SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF1603 FitnessBrowser__Phaeo:GFF1603 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)

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)
44% identity, 96% coverage: 8:221/223 of query aligns to 2:212/215 of P0AB87

query
sites
P0AB87

D

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S

R

D

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T

K

L

L

R

A

Q

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Q

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I

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D

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R

T26 (= T32) 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
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 50:51) binding
S71 (= S81) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 81:82) binding
E73 (= E83) active site, Proton donor/acceptor; binding ; mutation to Q: Loss of aldolase activity; when associated with F-113 and F-209.; mutation to S: Loss of aldolase activity.
H92 (= H102) binding
H94 (= H104) binding
Y113 (= Y123) 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 (= F141) 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 (= H165) binding
F206 (= F215) 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 (= Y218) 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)
44% identity, 95% coverage: 8:219/223 of query aligns to 2:210/210 of 2fuaA

query
sites
2fuaA

D

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S

R

D

N

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K

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L

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active site: E73 (= E83), H92 (= H102), H94 (= H104), Y113 (= Y123), A117 (= A127), H155 (= H165), Y209 (= Y218)
binding cobalt (ii) ion: E73 (= E83), H92 (= H102), H94 (= H104), H155 (= H165)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
43% identity, 95% coverage: 8:218/223 of query aligns to 2:209/209 of 1dzuP

query
sites
1dzuP

D

E

S

R

D

N

T

K

L

L

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A

Q

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S

Q

I

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D

D

A

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Y

binding zinc ion: E73 (= E83), H92 (= H102), H94 (= H104), H155 (= H165)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
44% identity, 93% coverage: 8:215/223 of query aligns to 2:206/206 of 4fuaA

query
sites
4fuaA

D

E

S

R

D

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K

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F

F

active site: E73 (= E83), H92 (= H102), H94 (= H104), Y113 (= Y123), A117 (= A127), H155 (= H165)
binding phosphoglycolohydroxamic acid: T26 (= T32), A27 (≠ S33), G28 (= G34), N29 (= N35), T43 (≠ S50), G44 (= G51), S71 (= S81), S72 (= S82), E73 (= E83), H92 (= H102), H94 (= H104), H155 (= H165)
binding zinc ion: H92 (= H102), H94 (= H104), H155 (= H165)

7x78A L-fuculose 1-phosphate aldolase (see paper)
46% identity, 87% coverage: 8:200/223 of query aligns to 2:187/203 of 7x78A

query
sites
7x78A

D

E

S

R

D

N

T
x
R

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L

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x
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P

binding magnesium ion: E70 (= E83), H89 (= H102), H91 (= H104), H152 (= H165)
binding sulfate ion: R5 (≠ T11), R8 (≠ Q14), N26 (= N35), T40 (≠ S50), H61 (≠ P71), Q63 (≠ P73), G64 (≠ Q74), S68 (= S81), S69 (= S82)

4c25A L-fuculose 1-phosphate aldolase (see paper)
34% identity, 90% coverage: 9:209/223 of query aligns to 6:204/212 of 4c25A

