SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_035241760.1 NCBI__GCF_000745975.1:WP_035241760.1 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 20 (the maximum) hits to proteins with known functional sites (download)

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)
57% identity, 97% coverage: 1:213/219 of query aligns to 1:213/213 of P0DTQ0

query
sites
P0DTQ0

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E76 (= E76) binding Mn(2+)
H95 (= H95) binding Mn(2+)
H97 (= H97) binding Mn(2+)
H157 (= H157) binding Mn(2+)

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
57% identity, 95% coverage: 1:207/219 of query aligns to 1:207/207 of 6btgA

query
sites
6btgA

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active site: E76 (= E76), H95 (= H95), H97 (= H97), Y116 (= Y116), H157 (= H157)
binding manganese (ii) ion: E76 (= E76), H95 (= H95), H97 (= H97), H157 (= H157)

4c25A L-fuculose 1-phosphate aldolase (see paper)
47% identity, 92% coverage: 7:208/219 of query aligns to 10:211/212 of 4c25A

query
sites
4c25A

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active site: E79 (= E76), H98 (= H95), H100 (= H97), Y119 (= Y116), H160 (= H157)
binding zinc ion: G30 (= G27), H98 (= H95), H100 (= H97), H160 (= H157)

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)
40% identity, 97% coverage: 1:213/219 of query aligns to 1:212/215 of P0AB87

query
sites
P0AB87

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T26 (= T26) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ G27) 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 45:46) binding substrate
S71 (= S74) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 74:75) binding substrate
E73 (= E76) 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 (= H95) binding Zn(2+)
H94 (= H97) binding Zn(2+)
Y113 (= Y116) 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 (= F133) 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 (= H157) binding Zn(2+)
F206 (= F207) 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 (= Y210) 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)
40% identity, 96% coverage: 1:211/219 of query aligns to 1:210/210 of 2fuaA

query
sites
2fuaA

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active site: E73 (= E76), H92 (= H95), H94 (= H97), Y113 (= Y116), A117 (≠ F120), H155 (= H157), Y209 (= Y210)
binding cobalt (ii) ion: E73 (= E76), H92 (= H95), H94 (= H97), H155 (= H157)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
39% identity, 96% coverage: 1:210/219 of query aligns to 1:209/209 of 1dzuP

query
sites
1dzuP

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H

I

E

D

E

G

G

E

K

A

L

R

-

P

P

S

S

E
|
E

L

W

G

R

F

F

H

H

L

M

S

A

L

A

Y

Y

G

Q

Q

S

R

R

K

P

D

D

I

A

Q

N

A

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

P

V

Y

H

A

C

V

T

T

A

M

V

A

S

C

I

L

L

G

N

W

R

E

S

I

I

P

P

A

A

V

I

H

H

Y

Y

L

M

V

I

G

A

F

A

A

A

G

G

-

G

K

N

K

S

V

I

P

P

L

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

P

R

E

E

L

L

A

S

Q

E

I

H

V

V

A

A

E

L

Y

A

I

L

G

K

D

N

Y

R

N

K

A

A

L

T

L

L

A

Q

N

H

H
|
H

G

G

L

L

V

I

A

A

V

C

G

E

S

V

S

N

M

L

D

E

T

K

A

A

F

L

A

W

A

L

A

A

E

H

E

E

I

V

E

E

F

V

V

L

A

A

R

Q

I

L

Y

Y

Y

L

Q

T

T

T

K

L

S

A

I

I

G

T

N

D

P

P

V

V

-

P

I

V

L

L

P

S

D

D

E

E

M

I

N

A

T

V

V

V

L

L

E

E

K

K

F

F

K

K

T

T

Y

Y

binding zinc ion: E73 (= E76), H92 (= H95), H94 (= H97), H155 (= H157)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
39% identity, 95% coverage: 1:207/219 of query aligns to 1:206/206 of 4fuaA

