A

A

L

T

D

Y

L

L

A

S

V

V

E

Y

V

L

E

E

A

R

L

A

A

A

R

R

binding fe (ii) ion: H91 (= H98), H93 (= H100), H155 (= H161)

P35611 Alpha-adducin; Erythrocyte adducin subunit alpha from Homo sapiens (Human) (see 5 papers)
26% identity, 76% coverage: 44:224/237 of query aligns to 180:366/737 of P35611

query
sites
P35611

F

F

L

L

V

I

T

V

P

P

S

F

G

G

V

L

A

L

Y

Y

E

S

A

E

M

V

T

T

P

A

D

S

M

S

L

L

V

V

P

K

V

I

T

N

L

L

D

Q

G

G

G

D

Y

I

-

V

-

D

R

R

G

G

D

S

L

T

R

N

-

L

-

G

-

V

P

N

S

Q

S

A

E

G

W

F

R

T

L

L

H

H

R

S

D

A

I

I

Y

Y

R

A

H

A

R

R

P

P

E

D

A

V

G

K

A

C

V

V

H

H

V

I

H

H

S

T

T

P

A

A

A

G

T

A

A

A

L

V

A

S

C

A

L

M

R

K

L

C

R

G

I

L

P

L

A

P

F

I

H

S

Y

P

M

E

V

A

A

L

M

S

A

L

G

G

G

-

T

-

S

E

I

V

E

A

L

Y

A

H

D

D

Y

Y

A

H

T

G

F

I

G

L

T

V

Q

D

E

E

L

E

S

E

D

K

A

V

M

L

L

I

A

Q

A

K

-

N

L

L

G

G

P

P

R

K

-

S

R

K

A

V

C

L

L

I

L

L

A

R

N

N

H

H

G

G

Q

L

I

V

A

S

Y

V

G

G

A

E

T

S

L

V

E

E

K

E

A

A

L

F

-

Y

-

I

-

H

D

N

L

L

A

V

V

V

E

A

V

C

E

E

A

I

L

Q

A

V

R

R

Q

T

Y

L

W

A

H

S

A

A

R

G

S

G

L

P

G

D

E

N

P

L

V

V

I

L

L

L

S

N

E

P

A

E

E

K

M

Y

A

K

E

A

V

K

T

S

R

R

R

-

F

-

A

-

A

S

Y

P

G

G

K

S

P

P

A

V

A

G

E

E

R

G

T

T

A

G

A

S

Sites not aligning to the query:

59 modified: Phosphoserine; by PKA
408 modified: Phosphoserine; by PKA
436 modified: Phosphoserine; by PKA
445 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-480.
460 G → W: in dbSNP:rs4961
480 modified: Phosphothreonine; by ROCK2; T→D: Abolishes phosphorylation by ROCK2; when associated with D-445.
481 modified: Phosphoserine; by PKA
586 S → C: in dbSNP:rs4963
716 modified: Phosphoserine; by PKC
726 modified: Phosphoserine; by PKA and PKC

P35612 Beta-adducin; Erythrocyte adducin subunit beta from Homo sapiens (Human) (see 2 papers)
26% identity, 55% coverage: 44:174/237 of query aligns to 168:303/726 of P35612