query
sites
4c25A

S

S

D

S

T

D

L

V

R

K

Q

Q

S

E

I

L

I

I

D

K

A

Y

C

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D

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K

G

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T

S
x
G

G

G

N

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S

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F

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E

G

K

E

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G

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K

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V

R

E

G

G

Q

E

P

R

S

L

P

P

S

S

E
|
E

W

W

Q

Y

F

M

H

H

Q

L

A

I

L

Q

L

Y

E

Q

D

T

K

R

P

D

E

D

V

I

M

D

A

A

V

I

H
|
H

A

A

H
|
H

P

T

V

T

N

Y

C

A

C

T

A

V

L

L

A

A

V

C

N

L

H

R

M

E

P

P

I

L

P

P

A

A

C

S

H

H

Y
|
Y

M

M

V

I

A

A

A

V

F

-

G

A

G

G

H

K

D

D

V

V

P

R

L

V

A

A

E

E

Y

Y

A

A

L

T

F

Y

G

G

T

T

T

K

E

E

L

L

S

A

A

V

H

N

V

A

A

K

A

A

M

M

A

E

D

G

R

R

E

R

G

A

C

V

L

L

M

L

A

A

N

N

H
|
H

G

G

A

I

I

L

C

A

T

G

G

A

D

Q

T

N

L

L

A

L

R

N

A

A

M

F

W

N

R

I

M

V

A

E

E

E

L

V

E

E

H

Y

L

C

A

A

A

K

T

I

Y

Y

I

C

R

L

A

A

R

K

S

N

I

F

G

G

T

E

P

P

R

V

L

V

L

L

S

P

S

D

A

E

Q

E

M

M

D

E

active site: E79 (= E83), H98 (= H102), H100 (= H104), Y119 (= Y123), H160 (= H165)
binding zinc ion: G30 (≠ S33), H98 (= H102), H100 (= H104), H160 (= H165)

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)
33% identity, 93% coverage: 13:219/223 of query aligns to 7:211/213 of P0DTQ0

query
sites
P0DTQ0

R

R

Q

E

S

E

I

I

I

V

D

A

A

Y

C

G

L

K

E

K

M

M

N

I

R

S

S

S

G

G

I

L

N

T

Q

K

G

G

T

T

S

G

G

G

N

N

I

I

S

S

L

I

-

F

R

N

I

R

A

E

G

Q

G

G

E

L

M

V

L

A

I

I

T

S

P

P

S

S

G

G

I

L

P

E

Y

Y

E

Y

A

E

M

T

S

K

P

P

D

E

M

D

I

V

V

V

R

I

M

L

P

N

V

L

V

D

G

G

S

-

P

-

D

E

P

V

Q

I

R

E

G

G

Q

E

P

R

S

K

P

P

S

S

E
|
E

W

L

Q

D

F

M

H

H

Q

L

A

I

L

Y

E

R

D

K

K

R

P

E

E

D

V

I

M

N

A

A

V

L

V

V

H
|
H

A

T

H
|
H

P

S

V

P

N

Y

C

A

C

K

A

T

L

I

A

A

V

S

N

L

H

G

M

W

P

E

I

L

P

P

A

A

C

V

H

S

Y

Y

M

L

V

I

A

A

A

-

F

F

G

A

G

G

H

P

D

N

V

V

P

R

L

C

A

A

E

P

Y

Y

A

E

L

T

F

F

G

G

T

T

T

K

E

Q

L

L

S

A

A

D

H

A

V

A

V

F

A

E

A

G

M

M

A

I

D

D

R

R

E

R

G

A

C

V

L

L

M

L

A

A

N

N

H
|
H

G

G

A

L

I

I

C

A

T

G

G

A

D

N

T

N

L

I

A

K

R

M

A

A

M

F

W

T

R

V

M

A

A

E

E

E

L

I

E

E

H

F

L

C

A

A

A

Q

T

I

Y

Y

I

Y

R

Q

A

T

R

K

S

S

I

I

G

G

T

E

P

P

R

K

L

L

S

P

S

E

A

D

Q

E

M

M

D

E

E

N

A

L

L

A

A

K

F

F

A

E

S

G

Y

Y

G

G

E76 (= E83) binding
H95 (= H102) binding
H97 (= H104) binding
H157 (= H165) binding