query
sites
4fuaA

M

M

E

E

L

R

E

N

N

K

E

L

R

A

K

R

A

Q

V

I

R

D

F

T

G

C

L

L

K

E

M

M

V

T

E

R

S

L

G

G

L

L

T

N

T

Q

G

G

T

T

G

A

G
|
G

N
|
N

L

V

S

S

I

V

I

-

D

-

R

R

K

Y

S

Q

G

D

T

G

V

M

A

L

V

I

S

T

P

P

S
x
T

G

G

I

I

E

P

Y

Y

A

E

V

K

L

L

Q

T

P

E

R

S

D

H

V

I

V

V

L

F

T

I

D

D

M

G

Q

N

G

G

N

K

V

H

I

E

D

E

G

G

E

K

A

L

R

-

P

P

S
|
S

E
|
E

L

W

G

R

F

F

H

H

L

M

S

A

L

A

Y

Y

G

Q

Q

S

R

R

K

P

D

D

I

A

Q

N

A

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

P

V

Y

H

A

C

V

T

T

A

M

V

A

S

C

I

L

L

G

N

W

R

E

S

I

I

P

P

A

A

V

I

H

H

Y
|
Y

L

M

V

I

G

A

F
x
A

A

A

G

G

-

G

K

N

K

S

V

I

P

P

L

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

P

R

E

E

L

L

A

S

Q

E

I

H

V

V

A

A

E

L

Y

A

I

L

G

K

D

N

Y

R

N

K

A

A

L

T

L

L

A

Q

N

H

H
|
H

G

G

L

L

V

I

A

A

V

C

G

E

S

V

S

N

M

L

D

E

T

K

A

A

F

L

A

W

A

L

A

A

E

H

E

E

I

V

E

E

F

V

V

L

A

A

R

Q

I

L

Y

Y

Y

L

Q

T

T

T

K

L

S

A

I

I

G

T

N

D

P

P

V

V

-

P

I

V

L

L

P

S

D

D

E

E

M

I

N

A

T

V

V

V

L

L

E

E

K

K

F

F

active site: E73 (= E76), H92 (= H95), H94 (= H97), Y113 (= Y116), A117 (≠ F120), H155 (= H157)
binding phosphoglycolohydroxamic acid: G28 (= G28), N29 (= N29), T43 (≠ S45), S71 (= S74), S72 (= S75), E73 (= E76), H92 (= H95), H94 (= H97), H155 (= H157)
binding zinc ion: H92 (= H95), H94 (= H97), H155 (= H157)

7x78A L-fuculose 1-phosphate aldolase (see paper)
39% identity, 95% coverage: 1:207/219 of query aligns to 1:203/203 of 7x78A

query
sites
7x78A

M

M

E

E

L

R

E

N

N
x
R

E

L

R

A

K
x
R

A

Q

V

I

R

D

F

T

G

C

L

L

K

E

M

M

V

T

E

R

S

L

G

G

L

L

T

N

T

-

G

-

T

-

G

A

G

G

N
|
N

L

V

S

S

I

V

I

-

D

-

R

R

K

Y

S

Q

G

G

T

G

V

M

A

L

V

I

S

T

P

P

S
x
T

G

G

I

I

E

P

Y

Y

A

E

V

K

L

L

Q

T

P

E

R

D

D

K

V

I

V

V

L

F

T

I

D

D

M

A

Q

D

G

G

N

Q

V
x
H

I

E

D
x
Q

G

G

E

K

A

L

R

-

P

P

S
|
S

E
|
E

L

W

G

R

F

F

H

H

L

Q

S

A

L

A

Y

Y

G

Q

Q

T

R

R

K

P

D

D

I

A

Q

Q

A

A

I

V

V

V

H
|
H

T

N

H
|
H

S

A

P

V

Y

H

A

C

V

T

T

A

M

V

A

S

C

I

L

L

G

N

W

R

E

P

I

I

P

P

A

A

V

I

H

H

Y

Y

L

M

V

I

G

A

F

A

A

A

G

G

-

G

K

N

K

S

V

I

P

P

L

C

A

A

P

P

Y

Y

A

A

T

T

F

F

G

G

T

T

P

R

E

E

L

L

A

S

Q

E

I

H

V

V

A

A

E

V

Y

A

I

L

G

K

D

H

Y

R

N

K

A

A

L

T

L

L

A

Q

N

H

H
|
H

G

G

L

L

V

I

A

A

V

C

G

E

S

A

S

S

M

L

D

E

T

K

A

A

F

L

A

W

A

L

A

A

E

H

E

E

I

V

E

E

F

V

V

L

A

A

R

Q

I

L

Y

Y

Y

L

Q

S

T

T

K

L

S

A

I

I

G

T

N

D

P

P

V

V

-

P

I

V

L

L

P

D

D

D

E

E

E

A

M

I

N

A

T

I

V

V

L

L

E

E

K

K

F

F

binding magnesium ion: E70 (= E76), H89 (= H95), H91 (= H97), H152 (= H157)
binding sulfate ion: R5 (≠ N5), R8 (≠ K8), N26 (= N29), T40 (≠ S45), H61 (≠ V66), Q63 (≠ D68), S68 (= S74), S69 (= S75)

