SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 3607101 FitnessBrowser__Dino:3607101 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 17 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, 90% coverage: 15:222/231 of query aligns to 8:215/215 of P0AB87

query
sites
P0AB87

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L

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T

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L

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E

T26 (= T33) mutation to A: Decrease of the aldolase activity mostly due to a decrease of the affinity for L-fuculose 1-phosphate (Fuc1P).
A27 (≠ S34) mutation Missing: Strong decrease of the aldolase activity.
GN 28:29 (= GN 35:36) binding
N29 (= N36) 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 (= S79) mutation to A: Loss of aldolase activity; when associated with L-29.; mutation to Q: Loss of aldolase activity.
SS 71:72 (= SS 79:80) binding
E73 (= E81) 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 (= H100) binding
H94 (= H102) binding
Y113 (= Y121) 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 (= F139) 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 (= H163) binding
F206 (= F213) 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.
207:215 (vs. 214:222, 44% identical) mutation Missing: Loss of aldolase activity. Has a slight preference for the D-aldehyde.
Y209 (= Y216) 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.
LRIEE 211:215 (≠ PRHPE 218:222) 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)
45% identity, 88% coverage: 15:217/231 of query aligns to 8:210/210 of 2fuaA

query
sites
2fuaA

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active site: E73 (= E81), H92 (= H100), H94 (= H102), Y113 (= Y121), A117 (= A125), H155 (= H163), Y209 (= Y216)
binding cobalt (ii) ion: E73 (= E81), H92 (= H100), H94 (= H102), H155 (= H163)

1dzuP L-fuculose-1-phosphate aldolase from escherichia coli mutant t26a (see paper)
44% identity, 87% coverage: 15:216/231 of query aligns to 8:209/209 of 1dzuP

query
sites
1dzuP

Q

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L

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Y

binding zinc ion: E73 (= E81), H92 (= H100), H94 (= H102), H155 (= H163)

4fuaA L-fuculose-1-phosphate aldolase complex with pgh (see paper)
45% identity, 86% coverage: 15:213/231 of query aligns to 8:206/206 of 4fuaA

query
sites
4fuaA

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active site: E73 (= E81), H92 (= H100), H94 (= H102), Y113 (= Y121), A117 (= A125), H155 (= H163)
binding phosphoglycolohydroxamic acid: G28 (= G35), N29 (= N36), T43 (≠ S50), S71 (= S79), S72 (= S80), E73 (= E81), H92 (= H100), H94 (= H102), H155 (= H163)
binding zinc ion: H92 (= H100), H94 (= H102), H155 (= H163)

7x78A L-fuculose 1-phosphate aldolase (see paper)
43% identity, 85% coverage: 17:213/231 of query aligns to 10:203/203 of 7x78A

query
sites
7x78A

L

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D

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K

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F

binding magnesium ion: E70 (= E81), H89 (= H100), H91 (= H102), H152 (= H163)
binding sulfate ion: N26 (= N36), T40 (≠ S50), H61 (≠ D72), Q63 (≠ N74), S68 (= S79), S69 (= S80)

Sites not aligning to the query:

binding sulfate ion: 5, 8

4c25A L-fuculose 1-phosphate aldolase (see paper)
35% identity, 85% coverage: 10:206/231 of query aligns to 6:203/212 of 4c25A

