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)
53% identity, 94% coverage: 1:267/283 of query aligns to 74:340/370 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, 97% coverage: 1:274/283 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 (= I172) 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 (= E251) 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, 97% coverage: 1:274/283 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 (≠ R83), 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, 97% coverage: 1:274/283 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, 97% coverage: 1:274/283 of query aligns to 2:275/296 of 3mp5B

query
sites
3mp5B

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M

L

L

T

S

D

E

A

A

G

G

F

L

R

S

R

V

I

I

E

E

V

T

A

T

S

S

F

F

V

V

S
|
S

P

P

R

K

W
|
W

V

V

P

P

Q

Q

M

M

A

G

G

D

S

H

G

T

E

E

V

V

L

L

A

K

G

G

I

I

R

Q

R

K

N

F

S

P

D

G

V

I

R

N

Y

Y

A

P

A

V

L

L

T

T

P

P

N

N

M

L

R

K

G

G

Y

F

E

E

D

A

A

A

L

V

T

A

A

A

K

G

A

A

D

K

E

E

I

V

A

V

I

I

F
|
F

A

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

A

C

S

S

V

I

A

E

E

E

S

S

I

F

E

Q

R

R

F

F

T

D

P

A

I

I

I

L

E

K

A

A

R

Q

H

S

I

A

D

N

M

I

P

S

V

V

R

R

G

G

Y
|
Y

I

V

S
|
S

C

C

V

A

T

L

E

G

C

C

P

P

F

Y

D

E

G

G

P

K

T

I

D

S

P

P

D

A

A

K

V

V

A

A

A

E

L

V

A

T

D

K

R

K

L

F

F

Y

S

S

M

M

G

G

C

C

Y

Y

E

E

I

I

S

S

L

L

G

G

D

D

T
|
T

I

I

G

G

Q

V

A

G

T

T

P

P

D

G

S

I

I

M

A

K

R

D

M

M

L

L

L

S

A

A

V

V

R

M

E

Q

R

E

V

V

P

P

V

L

T

A

R

A

L

L

A

A

G

V

H
|
H

Y

C

H
|
H

D

D

T

T

A

Y

G

G

R

Q

A

A

I

L

D

A

N

N

I

T

D

L

A

M

S

A

L

L

S

Q

L

M

G

G

V

V

R

S

V

V

F

V

D

D

A

S

V

V

G

A

G

G

L

L

G

G

C
|
C

P

P

Y

Y

A

A

P

Q

G

G

A

A

A

S

G

G

N

N

V

L

A

A

T

T

E

E

A

D

V

L

H

V

E

Y

H

M

L

L

T

E

R

G

L

L

G

G

Y

I

E

H

T

T

G

G

L

V

K

N

G

L

D

Q

V

K

L

L

T

L

D

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)

6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
37% identity, 100% coverage: 1:283/283 of query aligns to 4:285/305 of 6ndsA

