SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_054255928.1 NCBI__GCF_001298675.1:WP_054255928.1 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 20 (the maximum) hits to proteins with known functional sites (download)

P35914 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Homo sapiens (Human) (see 11 papers)
56% identity, 93% coverage: 2:295/315 of query aligns to 28:321/325 of P35914

query
sites
P35914

N

T

I

L

P

P

T

K

R

R

V

V

R

K

I

I

I

V

D
x
E

V

V

G

G

P

P

R
|
R

D
|
D

G

G

L

L

Q

Q

N

N

E

E

K
|
K

Q

N

A

I

V

V

P

S

S

T

E

P

V

V

K

K

I

I

G

K

L

L

V

I

Q

D

R

M

L

L

Q

S

D

E

A

A

G

G

L

L

R

S

E

V

I

I

E
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E

V

T

T

T

S

S

Y

F

V

V

S

S

P

P

K

K

W

W

V

V

P

P

Q

Q

M

M

A

G

D

D

N

H

H

T

A

E

V

V

M

L

S

K

G

G

I

I

A

Q

R

K

Q

F

A

P

G

G

V

I

R

N

Y

Y

S

P

V

V

L

L

T

T

P

P

N

N

L

L

K

K

G

G

W

F

E

E

A

A

V

V

A

A

D

A

R

G

P

A

D

K

E

E

I

V

V

V

V

I

F

F

G

G

A

A

S

S

E

E

A

L

F

F

S

T

Q

K

K

K

N

N

I

I

N

N

C

C

S
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S

I

I

A

E

E

E

S

S

I

F

E

Q

R

R

F

F

A

D

P

A

V

I

V

L

E

K

A

A

R

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A

S

A

A

G

N

V

I

A

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V

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R

G

G

A

Y

M

V

S

S

C

C

T

A

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L

G

G

C
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C

P

P

Y

Y

E

E

G

G

E

K

I

I

A

S

P

P

E

A

R

K

V

V

A

A

Y

E

L

V

A

T

G

K

L

K

M
x
F

K

Y

G

S

I

M

G

G

V

C

Q

Y

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E

V
x
I

D

S

V

L

A
x
G

D
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D

T

T

I

I

G

G

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V

G

G

T

T

P

P

L

G

K

I

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M

Q

K

R

D

A

M

I

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A

S

A

A

T

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M

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Q

H

E

Y

V

E

P

L

L

D

A

A

A

V

L

S

A

G

V

H
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H

F

C

H

H

D

D

T

T

Y

Y

G

G

Q

Q

A

A

L

L

S

A

N

N

T

T

L

L

A

M

A

A

L

L

E

Q

L

M

G

G

V

V

W

S

N

V

F

V

Q

D

S

S

V

V

A

A

G

G

L

L

G

G

C

C

P

P

Y

Y

A

A

K

Q

G

G

A

A

T

S

G

G

N

N

V

L

A

A

T

T

E
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E

D
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D

L

L

V

V

Y

Y

L

M

L

L

H

E

G

G

M

L

G

G

I

I

E

H

T

T

G

G

I

V

D

N

L

L

D

Q

K

K

L

L

V

L

D

E

A

A

G

G

A

N

Y

F

I

I

S

C

D

Q

F

A

L

L

G

N

R

R

K

K

S

T

G

S

S

S

R

K

V

V

A

A

V

Q

A

A

E37 (≠ D11) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
R41 (= R15) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
D42 (= D16) to E: in HMGCLD; reduced activity; to G: in HMGCLD; loss of activity; dbSNP:rs1467902610; to H: in HMGCLD; loss of activity; mutation D->A,N: Loss of activity, and reduced proton exchange rate.
K48 (= K22) to N: in HMGCLD; abolishes almost all enzymatic activity
E72 (= E46) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
S142 (= S116) to F: in HMGCLD; activity lower than 5% respect to the wild-type
C174 (= C148) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
F192 (≠ M166) to S: in HMGCLD; activity lower than 5% respect to the wild-type
I200 (≠ V174) to F: in HMGCLD; activity lower than 5% respect to the wild-type
G203 (≠ A177) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
D204 (= D178) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
H233 (= H207) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
E279 (= E253) mutation to A: Reduced thermal stability, but normal activity.
D280 (= D254) mutation to A: Normal activity.

Sites not aligning to the query:

323 modified: Interchain; C→S: Abolishes interchain homodimerization. Exhibits no DTT stimulated activity.

3mp3B Crystal structure of human lyase in complex with inhibitor hg-coa (see paper)
56% identity, 93% coverage: 2:295/315 of query aligns to 1:294/296 of 3mp3B