query
sites
4c25A

T

S

A

D

T

V

R

K

Q

Q

A

E

L

L

I

I

D

K

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K

G

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x
G

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G

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N

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F

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K

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P

D

D

D

M

I

P

D

V

A

V

I

L

I

H
|
H

A

A

H
|
H

P

T

Y

Y

C

A

S

T

V

V

L

L

A

A

V

C

Q

L

R

R

R

E

S

P

I

L

P

P

A

A

C

S

H

H

Y
|
Y

M

M

I

I

A

A

A

V

F

-

G

A

G

G

N

K

D

D

V

V

P

R

L

V

A

A

D

E

Y

Y

A

A

L

T

F

Y

G

G

S

T

P

K

E

E

L

L

C

A

A

V

N

N

M

A

A

A

R

K

I

A

M

M

A

E

D

G

R

R

H

R

G

A

C

V

L

L

M

L

A

A

N

N

H
|
H

G

G

A

I

T

L

V

A

L

G

G

A

E

Q

T

N

V

L

D

L

K

N

A

A

R

F

W

N

R

I

L

V

E

E

L

V

E

E

T

Y

L

C

A

A

R

K

T

I

Y

Y

L

C

F

L

S

A

S

K

I

N

G

F

G

G

A

E

P

P

H

V

I

V

L

L

S

P

D

D

A

E

E

E

I

M

active site: E79 (= E81), H98 (= H100), H100 (= H102), Y119 (= Y121), H160 (= H163)
binding zinc ion: G30 (≠ S34), H98 (= H100), H100 (= H102), H160 (= H163)

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, 89% coverage: 14:219/231 of query aligns to 7:213/213 of P0DTQ0

query
sites
P0DTQ0

R

R

Q

E

A

E

L

I

I

V

D

A

A

Y

C

G

L

K

W

K

M

M

N

I

A

S

R

S

H

G

L

L

N

T

Q

K

G

G

T

T

S

G

G

G

N

N

I

I

S

S

A

I

-

F

-

N

R

R

I

E

A

Q

S

G

G

L

I

V

L

A

I

I

T

S

P

P

S

S

G

G

V

L

P

E

Y

Y

E

Y

Y

E

L

T

T

K

P

P

D

E

A

D

L

V

V

V

T

I

I

L

P

N

L

L

D

D

G

G

L

E

P

V

D

I

S

E

N

G

G

E

A

R

Q

K

P

P

S

S

E
|
E

W

L

P

D

F

M

H

H

Q

L

G

I

M

Y

H

Y

Q

R

A

K

R

R

P

E

D

D

M

I

P

N

V

A

V

L

L

V

H
|
H

A

T

H
|
H

P

S

P

P

Y

Y

C

A

S

K

V

T

L

I

A

A

V

S

Q

L

R

G

R

W

S

E

I

L

P

P

A

A

C

V

H

S

Y

Y

M

L

I

I

A

-

A

A

F

F

G

A

G

G

N

P

D

N

V

V

P

R

L

C

A

A

D

P

Y

Y

A

E

L

T

F

F

G

G

S

T

P

K

E

Q

L

L

C

A

A

D

N

A

M

A

A

F

R

E

I

G

M

M

A

I

D

D

R

R

H

R

G

A

C

V

L

L

M

L

A

A

N

N

H
|
H

G

G

A

L

T

I

V

A

L

G

G

A

E

N

T

N

V

I

D

K

K

M

A

A

R

F

W

T

R

V

L

A

E

E

L

I

E

E

T

F

L

C

A

A

R

Q

T

I

Y

Y

L

Y

F

Q

S

T

S

K

I

S

G

I

G

G

A

E

P

P

H

K

I

L

L

L

S

P

D

E

A

D

E

E

I

M

A

E

E

N

V

L

M

A

V

K

A

K

F

F

S

E

S

G

Y

Y

G

G

P

Q

R

Q

E76 (= E81) binding
H95 (= H100) binding
H97 (= H102) binding
H157 (= H163) binding

6btgA Crystal structure of deoxyribose-phosphate aldolase bound with dhap from bacillus thuringiensis (see paper)
32% identity, 87% coverage: 14:213/231 of query aligns to 7:207/207 of 6btgA

