SitesBLAST

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)
51% identity, 95% coverage: 1:274/287 of query aligns to 74:347/370 of Q8TB92

query
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Q8TB92

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R86 (= R13) mutation to Q: Abolishes catalytic activity.
L237 (= L164) mutation to S: Abolishes catalytic activity.
H278 (= H205) 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.

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)
51% identity, 95% coverage: 1:274/287 of query aligns to 29:302/325 of P35914

query
sites
P35914

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E37 (= E9) to K: in HMGCLD; activity lower than 5% respect to the wild-type; mutation to D: Normal activity.
R41 (= R13) to Q: in HMGCLD; loss of activity and of proton exchange; dbSNP:rs121964997; mutation to M: Reduced activity, and loss of proton exchange.
D42 (= D14) 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 (= K20) to N: in HMGCLD; abolishes almost all enzymatic activity
E72 (= E44) mutation to A: Loss of activity, and reduced affinity for metal cofactor and substrate.
S142 (= S114) to F: in HMGCLD; activity lower than 5% respect to the wild-type
C174 (= C146) to Y: in HMGCLD; activity lower than 5% respect to the wild-type; dbSNP:rs765475941
F192 (≠ L164) to S: in HMGCLD; activity lower than 5% respect to the wild-type
I200 (≠ V172) to F: in HMGCLD; activity lower than 5% respect to the wild-type
G203 (= G175) to E: in HMGCLD; complete loss of activity; dbSNP:rs1553131940
D204 (= D176) mutation to A: Reduced activity, and reduced affinity for metal cofactor and substrate.
H233 (= H205) to R: in HMGCLD; loss of activity; dbSNP:rs727503963; mutation to A: Loss of activity, and reduced proton exchange rate.
E279 (≠ V251) mutation to A: Reduced thermal stability, but normal activity.
D280 (≠ A252) 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)
51% identity, 95% coverage: 1:274/287 of query aligns to 2:275/296 of 3mp3B

query
sites
3mp3B

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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 (= R13), D15 (= D14), Q18 (= Q17), F49 (= F48), V50 (= V49), S51 (= S50), W54 (= W53), P81 (= P80), N82 (= N81), K84 (= K83), G85 (= G84), N111 (= N110), R122 (= R121), Y140 (= Y139), S142 (= S141), T178 (= T177), H206 (= H205)
binding magnesium ion: D15 (= D14), H206 (= H205), H208 (= H207)

2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria (see paper)
51% identity, 95% coverage: 1:274/287 of query aligns to 2:275/296 of 2cw6A

query
sites
2cw6A

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binding 3-hydroxypentanedioic acid: Q18 (= Q17), F100 (= F99)
binding magnesium ion: D15 (= D14), H206 (= H205), H208 (= H207), N248 (= N247)

3mp5B Crystal structure of human lyase r41m in complex with hmg-coa (see paper)
50% identity, 95% coverage: 1:274/287 of query aligns to 2:275/296 of 3mp5B