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
32% identity, 91% coverage: 13:215/223 of query aligns to 7:207/207 of 6btgA

query
sites
6btgA

R

R

Q

E

S

E

I

I

I

V

D

A

A

Y

C

G

L

K

E

K

M

M

N

I

R

S

S

S

G

G

I

L

N

T

Q

K

G

G

T

T

S

G

G

G

N

N

I

I

S

S

L

I

-

F

R

N

I

R

A

E

G

Q

G

G

E

L

M

V

L

A

I

I

T

S

P

P

S

S

G

G

I

L

P

E

Y

Y

E

Y

A

E

M

T

S

K

P

P

D

E

M

D

I

V

V

V

R

I

M

L

P

N

V

L

V

D

G

G

S

-

P

-

D

E

P

V

Q

I

R

E

G

G

Q

E

P

R

S

K

P

P

S

S

E
|
E

W

L

Q

D

F

M

H

H

Q

L

A

I

L

Y

E

R

D

K

K

R

P

E

E

D

V

I

M

N

A

A

V

L

V

V

H
|
H

A

T

H
|
H

P

S

V

P

N

Y

C

A

C

K

A

T

L

I

A

A

V

S

N

L

H

G

M

W

P

E

I

L

P

P

A

A

C

V

H

S

Y
|
Y

M

L

V

I

A

A

A

-

F

F

G

A

G

G

H

P

D

N

V

V

P

R

L

C

A

A

E

P

Y

Y

A

E

L

T

F

F

G

G

T

T

T

K

E

Q

L

L

S

A

A

D

H

A

V

A

V

F

A

E

A

G

M

M

A

I

D

D

R

R

E

R

G

A

C

V

L

L

M

L

A

A

N

N

H
|
H

G

G

A

L

I

I

C

A

T

G

G

A

D

N

T

N

L

I

A

K

R

M

A

A

M

F

W

T

R

V

M

A

A

E

E

E

L

I

E

E

H

F

L

C

A

A

A

Q

T

I

Y

Y

I

Y

R

Q

A

T

R

K

S

S

I

I

G

G

T

E

P

P

R

K

L

L

S

P

S

E

A

D

Q

E

M

M

D

E

E

N

A

L

L

A

A

K

F

F

active site: E76 (= E83), H95 (= H102), H97 (= H104), Y116 (= Y123), H157 (= H165)
binding manganese (ii) ion: E76 (= E83), H95 (= H102), H97 (= H104), H157 (= H165)

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
30% identity, 79% coverage: 12:188/223 of query aligns to 7:184/207 of 6voqA

query
sites
6voqA

L

L

R

R

Q

E

S

E

I

M

I

V

D

Q

A

I

C

G

L

A

E

S

M

L

N

F

R

S

S

R

G

G

I

Y

N

A

Q

T

G

G

T

S

S

A

G

G

N

N

I

L

S

S

L

L

R

L

I

L

A

P

G

D

G

G

E

N

M

L

L

L

I

A

T

T

P

P

S

T

G

G

I

A

P

C

Y

L

E

G

A

E

M

L

S

Q

P

A

D

Q

M

-

I

-

V

-

R

R

M

L

P

S

V

V

G

T

S

L

P

Q

D

G

P

E

Q

W

R

I

G

S

Q

G

P

D

S

K

P

P

S

S

S

K

E
|
E

W

V

Q

T

F

F

H

H

Q

R

A

A

L

V

L

Y

E

L

D

H

K

N

P

P

E

A

V

C

M

K

A

A

V

I

V

V

H
|
H

A

L

H
|
H

P

S

V

H

N

Y

C

L

C

T

A

A

L

L

A

S

V

C

-

L

-

Q

-

G

-

L

-

D

-

P

N

H

H

N

M

C

P

I

I

R

P

P

A

F

C

T

H

P

Y
|
Y

M

V

V

V

A

M

A

R

F

V

G

G

G

-

H

-

D

D

V

V

P

P

L

V

A

V

E

P

Y

Y

A

Y

L

R

F

P

G

G

T

D

E

R

L

I

S

-

A

A

H

Q

V

A

V

L

A

A

A

G

M

L

A

A

D

P

R

R

-

Y

E

N

G

A

C

F

L

L

M

L

A

A

N

N

H
|
H

G

G

A

P

I

V

C

V

T

T

G

G

D

S

T

S

L

L

A

R

R

E

A

A

M

T

W

N

R

N

M

T

A

E

E

E

L

L

E

E

H

E

L

T

A

A

active site: E75 (= E83), H94 (= H102), H96 (= H104), Y121 (= Y123), H161 (= H165)
binding zinc ion: E75 (= E83), H94 (= H102), H96 (= H104), H161 (= H165)