query
sites
3mp3B

N

T

I

L

P

P

T

K

R

R

V

V

R

K

I

I

I

V

D

E

V

V

G

G

P

P

R
|
R

D
|
D

G

G

L

L

Q
|
Q

N

N

E

E

K

K

Q

N

A

I

V

V

P

S

S

T

E

P

V

V

K

K

I

I

G

K

L

L

V

I

Q

D

R

M

L

L

Q

S

D

E

A

A

G

G

L

L

R

S

E

V

I

I

E

E

V

T

T

T

S

S

Y
x
F

V
|
V

S
|
S

P

P

K

K

W
|
W

V

V

P

P

Q

Q

M

M

A

G

D

D

N

H

H

T

A

E

V

V

M

L

S

K

G

G

I

I

A

Q

R

K

Q

F

A

P

G

G

V

I

R

N

Y

Y

S

P

V

V

L

L

T

T

P
|
P

N
|
N

L

L

K
|
K

G
|
G

W

F

E

E

A

A

V

V

A

A

D

A

R

G

P

A

D

K

E

E

I

V

V

V

V

I

F

F

G

G

A

A

S

S

E

E

A

L

F

F

S

T

Q

K

K

K

N
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N

I

I

N

N

C

C

S

S

I

I

A

E

E

E

S

S

I

F

E

Q

R
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R

F

F

A

D

P

A

V

I

V

L

E

K

A

A

R

Q

A

S

A

A

G

N

V

I

A

S

V

V

R

R

G

G

A
x
Y

M

V

S
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S

C

C

T

A

V

L

G

G

C

C

P

P

Y

Y

E

E

G

G

E

K

I

I

A

S

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P

E

A

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A

A

Y

E

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A

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Y

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M

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G

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Y

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D

S

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A

G

D

D

T
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T

I

I

G

G

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V

G

G

T

T

P

P

L

G

K

I

V

M

Q

K

R

D

A

M

I

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A

S

A

A

T

V

L

M

Q

Q

H

E

Y

V

E

P

L

L

D

A

A

A

V

L

S

A

G

V

H
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H

F

C

H
|
H

D

D

T

T

Y

Y

G

G

Q

Q

A

A

L

L

S

A

N

N

T

T

L

L

A

M

A

A

L

L

E

Q

L

M

G

G

V

V

W

S

N

V

F

V

Q

D

S

S

V

V

A

A

G

G

L

L

G

G

C

C

P

P

Y

Y

A

A

K

Q

G

G

A

A

T

S

G

G

N

N

V

L

A

A

T

T

E

E

D

D

L

L

V

V

Y

Y

L

M

L

L

H

E

G

G

M

L

G

G

I

I

E

H

T

T

G

G

I

V

D

N

L

L

D

Q

K

K

L

L

V

L

D

E

A

A

G

G

A

N

Y

F

I

I

S

C

D

Q

F

A

L

L

G

N

R

R

K

K

S

T

G

S

S

S

R

K

V

V

A

A

V

Q

A

A

binding (3R,5S,9R,21S)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9,21-tetrahydroxy-8,8-dimethyl-10,14,19-trioxo-2,4,6-trioxa-18-thia-11,15-diaza-3,5-diphosphatricosan-23-oic acid 3,5-dioxide: R14 (= R15), D15 (= D16), Q18 (= Q19), F49 (≠ Y50), V50 (= V51), S51 (= S52), W54 (= W55), P81 (= P82), N82 (= N83), K84 (= K85), G85 (= G86), N111 (= N112), R122 (= R123), Y140 (≠ A141), S142 (= S143), T178 (= T179), H206 (= H207)
binding magnesium ion: D15 (= D16), H206 (= H207), H208 (= H209)

2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
56% identity, 93% coverage: 2:295/315 of query aligns to 1:294/296 of 2cw6A

query
sites
2cw6A

N

T

I

L

P

P

T

K

R

R

V

V

R

K

I

I

I

V

D

E

V

V

G

G

P

P

R

R

D
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D

G

G

L

L

Q
|
Q

N

N

E

E

K

K

Q

N

A

I

V

V

P

S

S

T

E

P

V

V

K

K

I

I

G

K

L

L

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I

Q

D

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M

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L

Q

S

D

E

A

A

G

G

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L

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S

E

V

I

I

E

E

V

T

T

T

S

S

Y

F

V

V

S

S

P

P

K

K

W

W

V

V

P

P

Q

Q

M

M

A

G

D

D

N

H

H

T

A

E

V

V

M

L

S

K

G

G

I

I

A

Q

R

K

Q

F

A

P

G

G

V

I

R

N

Y

Y

S

P

V

V

L

L

T

T

P

P

N

N

L

L

K

K

G

G

W

F

E

E

A

A

V

V

A

A

D

A

R

G

P

A

D

K

E

E

I

V

V

V

V

I

F
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F

G

G

A

A

S

S

E

E

A

L

F

F

S

T

Q

K

K

K

N

N

I

I

N

N

C

C

S

S

I

I

A

E

E

E

S

S

I

F

E

Q

R

R

F

F

A

D

P

A

V

I

V

L

E

K

A

A

R

Q

A

S

A

A

G

N

V

I

A

S

V

V

R

R

G

G

A

Y

M

V

S

S

C

C

T

A

V

L

G

G

C

C

P

P

Y

Y

E

E

G

G

E

K

I

I

A

S

P

P

E

A

R

K

V

V

A

A

Y

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A

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G

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M

F

K

Y

G

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G

G

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Y

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I

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V

L

A

G

D

D

T

T

I

I

G

G

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V

G

G

T

T

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P

L

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M

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K

R

D

A

M

I

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A

S

A

A

T

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L

M

Q

Q

H

E

Y

V

E

P

L

L

D

A

A

A

V

L

S

A

G

V

H
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H

F

C

H
|
H

D

D

T

T

Y

Y

G

G

Q

Q

A

A

L

L

S

A

N

N

T

T

L

L

A

M

A

A

L

L

E

Q

L

M

G

G

V

V

W

S

N

V

F

V

Q

D

S

S

V

V

A

A

G

G

L

L

G

G

C

C

P

P

Y

Y

A

A

K

Q

G

G

A

A

T

S

G

G

N
|
N

V

L

A

A

T

T

E

E

D

D

L

L

V

V

Y

Y

L

M

L

L

H

E

G

G

M

L

G

G

I

I

E

H

T

T

G

G

I

V

D

N

L

L

D

Q

K

K

L

L

V

L

D

E

A

A

G

G

A

N

Y

F

I

I

S

C

D

Q

F

A

L

L

G

N

R

R

K

K

S

T

G

S

S

S

R

K

V

V

A

A

V

Q

A

A

binding 3-hydroxypentanedioic acid: Q18 (= Q19), F100 (= F101)
binding magnesium ion: D15 (= D16), H206 (= H207), H208 (= H209), N248 (= N249)