query
sites
6btgA

R

R

Q

E

A

E

L

I

I

V

D

A

A

Y

C

G

L

K

W

K

M

M

N

I

A

S

R

S

H

G

L

L

N

T

Q

K

G

G

T

T

S

G

G

G

N

N

I

I

S

S

A

I

-

F

-

N

R

R

I

E

A

Q

S

G

G

L

I

V

L

A

I

I

T

S

P

P

S

S

G

G

V

L

P

E

Y

Y

E

Y

Y

E

L

T

T

K

P

P

D

E

A

D

L

V

V

V

T

I

I

L

P

N

L

L

D

D

G

G

L

E

P

V

D

I

S

E

N

G

G

E

A

R

Q

K

P

P

S

S

E
|
E

W

L

P

D

F

M

H

H

Q

L

G

I

M

Y

H

Y

Q

R

A

K

R

R

P

E

D

D

M

I

P

N

V

A

V

L

L

V

H
|
H

A

T

H
|
H

P

S

P

P

Y

Y

C

A

S

K

V

T

L

I

A

A

V

S

Q

L

R

G

R

W

S

E

I

L

P

P

A

A

C

V

H

S

Y
|
Y

M

L

I

I

A

-

A

A

F

F

G

A

G

G

N

P

D

N

V

V

P

R

L

C

A

A

D

P

Y

Y

A

E

L

T

F

F

G

G

S

T

P

K

E

Q

L

L

C

A

A

D

N

A

M

A

A

F

R

E

I

G

M

M

A

I

D

D

R

R

H

R

G

A

C

V

L

L

M

L

A

A

N

N

H
|
H

G

G

A

L

T

I

V

A

L

G

G

A

E

N

T

N

V

I

D

K

K

M

A

A

R

F

W

T

R

V

L

A

E

E

L

I

E

E

T

F

L

C

A

A

R

Q

T

I

Y

Y

L

Y

F

Q

S

T

S

K

I

S

G

I

G

G

A

E

P

P

H

K

I

L

L

L

S

P

D

E

A

D

E

E

I

M

A

E

E

N

V

L

M

A

V

K

A

K

F

F

active site: E76 (= E81), H95 (= H100), H97 (= H102), Y116 (= Y121), H157 (= H163)
binding manganese (ii) ion: E76 (= E81), H95 (= H100), H97 (= H102), H157 (= H163)

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)
25% identity, 77% coverage: 14:192/231 of query aligns to 3:176/181 of Q58813

query
sites
Q58813

R

K

Q

K

A

Q

L

F

I

I

D

K

A

I

C

C

L

R

W

K

M

L

N

Y

A

D

R

R

H

K

L

Y

N

V

Q

V

G

G

T

S

S

G

G

G

N
|
N

I

V

S

S

A

V

R

K

I

E

A

G

S

D

G

K

I

I

L

Y

I

L

T

T

P

P

S

T

G

G

V

S

P

I

Y

L

E

G

Y

F

L

L

T

K

P

E

D

D

A

D

L

I

V

A

T

E

I

M

P

D

L

L

D

D

G

G

L

-

P

-

D

N

S

V

N

I

G

K

A

G

Q

K

P

P

S

T

S

S

E

E

W

K

P

N

F

L

H

H

Q

L

G

M

M

I

H

Y

Q

R

A

K

R

R

P

N

D

D

M

I

P

N

V

A

V

I

L

I

H

H

A

T

H

H

P

S

P

L

Y

I

C

S

S

T

V

F

L

L

A

S

V

T

Q

I

R

N

R

K

S

E

I

I

-

E

-

L

-

T

P

P

A

E

C

G

H

K

Y

I

M

F

I

L

A

K

F

I

G

G

G

-

N

-

D

-

V

-

P

-

L

Y

A

V

D

D

Y

Y

A

Y

L

E

F

A

G

G

S

S

P

L

E

K

L

L

C

A

A

E

N

E

M

T

A

A

R

K

I

-

M

-

A

R

D

D

R

E

H

D

G

V

C

I

L

I

M

L

A

K

N

N

H

H

G

G

A

V

T

V

V

C

L

L

G

G

E

K

T

D

V

L

D

I

K

D

A

A

R

Y

W

I

R

K

L

V

E

E

E

V

L

L

E

E

T

E

L

Q

A

A

R

K

T

L

Y

T

L

L

F

L

S

N

N25 (= N36) 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.