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)
22% identity, 79% coverage: 13:189/223 of query aligns to 3:171/181 of Q58813

query
sites
Q58813

R

K

Q

K

S

Q

I

F

I

I

D

K

A

I

C

C

L

R

E

K

M

L

N

Y

R

D

S

R

G

K

I

Y

N

V

Q

V

G

G

T

S

S

G

G

G

N
|
N

I

V

S

S

L

V

R

K

I

-

A

E

G

G

G

D

E

K

M

I

L

Y

I

L

T

T

P

P

S

T

G

G

I

S

P

I

Y

L

E

G

A

F

M

L

S

K

P

E

D

D

M

D

I

I

V

A

R

E

M

M

P

D

V

L

V

D

G

G

S

N

P

V

D

I

P

K

Q

G

R

K

G

-

Q

-

P

-

S

-

P

P

S

T

S

S

E

E

W

K

Q

N

F

L

H

H

Q

L

A

M

L

I

L

Y

E

R

D

K

K

R

P

N

E

D

V

I

M

N

A

A

V

I

H

H

A

T

H

H

P

S

V

L

N

I

C

S

C

T

A

F

L

L

A

S

V

T

N

I

H

N

M

K

P

E

I

I

-

E

-

L

-

T

P

P

A

E

C

G

H

K

Y

I

M

F

V

L

A

K

F

I

G

G

G

-

H

-

D

-

V

-

P

-

L

Y

A

V

E

D

Y

Y

A

Y

L

E

F

A

G

G

T

S

T

L

E

K

L

L

S

A

A

E

H

E

V

-

A

T

A

A

M

K

A

R

D

D

R

E

E

D

G

V

C

I

L

I

M

L

A

K

N

N

H

H

G

G

A

V

I

V

C

C

T

L

G

G

D

K

T

D

L

L

A

I

R

D

A

A

M

Y

W

I

R

K

M

V

A

E

E

V

L

L

E

E

H

E

L

Q

A

A

A

K

N25 (= N35) mutation to L: It shows a 3-fold increase of the affinty 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 affinty for dihydroxyacetone phosphate (DHAP), but has the same affinity for DL-glyceraldehyde compared to the wild-type.

2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
25% identity, 91% coverage: 9:211/223 of query aligns to 1:212/237 of 2z7bA