3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
56% identity, 93% coverage: 2:295/315 of query aligns to 1:294/296 of 3mp5B

query
sites
3mp5B

N

T

I

L

P

P

T

K

R

R

V

V

R

K

I

I

I

V

D

E

V

V

G

G

P

P

R

M

D
|
D

G

G

L

L

Q
|
Q

N

N

E

E

K

K

Q

N

A

I

V

V

P

S

S

T

E

P

V

V

K

K

I

I

G

K

L

L

V

I

Q

D

R

M

L

L

Q

S

D

E

A

A

G

G

L

L

R

S

E

V

I

I

E

E

V

T

T

T

S

S

Y

F

V

V

S
|
S

P

P

K

K

W
|
W

V

V

P

P

Q

Q

M

M

A

G

D

D

N

H

H

T

A

E

V

V

M

L

S

K

G

G

I

I

A

Q

R

K

Q

F

A

P

G

G

V

I

R

N

Y

Y

S

P

V

V

L

L

T

T

P

P

N

N

L

L

K

K

G

G

W

F

E

E

A

A

V

V

A

A

D

A

R

G

P

A

D

K

E

E

I

V

V

V

V

I

F
|
F

G

G

A

A

S

S

E

E

A

L

F

F

S

T

Q

K

K

K

N
|
N

I

I

N
|
N

C

C

S

S

I

I

A

E

E

E

S

S

I

F

E

Q

R

R

F

F

A

D

P

A

V

I

V

L

E

K

A

A

R

Q

A

S

A

A

G

N

V

I

A

S

V

V

R

R

G

G

A
x
Y

M

V

S
|
S

C

C

T

A

V

L

G

G

C

C

P

P

Y

Y

E

E

G

G

E

K

I

I

A

S

P

P

E

A

R

K

V

V

A

A

Y

E

L

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A

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G

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L

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F

K

Y

G

S

I

M

G

G

V

C

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Y

R

E

V

I

D

S

V

L

A

G

D

D

T
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T

I

I

G

G

V

V

G

G

T

T

P

P

L

G

K

I

V

M

Q

K

R

D

A

M

I

L

A

S

A

A

T

V

L

M

Q

Q

H

E

Y

V

E

P

L

L

D

A

A

A

V

L

S

A

G

V

H
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H

F

C

H
|
H

D

D

T

T

Y

Y

G

G

Q

Q

A

A

L

L

S

A

N

N

T

T

L

L

A

M

A

A

L

L

E

Q

L

M

G

G

V

V

W

S

N

V

F

V

Q

D

S

S

V

V

A

A

G

G

L

L

G

G

C
|
C

P

P

Y

Y

A

A

K

Q

G

G

A

A

T

S

G

G

N

N

V

L

A

A

T

T

E

E

D

D

L

L

V

V

Y

Y

L

M

L

L

H

E

G

G

M

L

G

G

I

I

E

H

T

T

G

G

I

V

D

N

L

L

D

Q

K

K

L

L

V

L

D

E

A

A

G

G

A

N

Y

F

I

I

S

C

D

Q

F

A

L

L

G

N

R

R

K

K

S

T

G

S

S

S

R

K

V

V

A

A

V

Q

A

A

binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D16), Q18 (= Q19), S51 (= S52), W54 (= W55), F100 (= F101), N111 (= N112), N113 (= N114), Y140 (≠ A141), S142 (= S143), T178 (= T179), C239 (= C240)
binding magnesium ion: D15 (= D16), H206 (= H207), H208 (= H209)

Q8TB92 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; HMGCL-like 1; Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase; er-cHL; EC 4.1.3.4 from Homo sapiens (Human) (see 2 papers)
52% identity, 94% coverage: 3:298/315 of query aligns to 74:369/370 of Q8TB92

query
sites
Q8TB92

I

L

P

P

T

E

R

F

V

V

R

K

I

I

I

V

D

E

V

V

G

G

P

P

R
|
R

D

D

G

G

L

L

Q

Q

N

N

E

E

K

K

Q

V

A

I

V

V

P

P

S

T

E

D

V

I

K

K

I

I

G

E

L

F

V

I

Q

N

R

R

L

L

Q

S

D

Q

A

T

G

G

L

L

R

S

E

V

I

I

E

E

V

V

T

T

S

S

Y

F

V

V

S

S

P

S

K

R

W

W

V

V

P

P

Q

Q

M

M

A

A

D

D

N

H

H

T

A

E

V

V

M

M

S

K

G

G

I

I

A

H

R

Q

Q

Y

A

P

G

G

V

V

R

R

Y

Y

S

P

V

V

L

L

T

T

P

P

N

N

L

L

K

Q

G

G

W

F

E

H

A

H

A

A

V

V

A

A

D

A

R

G

P

A

D

T

E

E

I

I

V

S

V

V

F

F

G

G

A

A

S

S

E

E

A

S

F

F

S

S

Q

K

K

K

N

N

I

I

N

N

C

C

S

S

I

I

A

E

E

E

S

S

I

M

E

G

R

K

F

F

A

E

P

E

V

V

E

K

A

S

A

A

R

R

A

H

A

M

G

N

V

I

A

P

V

A

R

R

G

G

A

Y

M

V

S

S

C

C

T

A

V

L

G

G

C

C

P

P

Y

Y

E

E

G

G

E

S

I

I

A

T

P

P

E

Q

R

K

V

V

A

T

Y

E

L

V

A

S

G

K

L

R

M
x
L

K

Y

G

G

I

M

G

G

V

C

Q

Y

R

E

V

I

D

S

V

L

A

G

D

D

T

T

I

I

G

G

V

V

G

G

T

T

P

P

L

G

K

S

V

M

Q

K

R

R

A

M

I

L

A

E

A

S

T

V

L

M

Q

K

H

E

Y

I

E

P

L

P

D

G

A

A

V

L

S

A

G

V

H
|
H

F

C

H

H

D

D

T

T

Y

Y

G

G

Q

Q

A

A

L

L

S

A

N

N

T

I

L

L

A

T

A

A

L

L

E

Q

L

M

G

G

V

I

W

N

N

V

F

V

Q

D

S

S

S

A

V

V

A

S

G

G

L

L

G

G

C

C

P

P

Y

Y

A

A

K

K

G

G

A

A

T

S

G

G

N

N

V

V

A

A

T

T

E

E

D

D

L

L

V

I

Y

Y

L

M

L

L

H

N

G

G

M

L

G

G

I

L

E

N

T

T

G

G

I

V

D

N

L

L

D

Y

K

K

L

V

V

M

D

E

A

A

G

G

A

D

Y

F

I

I

S

C

D

K

F

A

L

V

G

N

R

K

K

T

S

T

G

N

S

S

R

K

V

V

A

A

V

Q

A

A

L

S

L

F

N

N

R86 (= R15) mutation to Q: Abolishes catalytic activity.
L237 (≠ M166) mutation to S: Abolishes catalytic activity.
H278 (= H207) mutation to R: Abolishes catalytic activity.