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
35% identity, 87% coverage: 1:191/219 of query aligns to 2:192/207 of 6voqA

query
sites
6voqA

M

M

E

T

L

E

E

Q

N

Q

E

L

R

R

K

E

A

E

V

M

V

V

R

Q

F

I

G

G

L

A

K

S

M

L

V

F

E

S

S

R

G

G

L

Y

T

A

T

T

G

G

T

S

G

A

G

G

N

N

L

L

S

S

I

L

D

-

R

L

K

P

S

D

G

G

T

N

V

L

A

L

V

A

S

T

P

P

S

T

G

G

I

A

E

C

Y

L

A

G

V

E

L

L

Q

Q

P

A

R

Q

D

R

V

L

V

S

L

V

T

V

D

T

M

L

Q

Q

G

G

N

E

V

W

I

I

D

S

G

G

E

D

A

-

R

K

P

P

S

S

S

K

E
|
E

L

V

G

T

F

F

H

H

L

R

S

A

L

V

Y

Y

G

L

Q

H

R

N

K

P

D

A

I

C

Q

K

A

A

I

I

V

V

H
|
H

T

L

H
|
H

S

S

P

H

Y

Y

A

L

V

T

T

A

M

L

A

S

C

C

L

L

-

Q

-

G

-

L

-

D

-

P

-

H

G

N

W

C

E

I

I

R

P

P

A

F

V

T

H

P

Y
|
Y

L

V

V

V

G

M

F

R

A

V

G

G

K

D

K

-

V

V

P

P

L

V

A

V

P

P

Y

Y

A

Y

T

R

F

P

G

G

T

D

P

D

E

R

L

I

A

A

Q

Q

I

A

V

L

A

A

E

G

Y

L

I

A

G

P

D

R

Y

Y

N

N

A

A

L

F

L

L

A

A

N

N

H
|
H

G

G

L

P

V

V

A

V

V

T

G

G

S

S

M

L

D

R

T

E

A

A

F

T

A

N

A

T

E

E

I

L

E

E

F

E

V

T

A

A

R

R

I

L

Y

I

Y

F

Q

-

T

-

K

-

S

T

I

L

G

G

N

N

active site: E75 (= E76), H94 (= H95), H96 (= H97), Y121 (= Y116), H161 (= H157)
binding zinc ion: E75 (= E76), H94 (= H95), H96 (= H97), H161 (= H157)

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)
29% identity, 81% coverage: 6:182/219 of query aligns to 2:172/181 of Q58813

query
sites
Q58813

E

D

R

K

K

K

A

Q

V

F

V

I

R

K

F

I

G

C

L

R

K

K

M

L

V

Y

E

D

S

R

G

K

L

Y

T

V

G

G

T

S

G

G

N
|
N

L

V

S

S

I

V

I

-

D

-

R

K

K

E

S

G

G

D

T

K

V

I

A

Y

V

L

S

T

P

P

S

T

G

G

I

S

E

I

Y

L

A

G

V

F

L

L

Q

K

P

E

R

D

D

D

V

I

V

A

L

E

T

M

D

D

M

L

Q

D

G

G

N

N

V

V

I

I

D

K

G

G

E

-

A

-

R

K

P

P

S

T

S

S

E

E

L

K

G

N

F

L

H

H

L

L

S

M

L

I

Y

Y

G

R

Q

K

R

R

K

N

D

D

I

I

Q

N

A

A

I

I

V

I

H

H

T

T

H

H

S

S

P

L

Y

I

A

S

V

T

T

F

M

L

A

S

C

T

L

I

G

N

W

K

E

E

I

I

P

E

A

L

V

L

H

T

Y

P

L

E

V

G

G

K

F

I

A

F

G

L

K

K

V

I

P

G

L

Y

A

V

P

D

Y

Y

A

Y

T

E

F

A

G

G

T

S

P

L

E

K

L

L

A

A

Q

E

I

E

V

T

A

A

E

K

Y

R

I

-

G

-

D

D

Y

E

N

D

A

V

L

I

L

L

A

K

N

N

H

H

G

G

L

V

V

V

A

C

V

L

G

G

S

K

S

D

M

L

D

I

T

D

A

A

F

Y

A

I

A

K

A

V

E

E

E

V

I

L

E

E

F

E

V

Q

A

A

R

K

I

L

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.