6voqA Crystal structure of ygbl, a putative aldolase/epimerase/decarboxylase from klebsiella pneumoniae
27% identity, 85% coverage: 14:209/231 of query aligns to 8:206/207 of 6voqA

query
sites
6voqA

R

R

Q

E

A

E

L

M

I

V

D

Q

A

I

C

G

L

A

W

S

M

L

N

F

A

S

R

R

H

G

L

Y

N

A

Q

T

G

G

T

S

S

A

G

G

N

N

I

L

S

S

A

L

R

L

I

L

A

P

S

D

G

G

-

N

I

L

L

L

I

A

T

T

P

P

S

T

G

G

V

A

P

C

Y

L

E

G

Y

E

L

L

T

Q

P

A

D

Q

A

R

L

L

V

S

T

V

I

V

P

T

L

L

D

Q

G

G

L

E

P

W

D

I

S

S

N

-

G

G

A

D

Q

K

P

P

S

S

S

K

E
|
E

W

V

P

T

F

F

H

H

Q

R

G

A

M

V

H

Y

Q

L

A

H

R

N

P

P

D

A

M

C

P

K

V

A

V

I

L

V

H
|
H

A

L

H
|
H

P

S

P

H

Y

Y

C

L

S

T

V

A

L

L

A

S

V

C

Q

L

R

Q

-

G

-

L

-

D

-

P

-

H

R

N

S

C

I

I

-

R

P

P

A

F

C

T

H

P

Y
|
Y

M

V

I

V

A

M

A

R

F

V

G

G

G

-

N

-

D

D

V

V

P

P

L

V

A

V

D

P

Y

Y

A

Y

L

R

F

P

G

G

S

D

P

D

E

R

L

I

C

A

A

Q

N

A

M

L

A

A

R

G

I

L

M

A

A

P

D

R

R

Y

H

N

G

A

C

F

L

L

M

L

A

A

N

N

H
|
H

G

G

A

P

T

V

V

V

L

T

G

G

E

S

T

S

V

L

D

R

K

E

A

A

R

T

W

N

R

N

L

T

E

E

L

L

E

E

T

E

L

T

A

A

R

R

T

-

Y

L

L

I

F

F

S

T

S

L

I

G

G

N

G

R

A

E

P

I

H

R

I

Y

L

L

S

T

D

A

A

D

E

E

I

V

A

K

E

E

V

L

active site: E75 (= E81), H94 (= H100), H96 (= H102), Y121 (= Y121), H161 (= H163)
binding zinc ion: E75 (= E81), H94 (= H100), H96 (= H102), H161 (= H163)

2z7bA Crystal structure of mesorhizobium loti 3-hydroxy-2-methylpyridine-4, 5-dicarboxylate decarboxylase (see paper)
32% identity, 75% coverage: 14:186/231 of query aligns to 5:189/237 of 2z7bA

query
sites
2z7bA

R

R

Q

R

A

K

L

V

I

F

D

E

A

E

C

L

L

V

W

T

M

A

N

T

A

K

R

I

H

L

L

L

N

N

Q

E

G

G

-

I

-

M

-

D

T

T

S

F

G

G

N

H

I

I

S

S

A

A

R

R

I

D

-

P

-

E

-

D

-

P

A

A

S

S

G

F

I

F

L

L

-

A

-

Q

-

K

I

L

T

A

P

P

S

S

G

-

V

-

P

-

Y

-

E

-

Y

L

L

I

T

T

P

V

D

D

A

D

L

I

V

Q

T

R

I

F

P

N

L

L

D

D

G

G

L

E

P

T

D

S

S

D

N

N

G

-

A

-

Q

R

P

P

S

S

S

Y

-

L

E
|
E

W

R

P

Y

F

I

H

H

Q

S

G

E

M

I

H

Y

Q

K

A

T

R

R

P

P

D

D

M

V

P

Q

V

C

V

V

L

L

H
|
H

A

T

H
|
H

P

S

P

P

-

A

-

V

-

L

-

P

Y

Y

C

C

S

F

V

V

L

D

A

T

V

P

Q

L

R

R

R

-

S

-

I

-

P

P

A

V

C

T

H

H

Y

-

M

-

I

M

A

G

A

A

F

F

G

I

G

G

N

E

D

S

V

V

P

P

L

V

A

Y

D

E

Y

I

A

R

-

D

-

K

-

H

-

G

-

D

-

E

-

T

-

D

L

L

F

F

G

G

-

G

S

S

P

P

E

D

L

V

C

C

A

A

N

D

M

I

A

A

R

E

I

S

M

L

A

G

D

S

R

Q

H

T

G

V

C

V

L

L

M

M

A

A

N

R

H
|
H

G

G

A

V

T

V

V

N

L

V

G

G

E

K

T

S

V

V

D

R

K

E

A

V

R

V

W

F

R

R

L

A

E

F

E

Y

L

L

E

E

T

Q

L

E

A

A

binding manganese (ii) ion: E76 (= E81), H95 (= H100), H97 (= H102), H166 (= H163)