Sites not aligning to the query:

2 modified: N-myristoyl glycine; G→A: Abolishes myristoylation and induces a subcellular location change.

1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35. (see paper)
53% identity, 87% coverage: 6:279/315 of query aligns to 3:276/283 of 1ydnA

query
sites
1ydnA

R

H

V

V

R

E

I

I

I

V

D

E

V

M

G

A

P

A

R

R

D
|
D

G

G

L

L

Q

Q

N

N

E

E

K

K

Q

R

A

F

V

V

P

P

S

T

E

A

V

D

K

K

I

I

G

A

L

L

V

I

Q

N

R

R

L

L

Q

S

D

D

A

C

G

G

L

Y

R

A

E

R

I

I

E

E

V

A

T

T

S

S

Y

F

V

V

S

S

P

P

K

K

W

W

V

V

P

P

Q

Q

M

L

A

A

D

D

N

S

H

R

A

E

V

V

M

M

S

A

G

G

I

I

A

R

R

R

Q

A

A

D

G

G

V

V

R

R

Y

Y

S

S

V

V

L

L

T

V

P

P

N

N

L

M

K

K

G

G

W

Y

E

E

A

A

V

A

A

A

D

A

R

H

P

A

D

D

E

E

I

I

V

A

V

V

F

F

G

I

A

S

A

A

S

S

E

E

A

G

F

F

S

S

Q

K

K

A

N

N

I

I

N

N

C

C

S

T

I

I

A

A

E

E

S

S

I

I

E

E

R

R

F

L

A

S

P

P

V

V

V

I

E

G

A

A

R

I

A

N

A

D

G

G

V

L

A

A

V

I

R

R

G

G

A

Y

M

V

S

S

C

C

T

V

V

V

G

E

C

C

P

P

Y

Y

E

D

G

G

E

P

I

V

A

T

P

P

E

Q

R

A

V

V

A

A

Y

S

L

V

A

T

G

E

L

Q

M

L

K

F

G

S

I

L

G

G

V

C

Q

H

R

E

V

V

D

S

V

L

A

G

D

D

T

T

I

I

G

G

V

R

G

G

T

T

P

P

L

D

K

T

V

V

Q

A

R

A

A

M

I

L

A

D

A

A

T

V

L

L

Q

A

H

I

Y

A

E

P

L

A

D

H

A

S

V

L

S

A

G

G

H
|
H

F

Y

H
|
H

D

D

T

T

Y

G

G

G

Q

R

A

A

L

L

S

D

N

N

T

I

L

R

A

V

A

S

L

L

E

E

L

K

G

G

V

L

W

R

N

V

F

F

Q

D

S

A

S

S

V

V

A

G

G

G

L

L

G

G

C

C

P

P

Y

F

A

A

K

P

G

G

A

A

T

K

G

G

N
|
N

V

V

A

D

T

T

E

V

D

A

L

V

V

V

Y

E

L

M

L

L

H

H

G

E

M

M

G

G

I

F

E

E

T

T

G

G

I

L

D

D

L

L

D

D

K

R

L

L

V

R

D

S

A

A

G

G

A

L

Y

F

binding calcium ion: D13 (= D16), H204 (= H207), H206 (= H209), N246 (= N249)

P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii (see paper)
49% identity, 94% coverage: 7:301/315 of query aligns to 4:298/301 of P13703

query
sites
P13703

V

V

R

K

I

V

I

F

D

E

V

V

G

G

P

P

R

R

D

D

G

G

L

L

Q

Q

N

N

E

E

K

R

Q

Q

A

P

V

L

P

S

S

V

E

A

V

A

K

R

I

V

G

G

L

L

V

I

Q

G

R

E

L

L

Q

A

D

G

A

T

G

G

L

L

R

R

E

H

I

I

E

E

V

A

T

G

S

A

Y

F

V

V

S

S

P

P

K

R

W

W

V

V

P

P

Q

Q

M

M

A

A

D

G

N

S

H

D

A

E

V

V

M

L

S

R

G

Q

I

L

A

P

R

S

Q

N

A

D

G

G

V

V

R

S

Y

Y

S

T

V

A

L

L

T

V

P

P

N

N

L

R

K

Q

G

G

W

F

E

E

A

A

V

Q

A

R

D

A

R

G

P

C

D

R

E

E

I

V

V

A

V

V

F

F

G

A

A

A

S

S

E

E

A

A

F

F

S

S

Q

R

K

N

N

N

I

I

N

N

C

C

S

S

I

I

A

D

E

E

S

S

I

F

E

E

R

R

F

F

A

T

P

P

V

V

V

L

E

R

A

A

R

N

A

E

A

A

G

S

V

I

A

R

V

V

R

R

G

G

A

Y

M

V

S

S

C

C

T

V

V

L

G

G

C

C

P

P

Y

F

E

S

G

G

E

A

I

V

A

A

P

P

E

E

R

A

V

V

A

A

Y

K

L

V

A

A

G

R

L

R

M

L

K

Y

G

E

I

L

G

G

V

C

Q

Y

R

E

V

I

D

S

V

L

A

G

D

D

T

T

I

I

G

G

V

A

G

G

T

R

P

P

L

D

K

E

V

T

Q

A

R

Q

A

L

I

F

A

E

A

L

T

C

L

A

Q

R

H

Q

Y

L

E

P

L

V

D

A

A

A

V

L

S

A

G

G

H

H

F

F

H

H

D

D

T

T

Y

W

G

G

Q

M

A

A

L

I

S

A

N

N

T

V

L

H

A

A

L

L

E

A

L

Q

G

G

V

V

W

R

N

T

F

F

Q

D

S

S

V

V

A

A

G

G

L

L

G

G

C
|
C

P

P

Y

Y

A

S

K

P

G

G

A

A

T

S

G

G

N

N

V

V

A

A

T

T

E

E

D

D

L

L

V

L

Y

Y

L

L

H

H

G

G

M

L

G

G

I

Y

E

S

T

T

G

G

I

V

D

D

L

L

D

E

K

A

L

V

V

A

D

Q

A

V

G

G

A

V

Y

R

I

I

S

S

D

A

F

Q

L

L

G

G

R

T

K

A

S

N

G

R

S

S

R

R

V

A

A

G

V

L

A

A

L

L

L

A

N

A

K

R

R

S

A

A

C237 (= C240) active site

6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
38% identity, 90% coverage: 11:295/315 of query aligns to 12:295/305 of 6ndsA