query
sites
3mp5B

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V

P

S

T

T

A

P

D

V

K

K

I

I

A

K

L

L

I

I

D

D

R

M

L

L

S

S

S

E

C

A

G

G

Y

L

S

S

R

V

I

I

E

E

A

T

T

T

S

S

F

F

V

V

S
|
S

P

P

K

K

W
|
W

V

V

P

P

Q

Q

L

M

A

G

D

D

A

H

V

T

E

E

V

V

M

L

A

K

G

G

I

I

R

Q

R

K

A

F

D

P

S

G

V

I

R

N

Y

Y

A

P

A

V

L

L

V

T

P

P

N

N

M

L

K

K

G

G

Y

F

E

E

L

A

A

A

A

V

S

A

A

A

N

G

V

A

D

K

E

E

I

V

A

V

V

I

F
|
F

I

G

S

A

A

A

S

S

E

E

G

L

F

F

S

T

K

K

A

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

L

F

A

D

P

A

V

I

I

L

G

K

A

A

I

Q

N

S

D

A

G

N

L

I

A

S

I

V

R

R

G

G

Y
|
Y

V

V

S
|
S

C

C

V

A

V

L

E

G

C

C

P

P

Y

Y

D

E

G

G

P

K

T

I

A

S

P

P

Q

A

A

K

V

V

A

A

D

E

V

V

T

T

E

K

Q

K

L

F

F

Y

S

S

L

M

G

G

C

C

H

Y

E

E

V

I

S

S

L

L

G

G

D

D

T
|
T

I

I

G

G

R

V

G

G

T

T

P

P

E

G

S

I

I

M

G

K

T

D

M

M

L

L

D

S

A

A

V

V

L

M

N

Q

V

E

A

V

T

P

P

L

H

A

S

A

L

L

A

A

G

V

H
|
H

Y

C

H
|
H

D

D

T

T

G

Y

G

G

R

Q

A

A

L

L

D

A

N

N

I

T

R

L

V

M

S

A

L

L

E

Q

K

M

G

G

L

V

R

S

V

V

F

V

D

D

A

S

S

S

V

V

G

A

G

G

L

L

G

G

C
|
C

P

P

F

Y

A

A

P

Q

G

G

A

A

K

S

G

G

N

N

V

L

D

A

T

T

V

E

A

D

A

L

V

V

E

Y

M

M

L

L

H

E

Q

G

L

L

G

G

F

I

E

H

T

T

G

G

L

V

D

N

I

L

D

Q

K

K

L

L

R

L

S

E

A

A

binding 3-hydroxy-3-methylglutaryl-coenzyme a: D15 (= D14), Q18 (= Q17), S51 (= S50), W54 (= W53), F100 (= F99), N111 (= N110), N113 (= N112), Y140 (= Y139), S142 (= S141), T178 (= T177), C239 (= C238)
binding magnesium ion: D15 (= D14), H206 (= H205), H208 (= H207)

P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii (see paper)
48% identity, 94% coverage: 3:271/287 of query aligns to 2:270/301 of P13703