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)
32% identity, 75% coverage: 14:186/231 of query aligns to 2:186/234 of Q988D0

query
sites
Q988D0

R

R

Q

R

A

K

L

V

I

F

D

E

A

E

C

L

L

V

W

T

M

A

N

T

A

K

R

I

H

L

L

L

N

N

Q

E

G

G

-

I

-

M

-

D

T

T

S

F

G

G

N

H

I

I

S

S

A

A

R

R

I

D

-

P

-

E

-

D

-

P

A

A

S

S

G

F

I

F

L

L

-

A

-

Q

-

K

I

L

T

A

P

P

S

S

G

-

V

-

P

-

Y

-

E

-

Y

L

L

I

T

T

P

V

D

D

A

D

L

I

V

Q

T

R

I

F

P

N

L

L

D

D

G

G

L

E

P

T

D

S

S

D

N

N

G

-

A

-

Q

R

P

P

S

S

S

Y

-

L

E
|
E

W

R

P

Y

F

I

H

H

Q

S

G

E

M

I

H

Y

Q

K

A

T

R

R

P

P

D

D

M

V

P

Q

V

C

V

V

L

L

H
|
H

A

T

H
|
H

P

S

P

P

-

A

-

V

-

L

-

P

Y

Y

C

C

S

F

V

V

L

D

A

T

V

P

Q

L

R

R

R

-

S

-

I

-

P

P

A

V

C

T

H

H

Y

-

M

-

I

M

A

G

A

A

F

F

G

I

G

G

N

E

D

S

V

V

P

P

L

V

A

Y

D

E

Y

I

A

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-

D

-

K

-

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-

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-

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D

L

L

F

F

G

G

-

G

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P

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D

L

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C

C

A

A

N

D

M

I

A

A

R

E

I

S

M

L

A

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D

S

R

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C

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L

L

M

M

A

A

N

R

H
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H

G

G

A

V

T

V

V

N

L

V

G

G

E

K

T

S

V

V

D

R

K

E

A

V

R

V

W

F

R

R

L

A

E

F

E

Y

L

L

E

E

T

Q

L

E

A

A

E73 (= E81) binding
H92 (= H100) binding
H94 (= H102) binding
H163 (= H163) binding

1jdiA Crystal structure of l-ribulose-5-phosphate 4-epimerase (see paper)
26% identity, 77% coverage: 14:191/231 of query aligns to 6:199/223 of 1jdiA

query
sites
1jdiA

R

K

Q

R

A

Q

L

V

I

L

D

E

A

A

C

N

L

L

W

A

M

L

N

P

A

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H

H

N

L

L

N

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L

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G

G

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N

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A

A

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-

D

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Y

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A

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L

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G

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K

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x
D

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x
T

M

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A

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x
D

F

Y

G

F

G

Y

N

G

D

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I

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P

-

C

-

T

-

R

-

K

L

M

A

T

D

D

Y

A

A

E

L

I

F

N

G

G

S

E

P

Y

E

E

L

W

-

E

C

T

A

G

N

N

M

V

A

I

R

V

I

E

M

T

A

F

D

E

R

K

H

Q

-

G

-

I

-

D

-

A

-

Q

-

M

-

P

G

G

C

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L

L

M

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N

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H

G

G

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P

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F

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A

L

W

G

G

E

K

T

N

V

A

D

E

K

D

A

A

R

V

W

H

R

N

L

A

E

I

E

V

L

L

E

E

T

E

L

V

A

A

R

Y

T

M

Y

G

L

I

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F

active site: D76 (≠ E81), H95 (= H100), H97 (= H102), T116 (≠ Y121), D120 (≠ A125), H171 (= H163)
binding zinc ion: H95 (= H100), H97 (= H102), H171 (= H163)