query
sites
6ndsA

D

E

V

V

G

S

P

P

R

R

D
|
D

G

G

L

L

Q

Q

N

I

E

E

K

P

Q

T

A

W

V

V

P

P

S

T

E

D

V

K

K

K

I

I

G

D

L

L

V

I

Q

N

R

Q

L

L

Q

S

D

T

A

M

G

G

L

F

R

S

E

R

I

I

E

E

V

A

T

G

S

S

Y

F

V
|
V

S
|
S

P

P

K

K

W

A

V
x
I

P

P

Q

N

M

L

A

R

D

D

N

G

H

E

A

E

V

V

M

F

S

T

G

G

I

I

A

T

R

R

Q

H

A

K

G

D

V

I

R

I

Y

Y

S

V

V

G

L

L

T

I

P

P

N
|
N

L

L

K

K

G
|
G

W

A

E

L

A
x
R

A

A

V

V

A

E

D

A

R

N

P

A

D

N

E

E

I

L

V

N

V

L

F

V

G

L

A

S

A

A

S

S

E

Q

A

T

F

H

S

N

Q

L

K

A

N
|
N

I
x
M

N
x
R

C

M

S

T

I

K

A

A

E

Q

S

S

I

F

E

A

R

G

F

F

A

T

P

E

V

I

V

V

E

E

A

Q

A

L

R

Q

A

G

A

K

G

-

V

T

A

Q

V

F

R

N

G

G

A

T

M

V

S

A

C

T

T

T

V

F

G

G

C

C

P

P

Y

F

E

E

G

G

E

K

I

I

A

S

P

E

E

R

R

E

V

V

A

F

Y

S

L

L

A

V

G

E

L

H

M

Y

K

L

G

K

I

L

G

G

V

I

Q

H

R

N

V

I

D

T

V

L

A

A

D

D

T

T

I

T

G

G

V

M

G

A

T

N

P

P

L

V

K

Q

V

V

Q

K

R

R

A

I

I

V

A

S

A

H

T

V

L

L

Q

S

H

L

Y

I

E

S

L

P

D

E

A

Q

V

L

S

T

G

L

H
|
H

F

F

H
|
H

D

N

T

T

Y

R

G

G

Q

L

A

G

L

L

S

T

N

N

T

V

L

L

A

A

L

Y

E

E

L

V

G

G

V

A

W

R

N

R

F

F

Q

D

S

A

V

L

A

G

G

G

L

L

G

G

C

C

P

P

Y

F

A

A

K

P

G

G

A

A

T

S

G

G

N

N

V

I

A

C

T

T

E

E

D

D

L

L

V

V

Y

N

L

M

L

C

H

E

G

E

M

I

G

G

I

I

E

P

T

T

G

T

I

I

D

D

L

L

D

D

K

A

L

L

V

I

D

Q

A

L

G

S

A

R

Y

T

I

L

S

P

D

A

F

L

L

L

G

G

R

H

K

D

S

T

G

P

S

S

R

Q

V

L

A

A

V

K

A

A

binding coenzyme a: V52 (= V51), S53 (= S52), I57 (≠ V56), N84 (= N83), G87 (= G86), R90 (≠ A89), N113 (= N112), M114 (≠ I113), R115 (≠ N114)
binding zinc ion: D17 (= D16), H207 (= H207), H209 (= H209)

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
27% identity, 89% coverage: 6:285/315 of query aligns to 3:277/308 of 3rmjB