query
sites
2z7bA

S

S

D

F

T

T

L

M

R

R

Q

R

S

K

I

V

I

F

D

E

A

E

C

L

L

V

E

T

M

A

N

T

R

K

S

I

G

L

I

L

N

N

Q

E

G

G

-

I

-

M

-

D

T

T

S

F

G

G

N

H

I

I

S

S

L

A

R

R

I

D

A

P

G

E

-

D

-

P

G

A

E

S

M

F

L

F

I

L

T

A

P

Q

S

K

G

L

I

A

P

P

Y

-

E

S

A

L

M

I

S

T

P

V

D

D

M

D

I

I

V

Q

R

R

M

F

P

N

V

L

V

D

G

G

S

E

P

T

D

S

P

D

Q

N

R

R

G

-

Q

-

P

-

S

-

P

P

S

S

S

Y

-

L

E
|
E

W

R

Q

Y

F

I

H

H

Q

S

A

E

L

I

L

Y

E

K

D

T

K

R

P

P

E

D

V

V

M

Q

A

C

V

V

V

L

H
|
H

A

T

H
|
H

P

S

V

P

N

A

C

V

C

L

A

P

L

Y

A

C

V

F

N

V

H

D

M

T

P

P

I

L

-

R

P

P

A

V

C

T

H

H

Y

-

M

-

V

M

A

G

A

A

F

F

G

I

G

G

H

E

D

S

V

V

P

P

L

V

A

Y

E

E

Y

I

A

R

-

D

-

K

-

H

-

G

-

D

-

E

-

T

-

D

L

L

F

F

G

G

T

G

T

S

-

P

E

D

L

V

S

C

A

A

H

D

V

I

V

A

A

E

A

S

M

L

A

G

D

S

R

Q

E

T

G

V

C

V

L

L

M

M

A

A

N

R

H
|
H

G

G

A

V

I

V

C

N

T

V

G

G

D

K

T

S

L

V

A

R

R

E

A

V

M

V

W

F

R

R

M

A

A

F

E

Y

L

L

E

E

H

Q

L

E

A

A

T

A

Y

L

I

T

R

A

A

G

R

L

S

K

I

I

G

G

T

N

P

V

R

K

L

Y

L

L

S

S

S

P

A

G

Q

E

M

I

D

K

E

T

A

A

binding manganese (ii) ion: E76 (= E83), H95 (= H102), H97 (= H104), H166 (= H165)

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)
24% identity, 90% coverage: 12:211/223 of query aligns to 1:209/234 of Q988D0

query
sites
Q988D0

L

M

R

R

Q

R

S

K

I

V

I

F

D

E

A

E

C

L

L

V

E

T

M

A

N

T

R

K

S

I

G

L

I

L

N

N

Q

E

G

G

-

I

-

M

-

D

T

T

S

F

G

G

N

H

I

I

S

S

L

A

R

R

I

D

A

P

G

E

G

D

-

P

E

A

M

S

L

F

I

F

T

L

P

A

S

Q

G

K

I

L

P

A

Y

P

E

S

A

L

M

I

S

T

P

V

D

D

M

D

I

I

V

Q

R

R

M

F

P

N

V

L

V

D

G

G

S

E

P

T

D

S

P

D

Q

N

R

R

G

-

Q

-

P

-

S

-

P

P

S

S

S

Y

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E73 (= E83) binding
H92 (= H102) binding
H94 (= H104) binding
H163 (= H165) binding

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
23% identity, 87% coverage: 10:202/223 of query aligns to 3:207/231 of P08203

query
sites
P08203

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N28 (= N35) mutation to A: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
K42 (≠ T48) mutation to M: Strong decrease of the affinity for L-ribulose 5-phosphate (LRu5P).
D76 (≠ E83) 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 (= H102) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H104) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+). Inhibited by glycolaldehyde phosphate.
T116 (≠ Y123) 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 (≠ A127) mutation to N: Loss of the epimerase activity.
E142 (= E145) 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 (= H165) binding

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)
23% identity, 87% coverage: 10:202/223 of query aligns to 3:207/223 of 1jdiA

query
sites
1jdiA

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active site: D76 (≠ E83), H95 (= H102), H97 (= H104), T116 (≠ Y123), D120 (≠ A127), H171 (= H165)
binding zinc ion: H95 (= H102), H97 (= H104), H171 (= H165)

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
22% identity, 91% coverage: 12:215/223 of query aligns to 22:217/249 of 4xxfA

query
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4xxfA

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F

active site: G98 (≠ E83), H117 (= H102), H119 (= H104), Q138 (≠ Y123), H172 (= H165)
binding zinc ion: H117 (= H102), H119 (= H104), H172 (= H165)

Query Sequence

>GFF1603 FitnessBrowser__Phaeo:GFF1603
MTKPAPDDSDTLRQSIIDACLEMNRSGINQGTSGNISLRIAGGEMLITPSGIPYEAMSPD
MIVRMPVVGSPDPQRGQPSPSSEWQFHQALLEDKPEVMAVVHAHPVNCCALAVNHMPIPA
CHYMVAAFGGHDVPLAEYALFGTTELSAHVVAAMADREGCLMANHGAICTGDTLARAMWR
MAELEHLAATYIRARSIGTPRLLSSAQMDEALAAFASYGLKQD

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