query
sites
P13703

E

Q

Y

A

V

V

E

K

I

V

V

F

E

E

M

V

V

G

A

P

R

R

D

D

G

G

L

L

Q

Q

N

N

E

E

K

R

G

Q

F

P

V

L

P

S

T

V

A

A

D

A

K

R

I

V

A

G

L

L

I

I

D

G

R

E

L

L

S

A

S

G

C

T

G

G

Y

L

S

R

R

H

I

I

E

E

A

A

T

G

S

A

F

F

V

V

S

S

P

P

K

R

W

W

V

V

P

P

Q

Q

L

M

A

A

D

G

A

S

V

D

E

E

V

V

M

L

A

R

G

Q

I

L

R

P

R

S

A

N

D

D

S

G

V

V

R

S

Y

Y

A

T

A

A

L

L

V

V

P

P

N

N

M

R

K

Q

G

G

Y

F

E

E

L

A

A

A

A

Q

S

R

A

A

N

G

V

C

D

R

E

E

I

V

A

A

V

V

F

F

I

A

S

A

A

A

S

S

E

E

G

A

F

F

S

S

K

R

A

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

L

F

A

T

P

P

V

V

I

L

G

R

A

A

I

N

N

E

D

A

G

S

L

I

A

R

I

V

R

R

G

G

Y

Y

V

V

S

S

C

C

V

V

V

L

E

G

C

C

P

P

Y

F

D

S

G

G

P

A

T

V

A

A

P

P

Q

E

A

A

V

V

A

A

D

K

V

V

T

A

E

R

Q

R

L

L

F

Y

S

E

L

L

G

G

C

C

H

Y

E

E

V

I

S

S

L

L

G

G

D

D

T

T

I

I

G

G

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A

G

G

T

R

P

P

E

D

S

E

I

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G

A

T

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M

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L

F

D

E

A

L

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C

L

A

N

R

V

Q

A

L

T

P

P

V

H

A

S

A

L

L

A

A

G

G

H

H

Y

F

H

H

D

D

T

T

G

W

G

G

R

M

A

A

L

I

D

A

N

N

I

V

R

H

V

A

S

A

L

L

E

A

K

Q

G

G

L

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R

R

V

T

F

F

D

D

A

S

S

S

V

V

G

A

G

G

L

L

G

G

C
|
C

P

P

F

Y

A

S

P

P

G

G

A

A

K

S

G

G

N

N

V

V

D

A

T

T

V

E

A

D

A

L

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M

L

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Q

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L

L

G

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Y

E

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D

D

I

L

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A

L

V

C237 (= C238) active site

6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
39% identity, 94% coverage: 1:271/287 of query aligns to 4:273/305 of 6ndsA

query
sites
6ndsA

M

F

A

S

E

D

Y

L

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L

E

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E

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M

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D
|
D

G

G

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L

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A

A

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F

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V

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S

P

P

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W

A

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x
I

P

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N

L

L

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D

D

A

G

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E

E

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M

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A

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R

A

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D

V

I

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I

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Y

A

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P

N
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N

M

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G
|
G

Y

A

E

L

L
x
R

A

A

A

V

S

E

A

A

N

N

V

A

D

N

E

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I

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A

N

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A

A

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A

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N

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x
M

N
x
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A

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S

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I

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E

A

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E

V

I

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G

-

A

E

A

Q

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N

Q

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N

G

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C

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P

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R

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A

F

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E

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C

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E

N

V

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A

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D

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T

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G

R

M

G

A

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P

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S

Q

I

V

G

K

T

R

M

I

L

V

D

S

A

H

V

V

L

L

N

S

V

L

A

I

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S

P

P

H

E

S

Q

L

L

A

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G

L

H
|
H

Y

F

H
|
H

D

N

T

T

G

R

G

G

R

L

A

G

L

L

D

T

N

N

I

V

R

L

V

A

S

A

L

Y

E

E

K

V

G

G

L

A

R

R

V

R

F

F

D

D

A

A

S

A

V

L

G

G

L

L

G

G

C

C

P

P

F

F

A

A

P

P

G

G

A

A

K

S

G

G

N

N

V

I

D

C

T

T

V

E

A

D

A

L

V

V

E

N

M

M

L

C

H

E

Q

E

L

I

G

G

F

I

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P

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T

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T

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D

D

I

L

D

D

K

A

L

L

binding coenzyme a: V52 (= V49), S53 (= S50), I57 (≠ V54), N84 (= N81), G87 (= G84), R90 (≠ L87), N113 (= N110), M114 (≠ I111), R115 (≠ N112)
binding zinc ion: D17 (= D14), H207 (= H205), H209 (= H207)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
21% identity, 97% coverage: 5:281/287 of query aligns to 22:286/399 of 6ktqA

