SitesBLAST

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)
33% identity, 84% coverage: 11:191/215 of query aligns to 3:175/181 of Q58813

query
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Q58813

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N25 (= N33) 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.

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
30% identity, 88% coverage: 1:189/215 of query aligns to 1:181/206 of 4fuaA

query
sites
4fuaA

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active site: E73 (≠ T77), H92 (= H96), H94 (= H98), Y113 (= Y123), A117 (≠ K127), H155 (≠ L163)
binding phosphoglycolohydroxamic acid: G28 (= G32), N29 (= N33), T43 (= T47), S71 (= S75), S72 (≠ K76), E73 (≠ T77), H92 (= H96), H94 (= H98), H155 (≠ L163)
binding zinc ion: H92 (= H96), H94 (= H98), H155 (≠ L163)

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)
30% identity, 88% coverage: 1:189/215 of query aligns to 1:181/215 of P0AB87

query
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P0AB87

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T26 (≠ S30) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (= A31) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 32:33) binding
N29 (= N33) 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 (≠ TD 47:48) binding
S71 (= S75) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (≠ SK 75:76) binding
E73 (≠ T77) 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 (= H96) binding
H94 (= H98) 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 (≠ P139) 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 (≠ L163) binding

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)
30% identity, 88% coverage: 1:189/215 of query aligns to 1:181/210 of 2fuaA

query
sites
2fuaA

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active site: E73 (≠ T77), H92 (= H96), H94 (= H98), Y113 (= Y123), A117 (≠ K127), H155 (≠ L163)
binding cobalt (ii) ion: E73 (≠ T77), H92 (= H96), H94 (= H98), H155 (≠ L163)

Sites not aligning to the query:

active site: 209

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
30% identity, 88% coverage: 1:189/215 of query aligns to 1:181/209 of 1dzuP

query
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1dzuP

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binding zinc ion: E73 (≠ T77), H92 (= H96), H94 (= H98), H155 (≠ L163)

7x78A L-fuculose 1-phosphate aldolase (see paper)
31% identity, 82% coverage: 30:206/215 of query aligns to 23:193/203 of 7x78A

query
sites
7x78A

S

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T

L

A

A

K

Q

L

L

W

Y

H

L

L

S

A

T

G

L

G

A

R

I

A

T

T

D

P

P

L

V

E

-

P

P

A

V

L

L

E

D

D

D

binding magnesium ion: E70 (≠ T77), H89 (= H96), H91 (= H98), H152 (≠ L163)
binding sulfate ion: N26 (= N33), T40 (= T47), H61 (≠ W68), Q63 (≠ S70), S68 (= S75), S69 (≠ K76)

Sites not aligning to the query:

binding sulfate ion: 5, 8

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)
28% identity, 94% coverage: 11:213/215 of query aligns to 7:209/213 of P0DTQ0

query
sites
P0DTQ0

R

R

E

E

I

I

C

V

R

A

I

Y

G

G

A

K

S

K

L

M

Y

I

Q

S

R

S

G

G

Y

L

T

T

V

K

G

G

S

T

A

G

G

G

N

N

I

I

S

S

A

I

R

F

L

N

E

R

D

E

G

Q

W

G

L

L

I

V

T

A

P

I

T

S

D

P

A

S

C

G

L

L

G

E

F

Y

L

Y

D

E

-

T

-

K

P

P

A

E

A

D

I

V

A

V

K

I

V

L

N

N

A

L

A

D

G

G

E

E

W

V

V

I

S

E

G

G

D

E

-

R

K

K

P

P

S

S

K

S

T
x
E

L

L

V

D

L

M

H

H

R

L

A

I

I

Y

Y

Y

D

R

N

K

N

R

P

E

E

D

M

I

H

N

A

A

V

L

V

V

H
|
H

T

T

H
|
H

S

S

T

P

H

Y

L

-

V

-

S

A

L

K

T

T

I

I

N

A

G

S

V

L

Y

G

S

W

E

E

Q

-

D

-

V

-

L

L

P

P

P

A

I

V

T

S

P

-

Y

Y

Y

L

V

I

M

A

K

F

V

A

G

G

H

-

I

-

P

P

L

N

I

V

R

R

-

C

-

A

-

P

Y

Y

A

E

R

T

P

F

G

G

A

T

P

K

E

Q

V

L

A

A

E

D

Q

A

V

A

A

F

K

E

I

G

A

M

T

I

Q

D

V

R

R

R

G

A

V

V

L

L

E

A

R

N

L
x
H

G

G

P

L

V

I

V

A

W

G

E

A

S

N

V

I

S

K

K

M

A

A

A

F

F

T

A

V

L

A

E

E

L

I

E

E

E

F

T

C

A

A

K

Q

L

I

W

Y

H

Y

L

Q

A

T

G

K

G

S

R

I

A

G

T

E

P

P

-

K

-

L

L

L

E

P

E

E

P

D

A

E

L

M

E

E

D

N

L

L

R

A

A

K

T

K

F

F

K

E

A

G

E76 (≠ T77) binding
H95 (= H96) binding
H97 (= H98) binding
H157 (≠ L163) binding