P08203 L-ribulose-5-phosphate 4-epimerase AraD; Phosphoribulose isomerase; EC 5.1.3.4 from Escherichia coli (strain K12) (see 4 papers)
26% identity, 77% coverage: 14:191/231 of query aligns to 6:199/231 of P08203

query
sites
P08203

R

K

Q

R

A

Q

L

V

I

L

D

E

A

A

C

N

L

L

W

A

M

L

N

P

A

K

R

H

H

N

L

L

N

V

Q

T

G

L

T

T

S

W

G

G

N
|
N

I

V

S

S

A

A

-

V

-

D

R

R

I

E

A

R

S

G

G

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I

F

L

V

I

I

T
x
K

P

P

S

S

G

G

V

V

P

D

Y

Y

E

S

Y

V

L

M

T

T

P

A

D

D

A

D

L

M

V

V

T

V

I

V

P

S

L

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D

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-

T

G

G

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N

G

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K

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x
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T

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A

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Q

A

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S

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I

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P

A

A

C

T

H

G

Y
x
T

M

T

I

H

A

A

A
x
D

F

Y

G

F

G

Y

N

G

D

T

V

I

P

P

-

C

-

T

-

R

-

K

L

M

A

T

D

D

Y

A

A

E

L

I

F

N

G

G

S

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P

Y

E
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E

L

W

-

E

C

T

A

G

N

N

M

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A

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R

V

I

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M

T

A

F

D

E

R

K

H

Q

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G

-

I

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D

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A

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M

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G

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H
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H

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G

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F

V

A

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G

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T

N

V

A

D

E

K

D

A

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F

N28 (= N36) 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 (≠ E81) 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 (= H100) binding ; mutation to N: Mutant shows a strong decrease of the catalytic efficiency and a reduced affinity for Zn(2+).
H97 (= H102) 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 (≠ Y121) 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 (≠ A125) mutation to N: Loss of the epimerase activity.
E142 (= E143) 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 (= H163) 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.

P35612 Beta-adducin; Erythrocyte adducin subunit beta from Homo sapiens (Human) (see 2 papers)
26% identity, 80% coverage: 46:229/231 of query aligns to 169:364/726 of P35612

query
sites
P35612

L

L

I

I

T

S

P

P

S

K

G

G

V

V

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S

Y

C

E

S

Y

E

L

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T

T

P

A

D

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A

S

L

L

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K

I

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N

L

I

D

L

G

G

L

E

P

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D

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E

N

K

G

G

A

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Q

S

-

C

-

F

-

P

-

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D

S

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E

G

W

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C

F

L

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A

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Y

Q

A

A

A

R

R

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P

D

D

M

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I

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H

A

L

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H

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T

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A

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M

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H

Y

N

M

-

I

-

A

A

A

L

F

L

G

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G

G

N

D

D

-

V

-

P

-

L

M

A

A

D

Y

Y

Y

A

D

L

F

F

N

G

G

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E

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M

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E

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A

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D

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R

-

I

N

N

M

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A

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R

K

I

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M

L

A

G

D

P

R

T

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C

G

K

C

I

L

L

-

V

M

L

A

R

N

N

H

H

G

G

A

V

T

V

V

A

L

L

G

G

E

D

T

T

V

V

D

E

K

E

A

A

R

F

W

Y

R

K

L

I

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F

E

H

L

L

E

Q

T

A

L

A

A

C

R

E

T

I

Y

Q

L

V

-

S

-

A

F

L

S

S

I

A

G

G

A

V

P

E

H

N

I

L

L

I

-

L

-

E

-

Q

-

E

-

K

-

H

S

R

D

P

A

H

E

E

I

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A

G

E

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V

V

M

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V

W

A

A

F

G

S

S

S

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Y

F

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G

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P

R

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Q

P

-

E

K

E

S

R

R

N

L

G

G

E

E

G

H

E

E

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

4xxfA L-fuculose 1-phosphate aldolase from glaciozyma antarctica pi12 (see paper)
21% identity, 65% coverage: 47:196/231 of query aligns to 59:205/249 of 4xxfA

query
sites
4xxfA

I

V

T

N

P

P

S

F

G

G

V

L

P

A

Y

F

E

R

Y

L

L

M

T

T

P

V

D

S

A

D

L

L

V

I

T

L

I

V

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N

L

Q

D

E

G

G

L

T

P

V

D

I

S

G

N

G

G

G

A

K

Q

E

P

G

S

R

-

R

-

I

-

V

-

N

-

L

S

A

E
x
G

W

F

P

M

F

I

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H

Q

S

G

A

M

I

H

H

Q

K

A

A

R

R

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M

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Q

V

A

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H

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H
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H