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
38% identity, 51% coverage: 3:113/219 of query aligns to 2:113/231 of P08203

query
sites
P08203

L

L

E

E

N

D

E

L

R

K

K

R

A

Q

V

V

V

L

R

E

F

A

G

N

L

L

K

A

M

L

V

P

E

K

S

H

G

N

L

L

T

V

T

T

G

L

T

T

G

W

G

G

N
|
N

L

V

S

S

I

A

I

V

D

D

R

R

K

E

S

R

G

G

T

V

V

F

A

V

V

I

S
x
K

P

P

S

S

G

G

I

V

E

D

Y

Y

A

S

V

V

L

M

Q

T

P

A

R

D

D

D

V

M

V

V

L

V

T

V

D

S

M

I

Q

E

-

T

G

G

N

E

V

V

I

V

D

E

G

G

E

T

A

K

R

K

P

P

S

S

E
x
D

L

T

G

P

F

T

H

H

L

R

S

L

L

L

Y

Y

G

Q

Q

A

R

F

K

P

D

S

I

I

Q

G

A

G

I

I

V

V

H
|
H

T

T

H
|
H

S

S

P

R

Y

H

A

A

V

T

T

I

M

W

A

A

C

Q

L

A

G

G

W

Q

E

S

I

I

P

P

A

A

N28 (= N29) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ S43) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E76) 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 (= H95) binding Zn(2+); mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H97) 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.

Sites not aligning to the query:

116 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.
120 D→N: Loss of the epimerase activity.
142 E→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.
171 binding Zn(2+)
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)
37% identity, 51% coverage: 3:113/219 of query aligns to 2:113/223 of 1jdiA

query
sites
1jdiA

L

L

E

E

N

D

E

L

R

K

K

R

A

Q

V

V

V

L

R

E

F

A

G

N

L

L

K

A

M

L

V

P

E

K

S

H

G

N

L

L

T

V

T

T

G

L

T

T

G

W

G

G

N

N

L

V

S

S

I

A

I

V

D

D

R

R

K

E

S

R

G

G

T

V

V

F

A

V

V

I

S

K

P

P

S

S

G

G

I

V

E

D

Y

Y

A

S

V

I

L

M

Q

T

P

A

R

D

D

D

V

M

V

V

L

V

T

V

D

S

M

I

Q

E

-

T

G

G

N

E

V

V

I

V

D

E

G

G

E

A

A

K

R

K

P

P

S

S

E
x
D

L

T

G

P

F

T

H

H

L

R

S

L

L

L

Y

Y

G

Q

Q

A

R

F

K

P

D

S

I

I

Q

G

A

G

I

I

V

V

H
|
H

T

T

H
|
H

S

S

P

R

Y

H

A

A

V

T

T

I

M

W

A

A

C

Q

L

A

G

G

W

Q

E

S

I

I

P

P

A

A

active site: D76 (≠ E76), H95 (= H95), H97 (= H97)
binding zinc ion: H95 (= H95), H97 (= H97)

Sites not aligning to the query:

active site: 116, 120, 171
binding zinc ion: 171

8il8A Crystal structure of pyruvic oxime dioxygenase (pod) from alcaligenes faecalis
27% identity, 80% coverage: 25:200/219 of query aligns to 21:198/230 of 8il8A