query
sites
3rmjB

R

R

V

V

R

I

I

I

I

F

D

D

V

T

G

T

P

L

R

R

D
|
D

G

G

L

E

Q
|
Q

N

S

E

P

K

G

Q

A

A

A

V

M

P

T

S

K

E

E

V

E

K

K

I

I

G

R

L

V

V

A

Q

R

R

Q

L

L

Q

E

D

K

A

L

G

G

L

V

R

D

E

I

I

I

E

E

V

A

-

G

T

F

S

A

Y

A

V

A

S

S

P

P

K

G

W

D

V

F

P

E

Q

A

M

V

A

-

D

-

N

-

H

N

A

A

V

I

M

A

S

K

G

T

I

I

A

T

R

K

Q

S

A

T

G

V

V

C

R

S

Y

L

S

S

-

R

V

A

L

I

T

E

P

R

N

D

L

I

K

R

G

Q

W

A

E

G

A

E

A

A

V

V

A

A

D

P

R

A

P

P

D

K

E

K

-

R

I

I

V

H

V

T

F

F

G

I

A

A

A

T

S

S

E

P

A

I

F

H

S

M

Q

E

K

Y

N

K

I

L

N

K

C

M

S

K

I

P

A

K

E

Q

S

V

I

I

E

E

R

A

F

A

A

V

P

K

V

A

V

V

E

K

A

I

A

A

R

R

A

E

A

Y

G

T

V

D

A

D

V

V

R

E

G

-

A

-

M

F

S

S

C

C

T

E

V

D

G

A

C

L

P

R

Y

S

E

E

G

I

E

D

I

F

A

-

P

-

E

-

R

-

V

L

A

A

Y

E

L

I

A

C

G

G

L

A

M

V

K

I

G

E

I

A

G

G

V

A

Q

T

R

T

V

I

D

N

V

I

A

P

D

D

T

T

I

V

G

G

V

Y

G

S

T

I

P

P

L

Y

K

K

V

T

Q

E

-

E

-

F

R

R

A

E

I

L

A

I

A

A

T

K

L

T

Q

P

H

N

Y

G

E

G

L

K

D

V

A

V

V

W

S

S

G

A

H
|
H

F

C

H
|
H

D

N

T

D

Y

L

G

G

Q

L

A

A

L

V

S

A

N

N

T

S

L

L

A

A

L

L

E

K

L

G

G

G

V

A

W

R

N

Q

F

V

Q

E

S

C

S

T

V

V

A

N

G

G

L

L

G

G

G

-

C

-

P

-

Y

-

A

-

K

-

G

E

A

R

T

A

G

G

N
|
N

V

A

A

S

T

V

E

E

D

E

L

I

V

V

Y

M

L

A

L

L

-

K

-

V

-

R

H

H

G

D

M

L

-

F

G

G

I

L

E

E

T

T

G

G

I

I

D

D

L

T

D

T

K

Q

L

I

V

V

D

P

A

S

G

S

A

K

Y

L

I

V

S

S

D

T

F

I

L

T

G

G

active site: Q16 (= Q19)
binding manganese (ii) ion: D13 (= D16), H201 (= H207), H203 (= H209), N237 (= N249)

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58) (see 2 papers)
27% identity, 90% coverage: 1:285/315 of query aligns to 1:280/517 of Q9JZG1

query
sites
Q9JZG1

M

M

N

T

I

Q

P

T

T

N

R

R

V

V

R

I

I

I

I

F

D

D

V

T

G

T

P

L

R

R

D
|
D

G

G

L

E

Q

Q

N

S

E

P

K

G

Q

A

A

A

V

M

P

T

S

K

E

E

V

E

K

K

I

I

G

R

L

V

V

A

Q

R

R

Q

L

L

Q

E

D

K

A

L

G

G

L

V

R

D

E

I

I

I

E

E

V

A

-

G

T

F

S

A

Y

A

V

A

S

S

P

P

K

G

W

D

V

F

P

E

Q

A

M

V

A

-

D

-

N

-

H

N

A

A

V

I

M

A

S

K

G

T

I

I

A

T

R

K

Q

S

A

T

G

V

V

C

R

S

Y

L

S

S

-

R

V

A

L

I

T

E

P

R

N

D

L

I

K

R

G

Q

W

A

E

G

A

E

A

A

V

V

A

A

D

P

R

A

P

P

D

K

E

K

-

R

I

I

V

H

V

T

F

F

G

I

A

A

A

T

S

S

E

P

A

I

F

H

S

M

Q

E

K

Y

N

K

I

L

N

K

C

M

S

K

I

P

A

K

E

Q

S

V

I

I

E

E

R

A

F

A

A

V

P

K

V

A

V

V

E

K

A

I

A

A

R

R

A

E

A

Y

G

T

V

D

A

D

V

V

R

E

G

-

A

-

M

F

S

S

C

C

T

E

V

D

G

A

C

L

P

R

Y

S

E

E

G

I

E

D

I

F

A

-

P

-

E

-

R

-

V

L

A

A

Y

E

L

I

A

C

G

G

L

A

M

V

K

I

G

E

I

A

G

G

V

A

Q

T

R

T

V

I

D

N

V

I

A

P

D

D

T

T

I

V

G

G

V

Y

G

S

T

I

P

P

L

Y

K

K

V

T

Q

E

-

E

-

F

R

R

A

E

I

L

A

I

A

A

T

K

L

T

Q

P

H

N

Y

G

E

G

L

K

D

V

A

V

V

W

S

S

G

A

H
|
H

F

C

H
|
H

D

N

T

D

Y

L

G

G

Q

L

A

A

L

V

S

A

N

N

T

S

L

L

A

A

L

L

E

K

L

G

G

G

V

A

W

R

N

Q

F

V

Q

E

S

C

S

T

V

V

A

N

G

G

L

L

G

G

G

-

C

-

P

-

Y

-

A

-

K

-

G

E

A

R

T

A

G

G

N
|
N

V

A

A

S

T

V

E

E

D

E

L

I

V

V

Y

M

L

A

L

L

-

K

-

V

-

R

H

H

G

D

M

L

-

F

G

G

I

L

E

E

T

T

G

G

I

I

D

D

L

T

D

T

K

Q

L

I

V

V

D

P

A

S

G

S

A

K

Y

L

I

V

S

S

D

T

F

I

L

T

G

G

D16 (= D16) binding Mn(2+)
H204 (= H207) binding Mn(2+)
H206 (= H209) binding Mn(2+)
N240 (= N249) binding Mn(2+)

Sites not aligning to the query:

366:517 Required for the condensation reaction. Not required to bind substrate

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
25% identity, 84% coverage: 9:274/315 of query aligns to 32:289/400 of 3ivtB