P

S

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T

Y

Y

C

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A

L

F

A

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S

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S

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I

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P

A

A

I

C

T

H

T

Y
x
Q

M

D

I

S

A

C

A

A

F

F

G

Y

G

G

N

-

D

-

V

-

P

-

L

-

A

-

D

D

Y

V

A

A

L

L

F

L

G

G

S

D

P

E

E

-

L

-

C

S

A

G

N

T

M

I

A

A

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V

I

A

M

L

A

Q

D

Q

R

K

H

K

G

A

C

I

L

I

M

L

A

Q

N

N

H
|
H

G

G

A

L

T

L

V

T

L

V

G

G

E

T

T

T

V

I

D

D

K

S

A

A

R

V

W

A

R

W

L

F

E

I

E

M

L

L

E

E

T

K

L

Q

A

C

R

Q

T

V

Y

Q

L

L

F

L

S

A

S

D

I

A

G

A

G

G

active site: G98 (≠ E81), H117 (= H100), H119 (= H102), Q138 (≠ Y121), H172 (= H163)
binding zinc ion: H117 (= H100), H119 (= H102), H172 (= H163)

P35611 Alpha-adducin; Erythrocyte adducin subunit alpha from Homo sapiens (Human) (see 5 papers)
25% identity, 71% coverage: 37:201/231 of query aligns to 169:342/737 of P35611

query
sites
P35611

I

I

S

T

A

T

R

R

I

V

A

N

S

S

G

E

-

Q

-

E

-

H

I

F

L

L

I

I

T

V

P

P

S

F

G

G

V

L

P

L

Y

Y

E

S

Y

E

L

V

T

T

P

A

D

S

A

S

L

L

V

V

T

K

I

I

P

N

L

L

D

Q

G

G

-

D

-

I

-

V

-

D

L

R

P

G

D

S

S

T

N

N

G

L

A

G

Q

V

P

N

S

Q

S

A

E

G

W

F

P

T

F

L

H

H

Q

S

G

A

M

I

H

Y

Q

A

A

A

R

R

P

P

D

D

M

V

P

K

V

C

V

V

L

V

H

H

A

I

H

H

P

T

P

P

Y

A

C

G

S

A

V

A

L

V

A

S

V

A

Q

M

R

K

R

C

S

G

I

L

P

L

A

P

C

I

H

S

Y

P

M

E

I

A

A

L

A

S

F

L

G

G

G

-

N

-

D

E

V

V

P

A

L

Y

A

H

D

D

Y

Y

-

H

-

G

A

I

L

L

F

V

G

D

S

E

P

E

E

E

L

K

C

V

A

L

N

I

M

Q

A

K

R

N

I

L

M

G

A

P

D

K

R

S

H

K

G

V

C

L

L

I

M

L

A

R

N

N

H

H

G

G

A

L

T

V

V

S

L

V

G

G

E

E

T

S

V

V

D

E

K

E

A

A

R

F

W

Y

R

Y

L

I

E

H

E

N

L

L

-

V

-

A

-

C

E

E

T

I

L

Q

A

V

R

R

T

T

Y

-

L

-

F

L

S

A

S

S

I

A

G

G

A

P

P

D

H

N

I

L

L

V

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

>3607101 FitnessBrowser__Dino:3607101
MTPATPLPDTTATRQALIDACLWMNARHLNQGTSGNISARIASGILITPSGVPYEYLTPD
ALVTIPLDGLPDSNGAQPSSEWPFHQGMHQARPDMPVVLHAHPPYCSVLAVQRRSIPACH
YMIAAFGGNDVPLADYALFGSPELCANMARIMADRHGCLMANHGATVLGETVDKARWRLE
ELETLARTYLFSSIGGAPHILSDAEIAEVMVAFSSYGPRHPEERNGEGERS

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