query
sites
8il8A

G

G

T

L

G

A

G

G

N

Q

L

I

S

S

I

V

I

R

D

S

R

E

K

R

S

P

G

G

T

A

V

Y

A

W

V

T

S

L

P

R

S

F

G

G

I

L

E

G

Y

F

A

D

V

E

L

A

Q

T

P

P

R

E

D

D

V

F

V

I

L

E

T

V

D

D

M

R

Q

D

G

L

N

N

V

T

I

L

D

S

G

G

E

E

A

G

R

M

P

A

S

N

S

P

E

A

L

T

G

R

F

F

H

H

L

L

S

W

L

V

Y

Y

G

E

Q

A

R

R

K

P

D

D

I

V

Q

N

A

S

I

I

V

I

H
|
H

T

T

H
|
H

S

S

P

P

Y

W

A

A

V

T

T

V

M

L

A

A

C

T

L

-

G

-

W

-

E

-

I

-

P

-

A

A

V

R

H

Q

Y

P

L

L

V

V

G

I

F

S

A

Q

G

M

K

D

K

M

V

T

P

P

L

L

A

H

P

N

Y

D

A

C

T

A

F

F

-

L

-

G

-

E

-

W

-

P

G

G

T

V

P

P

E

I

L

A

A

D

Q

Q

-

E

-

G

-

V

I

I

V

I

A

S

E

K

Y

A

I

L

G

G

D

D

Y

K

N

R

A

A

L

I

L

L

A

A

N

H

H
|
H

G

G

L

Y

V

L

A

T

V

A

G

G

S

K

S

S

M

C

D

Q

T

E

A

A

F

T

A

Y

A

L

A

S

E

V

E

Y

I

L

E

E

F

R

V

A

A

A

R

R

I

L

Y

Q

Y

V

Q

R

T

A

K

Q

S

A

I

A

G

F

N

G

P

P

V

L

I

T

L

P

P

V

D

D

E

D

E

T

M

L

binding fe (ii) ion: H91 (= H95), H93 (= H97), H155 (= H157)

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)
29% identity, 69% coverage: 52:202/219 of query aligns to 45:208/234 of Q988D0

query
sites
Q988D0

L

L

Q

A

P

P

R

S

D

L

V

I

V

T

L

V

T

D

D

D

M

I

Q

Q

G

R

N

F

V

N

I

L

D

D

G

G

E

E

A

T

-

S

-

D

-

N

R

R

P

P

S

S

S

Y

-

L

E
|
E

L

R

G

Y

F

I

H

H

L

S

S

E

L

I

Y

Y

G

K

Q

T

R

R

K

P

D

D

I

V

Q

Q

A

C

I

V

V

L

H
|
H

T

T

H
|
H

S

S

P

P

Y

A

A

V

V

L

T

P

M

Y

A

C

C

F

L

V

G

D

W

T

E

P

I

L

P

R

A

P

V

V

H

T

Y

H

L

M

V

G

G

A

F

F

A

I

G

G

K

E

K

S

V

V

P

P

L

V

A

Y

P

E

Y

I

A

R

T

D

F

K

-

H

-

G

-

D

-

E

-

T

-

D

-

L

-

F

-

G

G

G

T

S

P

P

E

D

L

V

A

C

Q

A

I

D

V

I

A

A

E

E

Y

S

I

L

G

G

D

S

Y

Q

N

T

A

V

L

V

L

L

L

M

A

A

N

R

H
|
H

G

G

L

V

V

V

A

N

V

V

G

G

S

K

S

S

M

V

D

R

T

E

A

V

F

V

A

F

A

R

A

A

E

F

E

Y

I

L

E

E

F

Q

V

E

A

A

R

A

I

A

Y

L

Y

T

Q

A

T

G

K

L

S

K

I

I

G

G

N

N

P

V

V

K

I

Y

L

L

P

S

D

P

E

G

E

E

M

I

N

K

T

T

E73 (= E76) binding Mn(2+)
H92 (= H95) binding Mn(2+)
H94 (= H97) binding Mn(2+)
H163 (= H157) binding Mn(2+)

2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
29% identity, 69% coverage: 52:202/219 of query aligns to 48:211/237 of 2z7bA