query
sites
3ivtB

I

I

D

E

V

S

G

T

P

L

R
|
R

D
x
E

G

G

L

E

Q
|
Q

N

F

E

A

K

N

Q

A

A

F

V

F

P

D

S

T

E

E

V

K

K

K

I

I

G

Q

L

I

V

A

Q

K

R

A

L

L

Q

D

D

N

A

F

G

G

L

V

R

D

E

Y

I

I

E

E

V

L

T

T

S

S

Y

P

V

V

S

A

P

S

K

E

W

Q

V

S

P

R

Q

Q

M

-

A

-

D

D

N

C

H

E

A

A

V

I

M

C

S

-

G

-

I

-

A

-

R

-

Q

K

A

L

G

G

V

L

R

K

Y

C

S

K

V

I

L

L

T

T

P
x
H

-

I

-

R

-

C

N

H

L

M

K

D

G

D

W

A

E

R

A

V

A

A

V

V

A

E

D

T

R

G

P

V

D

D

E

G

I

V

V

D

V

V

F

V

G

I

A

G

A

T

S

S

E

Q

A

Y

F

L

S

R

Q

K

K

Y

N

S

I

H

N

G

C

K

S

D

I

M

A

T

E

Y

S

I

I

I

E

D

R

S

F

A

A

T

P

E

V

V

V

I

E

N

A

F

A

V

R

K

A

S

A

K

G

G

V

I

A

E

V

V

R
|
R

G

F

A
x
S

M

S

S

E

C

D

T

S

V

-

G

-

C

-

P

-

Y

F

E

R

G

S

E

D

I

L

A

V

P

D

E

L

R

L

V

S

A

L

Y

Y

L

K

A

A

G

-

L

-

M

V

K

D

G

K

I

I

G

G

V

V

Q

N

R

R

V

V

D

G

V

I

A

A

D

D

T
|
T

I

V

G

G

V

C

G

A

T

T

P

P

L

R

K

Q

V

V

Q

Y

R

D

A

L

I

I

A

R

A

-

T

T

L

L

Q

R

H

G

Y

V

E

V

L

S

D

C

A

D

V

I

S

E

G

C

H
|
H

F

F

H
|
H

D

N

T

D

Y

T

G

G

Q

M

A

A

L

I

S

A

N

N

T

A

L

Y

A

C

A

A

L

L

E

E

L

A

G

G

V

A

W

T

N

H

F

I

Q

D

S

T

S

S

V

I

A

L

G

G

L

I

G

G

-

E

-

R

-

N

G

G

C

I

P

T

Y

P

A

L

K

G

G

A

A

L

T

L

G

A

N

R

V

M

A

Y

T

V

E

T

D

D

L

R

V

E

Y

Y

L

I

L

T

H

H

G

K

M

Y

G

K

I

L

E

N

T

Q

G

L

I

R

D

E

L

L

D

E

K

N

L

L

V

V

active site: Q42 (= Q19)
binding 2-oxoglutaric acid: R38 (= R15), H98 (≠ P82), R158 (= R139), S160 (≠ A141), T192 (= T179), H219 (= H207), H221 (= H209)
binding zinc ion: E39 (≠ D16), H219 (= H207), H221 (= H209)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
25% identity, 84% coverage: 9:274/315 of query aligns to 37:294/418 of Q9Y823

query
sites
Q9Y823

I

I

D

E

V

S

G

T

P

L

R
|
R

D
x
E

G

G

L

E

Q
|
Q

N

F

E

A

K

N

Q

A

A

F

V

F

P

D

S

T

E

E

V

K

K

K

I

I

G

Q

L

I

V

A

Q

K

R

A

L

L

Q

D

D

N

A

F

G

G

L

V

R

D

E

Y

I

I

E
|
E

V

L

T

T

S

S

Y

P

V

V

S

A

P

S

K

E

W

Q

V

S

P

R

Q

Q

M

-

A

-

D

D

N

C

H

E

A

A

V

I

M

C

S

-

G

-

I

-

A

-

R

-

Q

K

A

L

G

G

V

L

R

K

Y

C

S

K

V

I

L

L

T

T

P
x
H

-

I

-

R

-

C

N

H

L

M

K

D

G

D

W

A

E

R

A

V

A

A

V

V

A

E

D

T

R

G

P

V

D

D

E

G

I

V

V
x
D

V

V

F

V

G

I

A

G

A

T

S

S

E

Q

A

Y

F

L

S

R

Q

K

K

Y

N

S

I

H

N

G

C

K

S

D

I

M

A

T

E

Y

S

I

I

I

E

D

R

S

F

A

A

T

P

E

V

V

V

I

E

N

A

F

A

V

R

K

A

S

A

K

G

G

V

I

A

E

V

V

R
|
R

G

F

A
x
S

M

S

S
x
E

C

D

T

S

V

-

G

-

C

-

P

-

Y

F

E

R

G

S

E

D

I

L

A

V

P

D

E

L

R

L

V

S

A

L

Y

Y

L

K

A

A

G

-

L

-

M

V

K

D

G

K

I

I

G

G

V

V

Q

N

R

R

V

V

D

G

V

I

A

A

D

D

T
|
T

I

V

G

G

V

C

G

A

T

T

P

P

L

R

K

Q

V

V

Q

Y

R

D

A

L

I

I

A

R

A

-

T

T

L

L

Q

R

H

G

Y

V

E

V

L

S

D

C

A

D

V

I

S
x
E

G

C

H
|
H

F

F

H
|
H

D

N

T

D

Y

T

G

G

Q

M

A

A

L

I

S

A

N

N

T

A

L

Y

A

C

A

A

L

L

E

E

L

A

G

G

V

A

W

T

N

H

F

I

Q

D

S

T

S

S

V

I

A

L

G

G

L

I

G

G

-

E

-

R

-

N

G

G

C

I

P

T

Y

P

A

L

K

G

G

A

A

L

T

L

G

A

N

R

V

M

A

Y

T

V

E

T

D

D

L

R

V

E

Y

Y

L

I

L

T

H

H

G

K

M

Y

G

K

I

L

E

N

T

Q

G

L

I
x
R

D

E

L

L

D

E

K

N

L

L

V

V

R43 (= R15) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D16) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q19) mutation to A: Abolishes the catalytic activity.
E74 (= E46) mutation to A: Abolishes the catalytic activity.; mutation to Q: Results in a moderate decrease in the turnover number and a slight increase in the Km value for each substrate.
H103 (≠ P82) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ V99) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (= R139) binding 2-oxoglutarate; mutation R->A,Q: Abolishes the catalytic activity.; mutation to K: Severely diminishes affinity for 2-oxoglutarate and substantially impairs catalytic efficiency.
S165 (≠ A141) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (≠ S143) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T179) binding 2-oxoglutarate; binding L-lysine; mutation to A: Exhibits a 25-fold decrease in catalytic efficiency.; mutation to S: Results in a modest decrease in catalytic efficiency.; mutation to V: Abolishes the catalytic activity.
E222 (≠ S205) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H207) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H209) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ I268) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.

