SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 17942 b3902 rhamnulose-1-phosphate aldolase (NCBI) 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 4 hits to proteins with known functional sites (download)

1gt7A L-rhamnulose-1-phosphate aldolase from escherichia coli (see paper)
100% identity, 100% coverage: 1:274/274 of query aligns to 1:274/274 of 1gt7A

query
sites
1gt7A

M

M

Q

Q

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active site: E117 (= E117), H141 (= H141), H143 (= H143), E171 (= E171), H212 (= H212)
binding phosphoglycolohydroxamic acid: N29 (= N29), G30 (= G30), G31 (= G31), N32 (= N32), S75 (= S75), G76 (= G76), T115 (= T115), S116 (= S116), E117 (= E117), H141 (= H141), H143 (= H143), H212 (= H212)
binding zinc ion: H141 (= H141), H143 (= H143), H212 (= H212)

P32169 Rhamnulose-1-phosphate aldolase; EC 4.1.2.19 from Escherichia coli (strain K12) (see 2 papers)
100% identity, 100% coverage: 1:274/274 of query aligns to 1:274/274 of P32169

query
sites
P32169

M

M

Q

Q

N

N

I

I

T

T

Q

Q

S

S

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W

F

F

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V

Q

Q

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G

M

M

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I

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K

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A

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T

D

D

A

A

W

W

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L

K

K

G

G

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W

D

D

E

E

R
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R

N
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N

G

G

G

G

N

N

L

L

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T

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L

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R

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L

D

D

D

D

A

A

D

D

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P

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Y

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H

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D

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H

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F

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R28 (= R28) mutation R->A,S: Severe loss of enzymatic activity.
N29 (= N29) mutation to A: Severe loss of enzymatic activity.
E117 (= E117) active site; mutation to Q: Loss of enzymatic activity.
H141 (= H141) binding
H143 (= H143) binding
E171 (= E171) mutation E->S,A,Q: Loss of enzymatic activity.
E192 (= E192) mutation to A: No effect on enzymatic activity.
H212 (= H212) binding

1ojrA L-rhamnulose-1-phosphate aldolase from escherichia coli (mutant e192a) (see paper)
100% identity, 100% coverage: 1:274/274 of query aligns to 1:274/274 of 1ojrA

query
sites
1ojrA

M

M

Q

Q

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N

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I

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T

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Q

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S

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W

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F

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K

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D

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A

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W

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D

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E

R

R

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G
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G

G
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G

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L

L

T

T

L

L

R

R

L

L

D

D

D

D

A

A

D

D

I

I

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A

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H

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D

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N

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F

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M

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L

active site: E117 (= E117), H141 (= H141), H143 (= H143), E171 (= E171), H212 (= H212)
binding Dihydroxyacetone: N29 (= N29), G30 (= G30), G31 (= G31), N32 (= N32), E117 (= E117), H141 (= H141), H143 (= H143), H212 (= H212)
binding phosphate ion: N29 (= N29), N32 (= N32), N32 (= N32), S75 (= S75), G76 (= G76), T115 (= T115), S116 (= S116), E117 (= E117), H141 (= H141), H212 (= H212)
binding zinc ion: H141 (= H141), H143 (= H143), H212 (= H212)

2v9mA L-rhamnulose-1-phosphate aldolase from escherichia coli (mutant a87m- t109f-e192a) (see paper)
99% identity, 100% coverage: 1:274/274 of query aligns to 1:274/274 of 2v9mA

query
sites
2v9mA

M

M

Q

Q

N

N

I

I

T

T

Q

Q

S

S

W

W

F

F

V

V

Q

Q

G

G

M

M

I

I

K

K

A

A

T

T

T

T

D

D

A

A

W

W

L

L

K

K

G

G

W

W

D

D

E

E

R

R

N

N

G

G

G

G

N

N

L

L

T

T

L

L

R

R

L

L

D

D

D

D

A

A

D

D

I

I

A

A

P

P

Y

Y

H

H

D

D

N

N

F

F

H

H

Q

Q

Q

Q

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P

R

R

Y

Y

I

I

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P

L

L

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S

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Q

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P

M

M

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P

L

L

L

L

A

A

N

N

T

T

P

P

F

F

I

I

V

V

T

T

G

G

S

S

G

G

K

K

F

F

F

F

R

R

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V

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Q

L

L

D

D

P

P

A

M

A

A

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L

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G

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I

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V

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K

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D

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S

D

D

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G

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A

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G

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Y

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G

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L

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F

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H

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C

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E

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R

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I

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K

A

A

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T

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G

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K

D

D

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I

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A

A

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T

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N

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L

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I

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A

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T

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Y

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L

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E

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Q

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S

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H

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F

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L

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D

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L

active site: E117 (= E117), H141 (= H141), H143 (= H143), E171 (= E171), H212 (= H212)
binding calcium ion: E200 (= E200), H204 (= H204)
binding zinc ion: H141 (= H141), H143 (= H143), H212 (= H212)

Query Sequence

>17942 b3902 rhamnulose-1-phosphate aldolase (NCBI)
MQNITQSWFVQGMIKATTDAWLKGWDERNGGNLTLRLDDADIAPYHDNFHQQPRYIPLSQ
PMPLLANTPFIVTGSGKFFRNVQLDPAANLGIVKVDSDGAGYHILWGLTNEAVPTSELPA
HFLSHCERIKATNGKDRVIMHCHATNLIALTYVLENDTAVFTRQLWEGSTECLVVFPDGV
GILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAQVLVK
VYSMGGMKQTISREELIALGKRFGVTPLASALAL

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