query
sites
2z7bA

L

L

Q

A

P

P

R

S

D

L

V

I

V

T

L

V

T

D

D

D

M

I

Q

Q

G

R

N

F

V

N

I

L

D

D

G

G

E

E

A

T

-

S

-

D

-

N

R

R

P

P

S

S

S

Y

-

L

E
|
E

L

R

G

Y

F

I

H

H

L

S

S

E

L

I

Y

Y

G

K

Q

T

R

R

K

P

D

D

I

V

Q

Q

A

C

I

V

V

L

H
|
H

T

T

H
|
H

S

S

P

P

Y

A

A

V

V

L

T

P

M

Y

A

C

C

F

L

V

G

D

W

T

E

P

I

L

P

R

A

P

V

V

H

T

Y

H

L

M

V

G

G

A

F

F

A

I

G

G

K

E

K

S

V

V

P

P

L

V

A

Y

P

E

Y

I

A

R

T

D

F

K

-

H

-

G

-

D

-

E

-

T

-

D

-

L

-

F

-

G

G

G

T

S

P

P

E

D

L

V

A

C

Q

A

I

D

V

I

A

A

E

E

Y

S

I

L

G

G

D

S

Y

Q

N

T

A

V

L

V

L

L

L

M

A

A

N

R

H
|
H

G

G

L

V

V

V

A

N

V

V

G

G

S

K

S

S

M

V

D

R

T

E

A

V

F

V

A

F

A

R

A

A

E

F

E

Y

I

L

E

E

F

Q

V

E

A

A

R

A

I

A

Y

L

Y

T

Q

A

T

G

K

L

S

K

I

I

G

G

N

N

P

V

V

K

I

Y

L

L

P

S

D

P

E

G

E

E

M

I

N

K

T

T

binding manganese (ii) ion: E76 (= E76), H95 (= H95), H97 (= H97), H166 (= H157)

4m6rA Structural and biochemical basis for the inhibition of cell death by apip, a methionine salvage enzyme (see paper)
26% identity, 89% coverage: 1:196/219 of query aligns to 1:217/224 of 4m6rA

query
sites
4m6rA

M

M

E

D

L

K

E

E

N

H

E

P

R

R

K

Y

A

L

V

I

V

P

R

E

F

L

G

C

L

K

K

Q

M

F

V

Y

E

H

S

L

G

G

L

W

T

V

T

T

G

G

T

T

G

G

N

G

L

I

S

S

I

L

I

-

D

-

R

K

K

H

S

G

G

D

T

E

V

I

A

Y

V

I

S

A

P

P

S

S

G

G

I

V

E

Q

Y

K

A

E

V

R

L

I

Q

Q

P

P

R

E

D

D

V

M

V

F

L

V

T

C

D

D

M

I

Q

N

G

E

N

K

V

D

I

I

D

S

G

G

E

P

A

S

R

-

P

P

S

S

S

K

E

K

L

L

G

K

-

K

-

S

-

Q

-

C

-

T

-

P

F

L

H

F

L

M

S

N

L

A

Y

Y

G

T

Q

M

R

R

K

-

D

G

I

A

Q

G

A

A

I

V

V

I

H
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H

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T

H
|
H

S

S

P

K

Y

A

A

A

V

V

T

M

M

A

A

T

C

L

L

L

-

F

-

P

G

G

W

R

E

E

I

F

P

K

A

I

V

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H

H

Y

Q

L

E

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M

G

I

F

K

A

G

G

I

K

K

V

C

P

T

L

S

A

G

P

G

Y

Y

A

Y

T

R

F

Y

-

D

-

M

-

L

-

V

-

P

-

I

-

E

G

N

T

T

P

P

E

E

-

E

-

K

-

D

-

L

-

K

-

D

-

R

L

M

A

A

Q

H

I

A

V

M

A

N

E

E

Y

Y

I

-

G

P

D

D

Y

S

N

C

A

A

L

V

L

L

L

V

A

R

N

R

H
|
H

G

G

L

V

V

Y

A

V

V

W

G

G

S

E

S

T

M

W

D

E

T

K

A

A

F

K

A

T

A

M

A

C

E

E

E

C

I

Y

E

D

F

Y

V

L

A

F

R

D

I

I

Y

A

Y

V

Q

S

T

M

K

K

S

K

I

V

G

G

-

L

N

D

P

P

V

S

I

Q

L

L

P

P

binding zinc ion: H97 (= H95), H99 (= H97), H177 (= H157)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
27% identity, 89% coverage: 21:216/219 of query aligns to 37:228/249 of 4xxfA