query
sites
6ndsA

M

F

S

S

E

D

S

L

V

L

E

V

I

V

F

Q

E

E

V

V

G

S

P

P

R

R

D
|
D

G

G

L

L

Q

Q

N

I

E

E

K

P

R

T

D

W

I

V

P

P

V

T

A

D

E

K

K

K

I

I

A

D

L

L

I

I

D

N

R

Q

L

L

T

S

D

T

A

M

G

G

F

F

R

S

R

R

I

I

E

E

V

A

A

G

S

S

F

F

V
|
V

S
|
S

P

P

R

K

W

A

V
x
I

P

P

Q

N

M

L

A

R

G

D

S

G

G

E

E

E

V

V

L

F

A

T

G

G

I

I

R

T

R

R

N

H

S

K

D

D

V

I

R

I

Y

Y

A

V

A

G

L

L

T

I

P

P

N
|
N

M

L

R

K

G
|
G

Y

A

E

L

D
x
R

A

A

L

V

T

E

A

A

K

N

A

A

D

N

E

E

I

L

A

N

I

L

F

V

A

L

S

S

A

A

S

S

E

Q

G

T

F

H

S

N

K

L

A

A

N
|
N

I
x
M

N
x
R

A

M

S

T

V

K

A

A

E

Q

S

S

I

F

E

A

R

G

F

F

T

T

P

E

I

I

I

V

E

E

A

Q

A

L

R

Q

H

G

I

-

D

K

M

T

P

Q

V

F

R

N

G

G

Y

T

I

V

S

A

C

T

V

T

T

F

E

G

C

C

P

P

F

F

D

E

G

G

P

K

T

I

D

S

P

E

D

R

A

E

V

V

A

F

A

S

L

L

A

V

D

E

R

H

L

Y

F

L

S

K

M

L

G

G

C

I

Y

H

E

N

I

I

S

T

L

L

G

A

D

D

T

T

I

T

G

G

Q

M

A

A

T

N

P

P

D

V

S

Q

I

V

A

K

R

R

M

I

L

V

L

S

A

H

V

V

R

L

E

S

R

L

V

I

P

S

V

P

T

E

R

Q

L

L

A

T

G

L

H
|
H

Y

F

H
|
H

D

N

T

T

A

R

G

G

R

L

A

G

I

L

D

T

N

N

I

V

D

L

A

A

S

A

L

Y

S

E

L

V

G

G

V

A

R

R

V

R

F

F

D

D

A

A

V

L

G

G

L

L

G

G

C

C

P

P

Y

F

A

A

P

P

G

G

A

A

A

S

G

G

N

N

V

I

A

C

T

T

E

E

A

D

V

L

H

V

E

N

H

M

L

C

T

E

R

E

L

I

G

G

Y

I

E

P

T

T

G

T

L

I

K

D

G

L

D

D

V

A

L

L

T

I

D

Q

A

L

A

S

A

R

M

T

A

L

R

P

A

A

M

L

R

L

G

G

binding coenzyme a: V52 (= V49), S53 (= S50), I57 (≠ V54), N84 (= N81), G87 (= G84), R90 (≠ D87), N113 (= N110), M114 (≠ I111), R115 (≠ N112)
binding zinc ion: D17 (= D14), H207 (= H205), H209 (= H207)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
26% identity, 79% coverage: 13:236/283 of query aligns to 12:220/314 of 2zyfA

query
sites
2zyfA

R
|
R

D
x
E

G

G

L

E

Q
|
Q

N

F

E

E

K

K

R

A

D

N

I

F

P

S

V

T

A

Q

E

D

K

K

I

V

A

E

L

I

I

A

D

K

R

A

L

L

T

D

D

E

A

F

G

G

F

I

R

E

R

Y

I

I

E

E

V

V

A

T

S

-

F

-

V

-

S

T

P

P

R

V

W

A

V

S

P

P

Q

Q

M

S

A

R

G

K

S

D

G

A

E

E

V

V

L

L

A

A

G

S

I

L

R

G

R

L

N

K

S

A

D

K

V

V

R

-

Y

V

A

T

A
x
H

L

I

T

Q

P

C

N

R

M

L

R

D

G

A

Y

A

E

K

D

V

A

A

L

V

T

E

A

T

K

G

A

V

D

Q

E

G

I

I

A

D

I

L

F
x
L

A

F

S

G

A

T

S

S

E

K

G

G

F

-

S

-

K

-

A

R

N

D

I

I

N

P

A

R

S

I

V

I

A

E

E

E

S

A

I

K

E

E

R

V

F

I

T

A

P

Y

I

I

I

R

E

E

A

A

R

P

H

H

I

V

D

E

M

V

P
x
R

V

F

R

S

G

A

Y

E

I

D

S

T

C

F

V

R

T

S

E

E

C

E

P

Q

F

-

D

D

G

L

P

L

T

A

D

V

P

Y

D

E

A

A

V

V

A

A

A

P

L

Y

A

V

D

D

R

R

L

-

F

-

S

-

M

-

G

-

C

-

Y

-

E

-

I

V

S

G

L

L

G

A

D

D

T
|
T

I

V

G

G

Q

V

A

A

T

T

P

P

D

R

S

Q

I

V

A

Y

R

A

M

L

L

V

L

R

A

E

V

V

R

R

E

R

R

V

V

V

-

G

P

P

V

R

T

V

R

D

L

I

A

E

G

F

H
|
H

Y

G

H
|
H

D

N

T

D

A

T

G

G

R

C

A

A

I

I

D

A

N

N

I

A

D

Y

A

E

S

A

L

I

S

E

L

A

G

G

V

A

R

T

V

H

F

V

D

D

A

T

V

I

G

L

G

G

L

I

G

G

active site: Q16 (= Q17)
binding 2-oxoglutaric acid: R12 (= R13), H72 (≠ A77), L94 (≠ F99), R127 (≠ P135), T160 (= T177), H189 (= H205)
binding magnesium ion: E13 (≠ D14), H189 (= H205), H191 (= H207)