query
sites
6ktqA

V

V

E

G

I

I

V

L

E

D

M

S

V

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A

L

R
|
R

D
x
E

G

G

L

E

Q

Q

N

T

E

P

K

G

G

V

F

V

V

F

P

T

T

T

A

D

D

Q

K

R

I

V

A

E

L

I

I

A

D

K

R

A

L

L

S

S

S

D

C

I

G

G

Y

V

S

Q

R

M

I

I

E

E

A

A

T

G

S

H

F

-

V

-

S

-

P

P

K

A

W
x
V

V

S

P

P

Q

D

L

I

A

Y

D

E

A

G

V

I

E

R

V

R

M

I

A

I

G

K

I

L

R

K

R

R

A

E

D

G

S

V

V

I

R

K

Y

S

A

E

A

I

L

V

V

A

P

H

N

S

-
x
R

-
x
A

-

V

M

K

K

R

G

D

Y

I

E

E

L

V

A

G

A

A

S

E

A

I

N

E

V

A

D

D

E

R

I

I

A

A

V

I

F
|
F

I

Y

S

G

A

I

S

S

E

D

G

T

F

H

S

L

K

K

A

A

N

K

I
x
H

N

H

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T

I

R

A

D

E

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S

A

I

L

E

R

R

S

L

I

A

A

P

E

V

T

I

V

G

S

A

Y

A

A

I

K

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S

D

H

G

G

L

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A

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R

G

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x
T

V

A

S
x
E

C

D

V

A

V

T

E

R

C

A

P

D

Y

Y

D

-

G

-

P

-

T

-

A

-

P

-

Q

Q

A

Y

V

L

A

L

D

E

V

V

T

I

E

K

Q

T

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V

F

R

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D

L

A

G

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C

A

H

D

E

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|
S

L

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|
T

I

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R

V

G

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T

Y

P

P

E

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S

R

I

T

G

R

T

E

M

L

L

F

D

K

A

D

V

L

L

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N

S

V

R

A

F

T

P

P

D

H

I

S

E

L

F

A

D

G

I

H
|
H

Y

A

H
|
H

D

N

T

D

G

L

G

G

R

M

A

A

L

V

D

A

N

N

I

V

R

L

V

A

S

A

L

A

E

E

K

G

G

G

L

A

R

T

V

I

F

I

D

H

A

T

S

T

V

L

G

N

G

G

L

L

G

G

-

E

G

R

C

V

P

G

F

I

A

A

P

P

G

L

A

-

K

-

G

-

N

-

V

-

D

-

T

Q

V

V

A

V

A

A

V

A

E

A

M

L

L

K

H

Y

Q

H

L

F

G

G

F

I

E

E

T

V

G

-

L

V

D

D

I

L

D

K

K

K

L

L

R

S

S

E

A

V

A

A

L

S

L

L

A

V

Q

E

V

K

F

Y

binding 2-oxoglutaric acid: R30 (= R13), R154 (= R137), T156 (≠ Y139), E158 (≠ S141), S184 (= S173), T188 (= T177), H216 (= H205), H218 (= H207)
binding coenzyme a: V67 (≠ W53), R96 (vs. gap), A97 (vs. gap), F116 (= F99), H128 (≠ I111), E158 (≠ S141)
binding zinc ion: E31 (≠ D14), H216 (= H205), H218 (= H207)

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
23% identity, 80% coverage: 7:236/287 of query aligns to 32:250/400 of 3ivtB