query
sites
4xxfA

G

G

L

F

T

D

T

H

G

T

T

V

G

A

G

G

N

H

L

L

S

T

I

V

I

R

D

D

-

P

R

E

K

N

S

K

G

H

T

H

V

F

A

W

V

V

S

N

P

P

S

F

G

G

I

L

E

A

Y

F

A

R

V

L

L

M

Q

T

P

V

R

S

D

D

V

L

V

I

L

L

T

V

D

N

M

Q

Q

E

G

G

N

T

V

V

I

I

D

G

G

G

-

G

-

K

E

E

A

G

R

R

P

R

S

I

S

V

E

N

L

L

-

A

G
|
G

F

F

-

M

-

I

H

H

L

S

S

A

L

I

Y

H

G

K

Q

A

R

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K

P

D

E

I

V

Q

Q

A

A

I

I

V

C

H
|
H

T

S

H
|
H

S

S

P

T

Y

Y

A

G

V

K

T

A

M

F

A

S

C

S

L

L

G

G

W

K

E

P

I

L

P

A

-

I

A

T

V

T

H
x
Q

Y

D

L

S

V

C

G

A

F

F

A

Y

G

G

K

D

K

V

V

A

P

L

L

L

A

G

P

D

Y

E

A

S

T

-

F

-

G

G

T

T

P

-

E

-

L

-

A

-

Q

-

I

-

V

I

A

A

E

V

Y

A

I

L

G

Q

D

Q

Y

K

N

K

A

A

L

I

L

L

A

Q

N

N

H
|
H

G

G

L

L

V

L

A

T

V

V

G

G

S

T

M

I

D

D

T

S

A

A

F

V

A

A

A

W

A

F

E

I

E

M

I

L

E

E

F

K

V

Q

A

C

R

Q

I

V

Y

Q

Y

L

Q

L

T

A

K

D

S

A

I

A

G

G

N

Q

P

T

V

I

I

-

L

-

P

P

D

I

E

D

E

E

M

P

N

Q

T

A

V

A

L

F

E

-

K

T

F

F

K

K

T

E

Y

L

G

G

Q

H

K

E

K

Q

M

A

G

G

active site: G98 (= G78), H117 (= H95), H119 (= H97), Q138 (≠ H115), H172 (= H157)
binding zinc ion: H117 (= H95), H119 (= H97), H172 (= H157)

Q96GX9 Methylthioribulose-1-phosphate dehydratase; MTRu-1-P dehydratase; APAF1-interacting protein; hAPIP; EC 4.2.1.109 from Homo sapiens (Human) (see 5 papers)
26% identity, 88% coverage: 4:196/219 of query aligns to 22:235/242 of Q96GX9