query
sites
P35612

F

F

L

L

V

I

T

S

P

P

S

K

G

G

V

V

A

S

Y

C

E

S

A

E

M

V

T

T

P

A

D

S

M

S

L

L

V

I

P

K

V

V

T

N

L

I

D

L

G

G

-

E

-

V

-

E

-

K

G

G

Y

S

R

S

G

C

D

F

L

P

R

V

P

D

S

T

E

G

W

F

R

C

L

L

H

H

R

S

D

A

I

I

Y

Y

R

A

H

A

R

R

P

P

E

D

A

V

G

R

A

C

V

I

H

H

V

L

H

H

S

T

T

P

A

A

A

T

T

A

A

A

L

V

A

S

C

A

L

M

R

K

L

W

R

G

I

L

P

L

A

P

F

V

H

S

Y

H

M

N

V

A

A

L

M

L

A

V

G

G

G

-

T

-

S

-

I

-

E

D

L

M

A

A

D

Y

Y

Y

A

D

T

F

F

N

G

G

T

E

Q

M

E

E

L

Q

S

E

D

A

A

D

M

R

L

I

-

N

-

L

-

Q

A

K

A

C

L

L

G

G

P

P

R

T

-

C

R

K

A

I

C

L

L

V

L

L

A

R

N

N

H

H

G

G

Q

V

I

V

A

A

Y

L

G

G

A

D

T

T

L

V

E

E

K

E

A

A

L

F

Sites not aligning to the query:

55 modified: Phosphothreonine; by PKA
439 T → A: in dbSNP:rs17855969
703 modified: Phosphoserine; by PKC
713 modified: Phosphoserine; by PKA and PKC

Q02645 Protein hu-li tai shao; Adducin-like protein from Drosophila melanogaster (Fruit fly) (see 2 papers)
24% identity, 71% coverage: 13:180/237 of query aligns to 120:294/1156 of Q02645

query
sites
Q02645

R

R

A

C

A

K

L

L

L

A

R

A

A

T

A

F

Q

R

A

L

L

L

N

D

A

L

L

Y

G

G

I

W

N

T

Q

Q

G

G

R

L

S

G

G

A

N

Q

V

I

S

T

V

A

R

R

-

L

-

K

-

V

T

D

A

Q

Q

E

G

Y

F

F

L

L

V

V

T

N

P

P

S

Y

G

G

V

L

A

L

Y

Y

E

H

A

E

M

I

T

T

P

A

D

S

M

A

L

L

V

N

P

K

V

V

T

D

L

M

D

Q

G

G

-

Q

-

I

-

V

-

E

-

Q

G

G

Y

T

R

T

G

N

D

F

L

G

R

G

P

N

S

K

S

S

E

H

W

F

R

V

L

L

H

H

R

S

D

V

I

V

Y

H

R

A

H

A

R

R

P

P

E

D

A

I

G

R

A

C

V

A

V

I

H

Y

V

I

H

G

S

C

T

S

A

P

A

V

T

V

A

A

L

I

A

S

C

S

L

L

R

K

L

T

R

G

I

L

P

L

A

P

F

L

H

T

Y

K

M

D

V

A

A

C

M

V

A

L

G

G

G

-

T

-

S

E

I

I

E

T

L

T

A

H

D

A

Y

Y

A

T

T

G

F

L

G

F

T

D

Q

E

E

E

L

E

S

R

D

N

A

R

M

L

L

V

A

R

A

S

L

L

G

G

P

P

R

N

-

S

R

K

A

V

C

I

L

L

A

T

N

N

H

H

G

G

Q

A

I

L

A

C

Y

C

G

G

A

E

T

T

L

I

E

E

K

E

A

A

L

F

D

F

L

A

A

A

V

C

E

H

V

I

Sites not aligning to the query:

478 modified: Phosphoserine
480 modified: Phosphothreonine
498 modified: Phosphothreonine
603 modified: Phosphoserine
608 modified: Phosphotyrosine
609 modified: Phosphothreonine
611 modified: Phosphothreonine
614 modified: Phosphoserine
627 modified: Phosphotyrosine
630 modified: Phosphoserine

Query Sequence

>WP_012568279.1 NCBI__GCF_000016185.1:WP_012568279.1
MRSRTDESEAGARAALLRAAQALNALGINQGRSGNVSVRTAQGFLVTPSGVAYEAMTPDM
LVPVTLDGGYRGDLRPSSEWRLHRDIYRHRPEAGAVVHVHSTAATALACLRLRIPAFHYM
VAMAGGTSIELADYATFGTQELSDAMLAALGPRRACLLANHGQIAYGATLEKALDLAVEV
EALARQYWHARSLGEPVILSEAEMAEVTRRFAAYGKPAAERTAADDAVLGFPHRLDG

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