query
sites
3ivtB

I

I

V

I

E

E

M

S

V

T

A

L

R
|
R

D
x
E

G

G

L

E

Q
|
Q

N

F

E

A

K

N

G

A

F

F

V

F

P

D

T

T

A

E

D

K

K

K

I

I

A

Q

L

I

I

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A

L

L

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D

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N

C

F

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G

Y

V

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I

I

E

E

A

L

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S

S

F

P

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V

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A

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W

Q

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R

Q

Q

L

D

A

C

D

E

A

A

V

I

-

C

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K

-

L

-

G

-

L

-

K

-

C

E

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A

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G
x
H

I

I

R

R

R

-

A

-

D

-

S

-

V

-

R

-

Y

-

A

-

L

-

V

-

P

C

N

H

M

M

K

D

G

D

Y

A

E

R

L

V

A

A

A

V

S

E

A

T

N

G

V

V

D

D

E

G

I

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A

D

V

V

F

V

I

I

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A

T

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K

A

Y

N

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H

N

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I

I

I

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L

A

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A

F

A

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N

S

D

K

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G

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I

A

E

I

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R
|
R

-

F

-
x
S

-

S

-

E

-

D

G

S

Y

F

V

R

S

S

C

D

V

L

V

V

E

D

C

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Y

-

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-

A

-

P

-

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-

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-

V

L

A

L

D

S

V

L

T

Y

E

K

Q

A

L

V

F

D

S

K

L

I

G

G

C

V

H

N

E

R

V

V

S

G

L

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G

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T

I

V

G

G

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C

G

A

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T

P

P

E

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S

Q

I

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Y

T

D

M

L

L

I

D

R

A

T

V

L

L

R

N

G

V

V

A

V

T

S

P

C

H

-

S

D

L

I

A

E

G

C

H
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H

Y

F

H
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H

D

N

T

D

G

T

G

G

R

M

A

A

L

I

D

A

N

N

I

A

R

Y

V

C

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A

L

L

E

E

K

A

G

G

L

A

R

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D

D

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G

G

L

I

G

G

active site: Q42 (= Q17)
binding 2-oxoglutaric acid: R38 (= R13), H98 (≠ G66), R158 (= R137), S160 (vs. gap), T192 (= T177), H219 (= H205), H221 (= H207)
binding zinc ion: E39 (≠ D14), H219 (= H205), H221 (= H207)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
23% identity, 80% coverage: 7:236/287 of query aligns to 37:255/418 of Q9Y823

query
sites
Q9Y823

I

I

V

I

E

E

M

S

V

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A

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R
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R

D
x
E

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Q

N

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N

G

A

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F

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K

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E

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A

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x
H

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R

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A

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Y

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-

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P

C

N

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M

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Y

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x
D

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R

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x
S

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S

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E

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N

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T

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L

R

N

G

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C

H

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S

D

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I

A
x
E

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H

Y

F

H
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H

D

N

T

D

G

T

G

G

R

M

A

A

L

I

D

A

N

N

I

A

R

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S

A

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L

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E

K

A

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L

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G

R43 (= R13) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D14) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q17) mutation to A: Abolishes the catalytic activity.
E74 (= E44) 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 (≠ G66) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ A97) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (= R137) 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 (vs. gap) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (vs. gap) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T177) 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 (≠ A203) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H205) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H207) binding 2-oxoglutarate; binding Zn(2+)

Sites not aligning to the query:

288 R→K: Does not affect the catalytic activity but impairs L-lysine inhibition.
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.

2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
31% identity, 42% coverage: 155:275/287 of query aligns to 157:270/453 of 2nx9B

query
sites
2nx9B

Q

Q

A

T

V

W

A

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D

V

V

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E

Q

Q

Q

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x
K

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K

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V

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H

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H

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M

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A

A

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N

L

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D

A

T

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A

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V

-

E

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M

-

L

L

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Q

Q

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K

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I

A

A

active site: K177 (≠ G175), H206 (= H205), H208 (= H207)
binding zinc ion: H206 (= H205), H208 (= H207)

Sites not aligning to the query:

active site: 16, 19, 120, 341
binding zinc ion: 16

5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
25% identity, 97% coverage: 5:283/287 of query aligns to 3:271/580 of 5ks8D

query
sites
5ks8D

V

V

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K

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R

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R

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L

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x
R

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N

N

M

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K

L

G

G

Y

Y

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A

Y

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S

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A

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N

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x
D

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N

N

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I

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A

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A

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S

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x
K

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P

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L

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A

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P

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I

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H

L

L

A

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G

-

H
|
H

Y

A

H
|
H

D

A

T

T

G

S

G

G

R

L

A

A

L

S

D

M

N

S

I

I

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V

R

S

A

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D

K

N

G

G

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R

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F

V

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D

A

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V

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G

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L

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G

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C

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P

-

F

F

A

A

P

E

G

G

A

A

K

S

G

L

N

P

V

A

D

-

T

T

V

E

A

S

A

I

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E

A

M

A

L

L

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K

Q

G

L

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T

T

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G

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L

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D

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I

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K

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E

active site: D12 (= D14), D116 (≠ S107), K173 (≠ G175), H202 (= H205), H204 (= H207)
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: D51 (≠ F48), Y56 (≠ W53)
binding manganese (ii) ion: D12 (= D14), K173 (≠ G175), H202 (= H205), H204 (= H207)
binding pyruvic acid: Q15 (= Q17), G47 (vs. gap), L80 (= L78), R82 (vs. gap)