query
sites
Q96GX9

E

E

N
x
H

E

P

R

R

K

Y

A

L

V

I

V

P

R

E

F

L

G

C

L

K

K

Q

M

F

V

Y

E

H

S

L

G

G

L

W

T

V

T

T

G

G

T

T

G

G

N

G

L

I

S

S

I

L

I

-

D

-

R

K

K

H

S

G

G

D

T

E

V

I

A

Y

V

I

S

A

P

P

S

S

G

G

I

V

E

Q

Y

K

A

E

V

R

L

I

Q

Q

P

P

R

E

D

D

V

M

V

F

L

V

T
x
C

D

D

M

I

Q

N

G

E

N

K

V

D

I

I

D
x
S

G

G

E

P

A
x
S

R

-

P

P

S
|
S

S

K

E

K

L

L

G

K

-

K

-

S

-
x
Q

-
x
C

-

T

-

P

F

L

H

F

L

M

S

N

L

A

Y

Y

G

T

Q

M

R

R

K

-

D

G

I

A

Q

G

A

A

I

V

V

I

H
|
H

T

T

H
|
H

S

S

P

K

Y

A

A

A

V

V

T

M

M

A

A

T

C

L

L

L

-

F

-

P

G

G

W

R

E

E

I

F

P

K

A

I

V

T

H

H

Y

Q

L
x
E

V

M

G

I

F

K

A

G

G

I

K

K

V

C

P

T

L

S

A

G

P

G

Y

Y

A

Y

T

R

F

Y

-

D

-

M

-

L

-

V

-

P

-

I

-

E

G

N

T

T

P

P

E

E

-

E

-

K

-

D

-

L

-

K

-

D

-

R

L

M

A

A

Q

H

I

A

V
x
M

A

N

E

E

Y

Y

I

-

G

P

D

D

Y

S

N

C

A

A

L

V

L

L

L

V

A

R

N

R

H
|
H

G

G

L

V

V

Y

A

V

V

W

G

G

S

E

S

T

M

W

D

E

T

K

A

A

F

K

A

T

A

M

A

C

E

E

E

C

I

Y

E

D

F

Y

V

L

A

F

R

D

I

I

Y

A

Y

V

Q

S

T

M

K

K

S

K

I

V

G

G

-

L

N

D

P

P

V

S

I

Q

L

L

P

P

H23 (≠ N5) to R: in dbSNP:rs17850326
C76 (≠ T60) to Y: in dbSNP:rs1977420
S84 (≠ D68) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89.
S87 (≠ A71) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89.
S89 (= S74) mutation S->A,D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87.
Q96 (vs. gap) mutation to A: Mildly reduced enzyme activity.
C97 (vs. gap) mutation to A: Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression.; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
H115 (= H95) mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.; mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death.
H117 (= H97) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195.
E139 (≠ L117) active site, Proton donor/acceptor; mutation to A: Almost complete loss of enzyme activity. Abolishes protection against pyroptosis. No effect on anti-apoptotic activity.
M181 (≠ V142) to V: in dbSNP:rs17850327
H195 (= H157) mutation to A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89.

Sites not aligning to the query:

7 R → W: in dbSNP:rs2956114

P35612 Beta-adducin; Erythrocyte adducin subunit beta from Homo sapiens (Human) (see 2 papers)
26% identity, 59% coverage: 42:170/219 of query aligns to 170:303/726 of P35612

query
sites
P35612

V

I

S

S

P

P

S

K

G

G

I

V

E

S

Y

C

A

S

V

E

L

V

Q

T

P

A

R

S

D

S

V

L

V

I

L

K

T

V

D

N

M

I

Q

L

G

G

N

E

V

V

I

V

D

E

-

K

-

G

G

S

E

S

A

C

R

F

P

P

S

V

S

D

E

T

L

T

G

G

F

F

-

C

-

L

H

H

L

S

S

A

L

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Y

Y

G

A

Q

A

R

R

K

P

D

D

I

V

Q

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A

C

I

I

V

I

H

H

T

L

H

H

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T

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P

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A

A

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A

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A

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V

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C

A

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M

G

K

W

W

E

G

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L

A

P

V

V

H

S

Y

H

L

N

V

A

G

L

F

L

A

V

G

G

K

D

K

-

V

-

P

-

L

M

A

A

P

Y

Y

Y

A

D

T

F

F

N

G

G

T

-

P

-

E

E

L

M

A

E

Q

Q

I

-

V

E

A

A

E

D

Y

R

I

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G

N

-

L

-

Q

-

K

-

C

-

L

-

G

-

P

D

T

Y

C

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A

I

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L

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L

L

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N

H

H

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G

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V

V

A

A

V

L

G

G

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D

S

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M

V

D

E

T

E

A

A

F

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

P35611 Alpha-adducin; Erythrocyte adducin subunit alpha from Homo sapiens (Human) (see 5 papers)
25% identity, 59% coverage: 42:170/219 of query aligns to 182:315/737 of P35611

query
sites
P35611

V

I

S

V

P

P

S

F

G

G

I

L

E

L

Y

Y

A

S

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A

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S

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V

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Q

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G

N

D

V

I

I

V

D

D

G

-

E

-

A

-

R

R

P

G

S

S

S

T

E

N

L

L

G

G

-

V

-

N

-

Q

-

A

-

G

-

F

-

T

F

L

H

H

L

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S

A

L

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A

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A

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R

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D

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A

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V

V

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H

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H

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P

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A

A

G

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A

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A

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A

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W

C

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A

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A

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V

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A

D

P

Y

Y

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A

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T

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P

E

E

E

L

E

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V

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L

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A

Q

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Y

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I

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G

D

P

Y

K

N

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A

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-

V

L

L

L

I

L

L

A

R

N

N

H

H

G

G

L

L

V

V

A

S

V

V

G

G

S

E

S

S

M

V

D

E

T

E

A

A

F

F

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

Query Sequence

>WP_035241760.1 NCBI__GCF_000745975.1:WP_035241760.1
MELENERKAVVRFGLKMVESGLTTGTGGNLSIIDRKSGTVAVSPSGIEYAVLQPRDVVLT
DMQGNVIDGEARPSSELGFHLSLYGQRKDIQAIVHTHSPYAVTMACLGWEIPAVHYLVGF
AGKKVPLAPYATFGTPELAQIVAEYIGDYNALLLANHGLVAVGSSMDTAFAAAEEIEFVA
RIYYQTKSIGNPVILPDEEMNTVLEKFKTYGQKKMGIGK

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