5ks8D Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
29% identity, 55% coverage: 126:282/283 of query aligns to 128:273/580 of 5ks8D

query
sites
5ks8D

I

I

E

E

A

S

A

V

R

K

H

A

I

V

D

G

M

K

P

H

V

A

R

E

G

G

Y

T

I

I

S

S

C

Y

V

T

T

T

E

S

C

P

P

V

F

H

D

D

G

I

P

P

T

Y

D

-

P

-

D

-

A

-

V

F

A

V

A

N

L

L

A

A

D

K

R

E

L

L

F

E

S

S

M

F

G

G

C

C

Y

D

E

T

I

I

S

A

L

I

G
x
K

D

D

T

M

I

A

G

S

Q

L

A

L

T

T

P

P

D

Q

S

V

I

T

A

G

R

D

M

L

L

V

L

K

A

A

V

L

R

R

E

E

R

A

V

V

P

S

V

L

T

P

R

-

L

I

A

H

G

L

H
|
H

Y

A

H
|
H

D

A

T

T

A

S

G

G

R

L

A

A

I

S

D

M

N

S

I

I

D

Q

A

R

S

A

L

V

S

D

L

N

G

G

V

V

R

A

V

I

F

V

D

D

A

G

A

C

V

I

G

S

L

-

G

-

C

-

P

-

Y

F

A

A

P

E

G

G

A

A

A

S

G

L

N

P

V

-

A

A

T

T

E

E

A

S

V

I

H

V

E

A

H

A

L

L

T

K

R

G

L

T

G

E

Y

Y

E

D

T

T

G

G

L

L

K

D

G

I

D

G

V

L

L

L

T

Q

D

E

A

I

A

S

A

A

M

Y

A

F

R

R

A

E

M

V

R

R

active site: K173 (≠ G175), H202 (= H205), H204 (= H207)
binding manganese (ii) ion: K173 (≠ G175), H202 (= H205), H204 (= H207)

Sites not aligning to the query:

active site: 12, 116
binding 5-(hexahydro-2-oxo-1h-thieno[3,4-d]imidazol-6-yl)pentanal: 51, 56, 299, 337, 340, 341
binding manganese (ii) ion: 12
binding pyruvic acid: 15, 47, 80, 82, 337

5ks8C Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
29% identity, 55% coverage: 126:282/283 of query aligns to 127:272/603 of 5ks8C

query
sites
5ks8C

I

I

E

E

A

S

A

V

R

K

H

A

I

V

D

G

M

K

P

H

V

A

R

E

G

G

Y

T

I

I

S

S

C

Y

V

T

T

T

E

S

C

P

P

V

F

H

D

D

G

I

P

P

T

Y

D

-

P

-

D

-

A

-

V

F

A

V

A

N

L

L

A

A

D

K

R

E

L

L

F

E

S

S

M

F

G

G

C

C

Y

D

E

T

I

I

S

A

L

I

G
x
K

D

D

T
x
M

I

A

G

S

Q

L

A

L

T

T

P

P

D

Q

S

V

I

T

A

G

R

D

M

L

L

V

L

K

A

A

V

L

R

R

E

E

R

A

V

V

P

S

V

L

T

P

R

-

L

I

A

H

G

L

H
|
H

Y

A

H
|
H

D

A

T

T

A

S

G

G

R

L

A

A

I

S

D

M

N

S

I

I

D

Q

A

R

S

A

L

V

S

D

L

N

G

G

V

V

R

A

V

I

F

V

D

D

A

G

A

C

V

I

G

S

L

-

G

-

C

-

P

-

Y

F

A

A

P

E

G

G

A

A

A

S

G

L

N

P

V

-

A

A

T

T

E

E

A

S

V

I

H

V

E

A

H

A

L

L

T

K

R

G

L

T

G

E

Y

Y

E

D

T

T

G

G

L

L

K

D

G

I

D

G

V

L

L

L

T

Q

D

E

A

I

A

S

A

A

M

Y

A

F

R

R

A

E

M

V

R

R

active site: K172 (≠ G175), H201 (= H205), H203 (= H207)
binding manganese (ii) ion: K172 (≠ G175), H201 (= H205), H203 (= H207)
binding pyruvic acid: M174 (≠ T177)

Sites not aligning to the query:

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
26% identity, 79% coverage: 13:236/283 of query aligns to 12:226/376 of O87198