Sites not aligning to the query:

5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
25% identity, 97% coverage: 5:283/287 of query aligns to 2:270/603 of 5ks8C

query
sites
5ks8C

V

V

E

H

I

V

V

T

E

D

M

V

V

V

A

L

R

R

D
|
D

G

G

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H

Q

Q

N

S

E

L

K

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G

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R

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D

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S

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Y

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A

A

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F

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L

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D

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K

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R

R

K

A

A

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S

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R

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L

A

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A

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L

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L

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x
R

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G

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Q

N

N

M

L

K

L

G

G

Y

Y

E

R

L

H

A

Y

A

S

S

D

A

-

N

-

V

-

D

D

E

V

I

V

A

R

V

A

F

F

I

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Q

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K

S

S

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A

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N

G

G

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I

-

D

-

V

-

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-

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-

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F
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F

S
x
D

K

A

A

M

N

N

I

D

N

L

C

R

S

N

I

L

A

K

E

V

S

S

I

I

E

E

R

S

L

V

A

K

P

A

V

V

I

-

G

-

A

-

I

-

N

-

D

-

G

G

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K

A

H

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A

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G

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T

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P

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H

D

D

G

I

P

P

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Y

A

-

P

-

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-

A

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F

A

V

D

N

V

L

T

A

E

K

Q

E

L

L

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S

L

F

G

G

C

C

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D

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A

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x
K

D

D

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x
M

I

A

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G

L

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T

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P

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S

V

I

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G

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M

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L

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D

K

A

A

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E

-

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V

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P

H

I

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H

L

L

A

-

G

-

H
|
H

Y

A

H
|
H

D

A

T

T

G

S

G

G

R

L

A

A

L

S

D

M

N

S

I

I

R

Q

V

R

S

A

L

V

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D

K

N

G

G

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R

A

V

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F

V

D

D

A

G

S

C

V

I

G

S

L

-

G

-

C

-

P

-

F

F

A

A

P

E

G

G

A

A

K

S

G

L

N

P

V

A

D

-

T

T

V

E

A

S

A

I

V

V

E

A

M

A

L

L

H

K

Q

G

L

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G

E

F

Y

E

D

T

T

G

G

L

L

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D

I

I

D

G

K

L

L

L

R

Q

S

E

A

-

L

-

L

I

A

S

Q

A

V

Y

F

F

R

R

Q

E

active site: D11 (= D14), D115 (≠ S107), K172 (≠ G175), H201 (= H205), H203 (= H207)
binding manganese (ii) ion: D11 (= D14), K172 (≠ G175), H201 (= H205), H203 (= H207)
binding pyruvic acid: L79 (= L78), R81 (vs. gap), F114 (= F106), M174 (≠ T177)

Query Sequence

>WP_094506056.1 NCBI__GCF_002252445.1:WP_094506056.1
MAEYVEIVEMVARDGLQNEKGFVPTADKIALIDRLSSCGYSRIEATSFVSPKWVPQLADA
VEVMAGIRRADSVRYAALVPNMKGYELAASANVDEIAVFISASEGFSKANINCSIAESIE
RLAPVIGAAINDGLAIRGYVSCVVECPYDGPTAPQAVADVTEQLFSLGCHEVSLGDTIGR
GTPESIGTMLDAVLNVATPHSLAGHYHDTGGRALDNIRVSLEKGLRVFDASVGGLGGCPF
APGAKGNVDTVAAVEMLHQLGFETGLDIDKLRSAALLAQVFRQDKAA

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