SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_068106088.1 NCBI__GCF_001653335.1:WP_068106088.1 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)

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)
32% identity, 90% coverage: 11:206/217 of query aligns to 10:212/213 of P0DTQ0

query
sites
P0DTQ0

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E76 (= E69) binding Mn(2+)
H95 (= H87) binding Mn(2+)
H97 (= H89) binding Mn(2+)
H157 (= H149) binding Mn(2+)

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
32% identity, 85% coverage: 11:195/217 of query aligns to 10:203/207 of 6btgA

query
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6btgA

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active site: E76 (= E69), H95 (= H87), H97 (= H89), Y116 (= Y108), H157 (= H149)
binding manganese (ii) ion: E76 (= E69), H95 (= H87), H97 (= H89), H157 (= H149)

4c25A L-fuculose 1-phosphate aldolase (see paper)
34% identity, 79% coverage: 16:187/217 of query aligns to 18:198/212 of 4c25A

query
sites
4c25A

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active site: E79 (= E69), H98 (= H87), H100 (= H89), Y119 (= Y108), H160 (= H149)
binding zinc ion: G30 (≠ A28), H98 (= H87), H100 (= H89), H160 (= H149)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
38% identity, 77% coverage: 22:188/217 of query aligns to 21:184/206 of 4fuaA

query
sites
4fuaA

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active site: E73 (= E69), H92 (= H87), H94 (= H89), Y113 (= Y108), A117 (≠ L112), H155 (= H149)
binding phosphoglycolohydroxamic acid: G28 (= G29), N29 (= N30), T43 (≠ S44), S71 (≠ T67), S72 (= S68), E73 (= E69), H92 (= H87), H94 (= H89), H155 (= H149)
binding zinc ion: H92 (= H87), H94 (= H89), H155 (= H149)

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)
38% identity, 77% coverage: 22:188/217 of query aligns to 21:184/215 of P0AB87

query
sites
P0AB87

G

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T26 (≠ S27) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (= A28) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 29:30) binding substrate
N29 (= N30) 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 44:45) binding substrate
S71 (≠ T67) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (≠ TS 67:68) binding substrate
E73 (= E69) 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 (= H87) binding Zn(2+)
H94 (= H89) binding Zn(2+)
Y113 (= Y108) 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 (= F125) 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 (= H149) 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)
38% identity, 77% coverage: 22:188/217 of query aligns to 21:184/210 of 2fuaA

query
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2fuaA

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T

T

active site: E73 (= E69), H92 (= H87), H94 (= H89), Y113 (= Y108), A117 (≠ L112), H155 (= H149)
binding cobalt (ii) ion: E73 (= E69), H92 (= H87), H94 (= H89), H155 (= H149)

Sites not aligning to the query:

active site: 209

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
38% identity, 77% coverage: 22:188/217 of query aligns to 21:184/209 of 1dzuP

query
sites
1dzuP

G

G

L

L

V

N

V

Q

G

G

S

A

A

A

G

G

N

N

V

V

S

S

L

V

R

R

V

Y

G

Q

A

D

A

G

V

M

L

L

V

I

T

T

A

P

S

T

G

G

V

I

D

P

L

Y

S

E

T

K

C

L

G

T

A

E

D

S

D

H

V

I

V

V

L

F

L

I

-

D

G

G

S

N

G

G

R

K

G

H

R

E

-

E

-

G

-

K

-

L

P

P

T

S

S

S

E
|
E

V

W

D

R

L

F

H

H

L

M

G

A

-

A

V

Y

Q

Q

A

S

D

R

T

P

G

D

A

A

T

N

A

A

V

V

H
|
H

T

N

H
|
H

A

A

P

V

Y

H

S

C

T

T

A

A

V

V

A

S

C

I

V

L

L

N

D

R

E

S

L

I

P

P

V

A

L

I

H

H

Y

Y

Q

M

Q

I

M

A

L

A

G

G

-

N

A

S

V

I

R

P

V

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

A

E

H

H

V

V

R

A

A

L

A

A

L

L

A

K

G

N

R

R

S

K

A

A

A

T

L

L

M

L

A

Q

N

H

H
|
H

G

G

S

L

V

I

A

A

V

C

G

E

A

V

T

N

L

L

D

E

E

K

A

A

V

L

E

-

R

-

A

-

L

-

E

-

W

W

L

L

A

A

A

-

L

-

H

-

H

H

R

E

V

V

A

E

V

V

L

L

G

A

A

Q

P

L

R

Y

L

L

L

T

T

T

binding zinc ion: E73 (= E69), H92 (= H87), H94 (= H89), H155 (= H149)

7x78A L-fuculose 1-phosphate aldolase (see paper)
37% identity, 74% coverage: 15:175/217 of query aligns to 7:178/203 of 7x78A