Sites not aligning to the query:

332 Y→A: Abolishes the catalytic activity.; Y→F: Results in a decrease in catalytic efficiency.
364 Q→R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
25% identity, 84% coverage: 9:274/315 of query aligns to 14:260/370 of 3mi3A

query
sites
3mi3A

I

I

D

E

V

S

G

T

P

L

R
|
R

D
x
E

G

G

L

E

Q
|
Q

N

F

E

A

K

N

Q

A

A

F

V

F

P

D

S

T

E

E

V

K

K

K

I

I

G

Q

L

I

V

A

Q

K

R

A

L

L

Q

D

D

N

A

F

G

G

L

V

R

D

E

Y

I

I

E

E

V

L

T

T

S

S

Y

P

V

V

S

A

P

S

K

E

W

Q

V

S

P

R

Q

Q

M

-

A

-

D

D

N

C

H

E

A

A

V

I

M

C

S

-

G

-

I

-

A

-

R

-

Q

K

A

L

G

G

V

L

R

K

Y

C

S

K

V

I

L

L

T

T

P

H

-

I

-

R

-

C

N

H

L

M

K

D

G

D

W

A

E

R

A

V

A

A

V

V

A

E

D

T

R

G

P

V

D

D

E

G

I

V

V
x
D

V

V

F

V

G

-

A

-

S

-

E

-

A

-

F

-

S

-

Q

-

K

-

N

-

I

I

N

G

C

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S

S

I

M

A

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E

Y

S

I

I

I

E

D

R

S

F

A

A

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P

E

V

V

V

I

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N

A

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A

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A

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A

K

G

G

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I

A

E

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A

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M

S

S

E

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-

G

-

C

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Y

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E

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I

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A

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P

D

E

L

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A

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Y

Y

L

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A

A

G

-

L

-

M

V

K

D

G

K

I

I

G

G

V

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Q

N

R

R

V

V

D

G

V

I

A

A

D

D

T
|
T

I

V

G

G

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C

G

A

T

T

P

P

L

R

K

Q

V

V

Q

Y

R

D

A

L

I

I

A

R

A

-

T

T

L

L

Q

R

H

G

Y

V

E

V

L

S

D

C

A

D

V

I

S

E

G

C

H
|
H

F

F

H
|
H

D

N

T

D

Y

T

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G

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M

A

A

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I

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A

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N

T

A

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A

C

A

A

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S

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I

A

L

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G

L

I

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G

-

E

-

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-

N

G

G

C

I

P

T

Y

P

A

L

K

G

G

A

A

L

T

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G

A

N

R

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M

A

Y

T

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T

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D

L

R

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E

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Y

L

I

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T

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H

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M

Y

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T

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L

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N

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L

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V

active site: Q24 (= Q19)
binding lysine: R20 (= R15), D100 (≠ V99), T163 (= T179), H190 (= H207), H192 (= H209)
binding zinc ion: E21 (≠ D16), H190 (= H207), H192 (= H209)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
22% identity, 90% coverage: 2:285/315 of query aligns to 17:288/399 of 6ktqA

query
sites
6ktqA

N

S

I

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P

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R

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x
E

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A

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M

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x
V

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M

I

A

Y

D

E

N

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H

I

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M

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I

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I

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A

K

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Q

E

A

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G

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V

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E

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I

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A

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H

N

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x
R

-
x
A

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-

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K

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I

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A

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A

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A

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F

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A

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x
H

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E

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I

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A

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A

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A

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G

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A

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R

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x
T

M

A

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x
E

C

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C

A

P

D

Y

Y

E

Q

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-

E

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I

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L

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A

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x
S

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I

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T

I

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P

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R

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A

L

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F

A

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A

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L

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D

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A

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H

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|
H

D

N

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D

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L

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M

A

A

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A

N

N

T

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A

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A

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G

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L

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E

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R

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-

I

C

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A

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A

A

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A

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A

N

-

V

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A

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-

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-

D

-

L

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Y

-

L

L

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F

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G

-

I

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D

L

L

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A

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L

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G

binding 2-oxoglutaric acid: R30 (= R15), R154 (= R139), T156 (≠ A141), E158 (≠ S143), S184 (≠ D175), T188 (= T179), H216 (= H207), H218 (= H209)
binding coenzyme a: V67 (≠ W55), R96 (≠ L84), A97 (vs. gap), F116 (= F101), H128 (≠ I113), E158 (≠ S143)
binding zinc ion: E31 (≠ D16), H216 (= H207), H218 (= H209)

3ivsA Homocitrate synthase lys4 (see paper)
25% identity, 84% coverage: 9:274/315 of query aligns to 14:258/364 of 3ivsA

query
sites
3ivsA

I

I

D

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x
E

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A

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-

A

-

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A

A

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A

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L

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A

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Y

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A

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A

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D

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I

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A

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I

A

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A

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C

A

D

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I

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E

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C

H
|
H

F

F

H
|
H

D

N

T

D

Y

T

G

G

Q

M

A

A

L

I

S

A

N

N

T

A

L

Y

A

C

A

A

L

L

E

E

L

A

G

G

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A

W

T

N

H

F

I

Q

D

S

T

S

S

V

I

A

L

G

G

L

I

G

G

-

E

-

R

-

N

G

G

C

I

P

T

Y

P

A

L

K

G

G

A

A

L

T

L

G

A

N

R

V

M

A

Y

T

V

E

T

D

D

L

R

V

E

Y

Y

L

I

L

T

H

H

G

K

M

Y

G

K

I

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E

N

T

Q

G

L

I

R

D

E

L

L

D

E

K

N

L

L

V

V

active site: Q24 (= Q19)
binding cobalt (ii) ion: E21 (≠ D16), H188 (= H207), H190 (= H209)

Q53WI0 4-hydroxy-2-oxovalerate aldolase; HOA; 4-hydroxy-2-keto-pentanoic acid aldolase; 4-hydroxy-2-oxohexanoate aldolase; 4-hydroxy-2-oxopentanoate aldolase; EC 4.1.3.39; EC 4.1.3.43 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see paper)
25% identity, 86% coverage: 9:280/315 of query aligns to 13:268/347 of Q53WI0

query
sites
Q53WI0

I

V

D

D

V

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T

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R

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D

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A

E

H

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Q

H

A

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V

E

E

V

E

K

A

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A

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I

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A

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Q

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A

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L

Q

D

D

E

A

A

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G

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Y

E

A

I

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Y

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-

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G

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D

N

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H

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G

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Q

A

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G

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A

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E

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A

A

A

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E

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A

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A

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A

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A

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M

-

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