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
28% identity, 93% coverage: 11:211/215 of query aligns to 7:207/207 of 6btgA

query
sites
6btgA

R

R

E

E

I

I

C

V

R

A

I

Y

G

G

A

K

S

K

L

M

Y

I

Q

S

R

S

G

G

Y

L

T

T

V

K

G

G

S

T

A

G

G

G

N

N

I

I

S

S

A

I

R

F

L

N

E

R

D

E

G

Q

W

G

L

L

I

V

T

A

P

I

T

S

D

P

A

S

C

G

L

L

G

E

F

Y

L

Y

D

E

-

T

-

K

P

P

A

E

A

D

I

V

A

V

K

I

V

L

N

N

A

L

A

D

G

G

E

E

W

V

V

I

S

E

G

G

D

E

-

R

K

K

P

P

S

S

K

S

T
x
E

L

L

V

D

L

M

H

H

R

L

A

I

I

Y

Y

Y

D

R

N

K

N

R

P

E

E

D

M

I

H

N

A

A

V

L

V

V

H
|
H

T

T

H
|
H

S

S

T

P

H

Y

L

-

V

-

S

A

L

K

T

T

I

I

N

A

G

S

V

L

Y

G

S

W

E

E

Q

-

D

-

V

-

L

L

P

P

P

A

I

V

T

S

P

-

Y
|
Y

Y

L

V

I

M

A

K

F

V

A

G

G

H

-

I

-

P

P

L

N

I

V

R

R

-

C

-

A

-

P

Y

Y

A

E

R

T

P

F

G

G

A

T

P

K

E

Q

V

L

A

A

E

D

Q

A

V

A

A

F

K

E

I

G

A

M

T

I

Q

D

V

R

R

R

G

A

V

V

L

L

E

A

R

N

L
x
H

G

G

P

L

V

I

V

A

W

G

E

A

S

N

V

I

S

K

K

M

A

A

A

F

F

T

A

V

L

A

E

E

L

I

E

E

E

F

T

C

A

A

K

Q

L

I

W

Y

H

Y

L

Q

A

T

G

K

G

S

R

I

A

G

T

E

P

P

-

K

-

L

L

L

E

P

E

E

P

D

A

E

L

M

E

E

D

N

L

L

R

A

A

K

T

K

F

F

active site: E76 (≠ T77), H95 (= H96), H97 (= H98), Y116 (= Y123), H157 (≠ L163)
binding manganese (ii) ion: E76 (≠ T77), H95 (= H96), H97 (= H98), H157 (≠ L163)

4c25A L-fuculose 1-phosphate aldolase (see paper)
25% identity, 95% coverage: 8:212/215 of query aligns to 7:211/212 of 4c25A

query
sites
4c25A

S

S

A

D

L

V

R

K

E

Q

E

E

I

L

C

I

R

K

I

Y

G

G

A

K

S

K

L

L

Y

V

Q

E

R

T

G

D

Y

L

T

T

V

K

G

G

S

T

A
x
G

G

G

N

N

I

L

S

S

A

V

R

F

L

D

E

R

D

E

G

K

W

Q

L

L

I

M

T

A

P

I

T

T

D

P

A

S

C

G

L

I

G

D

F

F

L

F

D

E

-

I

-

K

P

E

A

S

A

D

I

I

A

V

K

V

V

M

N

D

A

I

A

N

G

G

E

N

W

V

V

V

S

E

G

G

D

E

K

R

-

L

P

P

S

S

K

S

T
x
E

L

W

V

Y

L

M

H

H

R

L

A

I

I

Q

Y

Y

D

Q

N

T

N

R

P

D

E

D

M

I

H

D

A

A

V

I

H
|
H

T

A

H
|
H

S

T

T

T

H

Y

L

A

V

T

S

V

L

L

T

A

I

-

N

-

G

-

V

-

Y

-

S

C

E

L

Q

R

D

E

V

P

L

L

P

P

P

-

I

-

T

A

P

S

Y

H

Y
|
Y

V

M

M

I

K

A

V

V

G

A

-

G

-

K

H

D

I

V

P

R

L

V

I

A

R

E

Y

Y

A

A

R

T

P

Y

G

G

A

T

P

K

E

E

V

L

A

A

E

V

Q

N

V

A

A

A

K

K

I

A

A

M

T

E

Q

G

V

R

R

R

G

A

V

V

L

L

E

A

R

N

L
x
H

G

G

P

I

V

L

V

A

W

G

E

A

S

Q

S

N

V

L

S

L

K

N

A

A

A

F

F

N

A

I

L

V

E

E

L

V

E

E

E

Y

T

C

A

A

K

K

L

I

W

Y

H

C

L

L

A

A

G

K

G

N

R

F

A

G

T

E

P

P

-

V

L

L

E

P

E

D

P

E

A

E

L

M

E

E

D

L

L

M

R

A

A

E

T

K

F

F

K

K

active site: E79 (≠ T77), H98 (= H96), H100 (= H98), Y119 (= Y124), H160 (≠ L163)
binding zinc ion: G30 (≠ A31), H98 (= H96), H100 (= H98), H160 (≠ L163)

Query Sequence

>HSERO_RS21150 FitnessBrowser__HerbieS:HSERO_RS21150
MSRNTNESALREEICRIGASLYQRGYTVGSAGNISARLEDGWLITPTDACLGFLDPAAIA
KVNAAGEWVSGDKPSKTLVLHRAIYDNNPEMHAVVHTHSTHLVSLTINGVYSEQDVLPPI
TPYYVMKVGHIPLIRYARPGAPEVAEQVAKIATQVRGVLLERLGPVVWESSVSKAAFALE
ELEETAKLWHLAGGRATPLEEPALEDLRATFKARW

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