query
sites
7x78A

A

A

R
|
R

R

Q

L

I

A

I

D

D

E

T

G

C

L

L

V

E

V

M

G

T

-

R

-

L

-

G

-

L

S

N

A

A

G

G

N
|
N

V

V

S

S

L

V

R

R

V

Y

G

Q

A

G

V

M

L

L

V

I

T

T

A

P

S
x
T

G

G

V

I

D

P

L

Y

S

E

T

K

C

L

G

T

A

E

D

D

D

K

V

I

V

V

L

F

L

I

G

D

S

A

G

D

-

G

-

Q

-
x
H

-

E

R
x
Q

G

G

R

K

-

L

P

P

T
x
S

S
|
S

E
|
E

V

W

D

R

L

F

H

H

L

Q

G

A

-

A

V

Y

Q

Q

A

T

D

R

T

P

G

D

A

A

T

Q

A

A

V

V

H
|
H

T

N

H
|
H

A

A

P

V

Y

H

S

C

T

T

A

A

V

V

A

S

C

I

V

L

L

N

D

R

E

P

L

I

P

P

V

A

L

I

H

H

Y

Y

Q

M

Q

I

M

A

L

A

G

G

-

N

A

S

V

I

R

P

V

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

A

E

H

H

V

V

R

A

A

V

A

A

L

L

A

K

G

H

R

R

S

K

A

A

A

T

L

L

M

L

A

Q

N

H

H
|
H

G

G

S

L

V

I

A

A

V

C

G

E

A

A

T

S

L

L

D

E

E

K

A

A

V

L

E

W

R

L

A

A

L

H

L

E

L

V

E

E

W

V

L

L

A

A

A

Q

L

L

H

Y

binding magnesium ion: E70 (= E69), H89 (= H87), H91 (= H89), H152 (= H149)
binding sulfate ion: R8 (= R16), N26 (= N30), T40 (≠ S44), H61 (vs. gap), Q63 (≠ R63), S68 (≠ T67), S69 (= S68)

Sites not aligning to the query:

binding sulfate ion: 5

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, 74% coverage: 15:174/217 of query aligns to 10:172/181 of Q58813

query
sites
Q58813

A

C

R

R

R

K

L

L

A

Y

D

D

E

R

G

K

L

Y

V

V

G

G

S

S

A

G

G

G

N
|
N

V

V

S

S

L

V

R

K

V

E

G

G

A

D

A

K

V

I

L

Y

V

L

T

T

A

P

S

T

G

G

V

S

D

I

L

L

S

G

T

F

C

L

G

K

A

E

D

D

V

I

V

A

L

E

L

M

G

D

S

L

G

D

-

G

-

N

-

V

-

I

R

K

G

G

R

K

P

P

T

T

S

S

E

E

V

K

D

N

L

L

H

H

L

L

G

M

V

I

-

Y

Q

R

A

K

D

R

T

N

G

D

A

I

T

N

A

A

V

I

H

H

T

T

H

H

A

S

P

L

Y

I

S

S

T

T

A

F

V

L

A

S

C

T

V

I

L

N

D

K

E

E

L

I

P

E

V

L

L

L

H

T

Y

P

Q

E

Q

G

M

K

L

I

L

F

G

L

G

K

A

K

V

I

R

G

V

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

A

E

H

E

V

-

R

-

A

T

A

A

L

K

A

R

G

D

R

E

S

D

A

V

A

I

L

I

M

L

A

K

N

N

H

H

G

G

S

V

V

V

A

C

V

L

G

G

A

K

T

D

L

L

D

I

E

D

A

A

V

Y

E

I

R

K

A

V

L

E

L

V

L

L

E

E

W

E

L

Q

A

A

A

K

L

L

N25 (= N30) 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.

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
37% identity, 72% coverage: 18:174/217 of query aligns to 18:186/207 of 6voqA

query
sites
6voqA

L

L

A

F

D

S

E

R

G

G

L

Y

V

A

V

T

G

G

S

S

A

A

G

G

N

N

V

L

S

S

L

L

R

L

V

L

-

P

G

D

A

G

A

N

V

L

L

L

V

A

T

T

A

P

S

T

G

G

V

A

D

C

L

L

S

G

T

E

C

L

G

Q

A

A

D

Q

D

R

-

L

-

S

-

V

V

V

V

T

L

L

L

Q

G

G

-

E

-

W

-

I

S

S

G

G

R

-

G

D

R

K

P

P

T

S

S

K

E
|
E

V

V

D

T

L

F

H

H

L

R

G

A

V

V

Q

Y

A

L

-

H

D

N

T

P

G

A

A

C

T

K

A

A

V

I

V

V

H
|
H

T

L

H
|
H

A

S

P

H

Y

Y

S

L

T

T

A

A

V

L

A

S

C

C

V

L

-

Q

-

G

L

L

D

D

E

P

-

H

-

N

-

C

-

I

L

R

P

P

V

F

L

T

H

P

Y
|
Y

Q

V

M

M

L

R

L

V

G

G

G

D

A

-

V

V

R

P

V

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

A

Q

H

A

V

L

R

-

A

A

A

G

L

L

A

A

G

P

R

R

-

Y

S

N

A

A

A

F

L

L

M

L

A

A

N

N

H
|
H

G

G

S

P

V

V

A

V

V

T

G

G

A

S

T

S

L

L

D

R

E

E

A

A

V

T

E

N

R

N

A

T

L

E

L

L

E

E

W

E

L

T

A

A

A

R

L

L

active site: E75 (= E69), H94 (= H87), H96 (= H89), Y121 (= Y108), H161 (= H149)
binding zinc ion: E75 (= E69), H94 (= H87), H96 (= H89), H161 (= H149)

Query Sequence

>WP_068106088.1 NCBI__GCF_001653335.1:WP_068106088.1
MTPAPESYAAVAAAARRLADEGLVVGSAGNVSLRVGAAVLVTASGVDLSTCGADDVVLLG
SGRGRPTSEVDLHLGVQADTGATAVVHTHAPYSTAVACVLDELPVLHYQQMLLGGAVRVA
PYATFGTPELAAHVRAALAGRSAALMANHGSVAVGATLDEAVERALLLEWLAALHHRVAV
LGAPRLLTATQQHDVVVAALTRGYGRTDPSTSTGGAE

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