query
sites
O87198

R
|
R

D
x
E

G

G

L

E

Q

Q

N

F

E

E

K

K

R

A

D

N

I

F

P

S

V

T

A

Q

E

D

K

K

I

V

A

E

L

I

I

A

D

K

R

A

L

L

T

D

D

E

A

F

G

G

F

I

R

E

R

Y

I

I

E

E

V

V

A

T

S

T

F

P

V

V

S

A

P

S

R

-

W

-

V

-

P

P

Q

Q

M

S

A

R

G

K

S

D

G

A

E

E

V

V

L

L

A

A

G

S

I

L

R

G

R

L

N

K

S

A

D

K

V

V

R

-

Y

V

A

T

A
x
H

L

I

T

Q

P

C

N

R

M

L

R

D

G

A

Y

A

E

K

D

V

A

A

L

V

T

E

A

T

K

G

A

V

D

Q

E

G

I

I

A
x
D

I

L

F

L

A

F

S

G

A

T

S

S

E

K

G

Y

F

L

S

R

K

A

A

A

N

H

-

G

-

R

-

D

I

I

N

P

A

R

S

I

V

I

A

E

E

E

S

A

I

K

E

E

R

V

F

I

T

A

P

Y

I

I

I

R

E

E

A

A

R

P

H

H

I

V

D

E

M

V

P
x
R

V

F

R
x
S

G

A

Y

E

I

D

S

T

C

F

V

R

T

S

E

E

C

E

P

Q

F

-

D

D

G

L

P

L

T

A

D

V

P

Y

D

E

A

A

V

V

A

A

A

P

L

Y

A

V

D

D

R

R

L

-

F

-

S

-

M

-

G

-

C

-

Y

-

E

-

I

V

S

G

L

L

G

A

D

D

T
|
T

I

V

G

G

Q

V

A

A

T

T

P

P

D

R

S

Q

I

V

A

Y

R

A

M

L

L

V

L

R

A

E

V

V

R

R

E

R

R

V

V

V

-

G

P

P

V

R

T

V

R

D

L

I

A

E

G

F

H
|
H

Y

G

H
|
H

D

N

T

D

A

T

G

G

R

C

A

A

I

I

D

A

N

N

I

A

D

Y

A

E

S

A

L

I

S

E

L

A

G

G

V

A

R

T

V

H

F

V

D

D

A

T

V

I

G

L

G

G

L

I

G

G

R12 (= R13) binding 2-oxoglutarate
E13 (≠ D14) binding Mg(2+)
H72 (≠ A77) binding 2-oxoglutarate; mutation to L: Significant decrease in sensitivity to lysine inhibition. Large decrease in affinity for 2-oxoglutarate. Almost no effect on affinity for acetyl-CoA and on turnover number.
D92 (≠ A97) binding L-lysine
R133 (≠ P135) binding 2-oxoglutarate
S135 (≠ R137) binding L-lysine
T166 (= T177) binding 2-oxoglutarate; binding L-lysine
H195 (= H205) binding Mg(2+)
H197 (= H207) binding Mg(2+)

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
23% identity, 54% coverage: 85:236/283 of query aligns to 174:323/503 of P0DO78

query
sites
P0DO78

Y

W

E

E

D

A

A

V

L

K

T

Y

A

A

K

K

A

R

D

P

E

K

I

I

A

L

I

I

F

F

A

T

S

S

A

T

S

S

E

D

G

I

F

H

S

M

K

K

A

Y

N

K

I

L

N

K

A

K

S

T

V

K

A

E

E

E

S

V

I

I

E

E

R

M

F

A

T

T

P

S

I

S

I

I

E

R

A

F

A

A

R

K

H

S

I

L

D

-

M

-

P

-

V

-

R

-

G

G

Y

F

I

I

S

D

C

V

V

Q

T

L

E

G

C

C

P

E

F

D

D

G

G

G

P

R

T

S

D

E

P

K

D

E

A

F

V

L

A

C

A

K

L

I

A

L

D

G

R

E

L

A

F

I

S

K

M

A

G

G

C

A

Y

T

E

A

I

V

S

N

L

V

G

A

D

D

T

T

I

V

G

G

Q

I

A

N

T

M

P

P

D

E

S

E

I

Y

A

G

R

E

M

L

L

V

L

R

A

Y

V

L

R

K

E

A

R

N

V

T

P

P

V

G

T

I

R

D

-

D

-

I

-

V

L

F

A

S

G

V

H
|
H

Y

C

H
|
H

D

N

T

D

A

L

G

G

R

V

A

A

I

T

D

A

N

N

I

T

D

I

A

A

S

G

L

V

S

C

L

A

G

G

V

A

R

R

V

Q

F

V

D

E

A

V

A

T

V

V

G

N

G

G

L

I

G

G

H292 (= H205) mutation to A: Lost catalytic activity.
H294 (= H207) mutation to A: Lost catalytic activity.

Sites not aligning to the query:

93 R→A: Lost catalytic activity.
94 D→A: Lost catalytic activity.
392 H→A: Lost catalytic activity.

5ks8F Crystal structure of two-subunit pyruvate carboxylase from methylobacillus flagellatus (see paper)
29% identity, 55% coverage: 126:282/283 of query aligns to 127:266/482 of 5ks8F

query
sites
5ks8F

I

I

E

E

A

S

A

V

R

K

H

A

I

V

D

G

M

K

P

H

V

A

R

E

G

G

Y

T

I

I

S

S

C

Y

V

T

T

T

E

S

C

P

P

V

F

H

D

D

G

I

P

P

T

Y

D

-

P

-

D

-

A

-

V

F

A

V

A

N

L

L

A

A

D

K

R

E

L

L

F

E

S

S

M

F

G

G

C

C

Y

D

E

T

I

I

S

A

L

I

G
x
K

D

D

T
x
M

I

A

G

S

Q

L

A

L

T

T

P

P

D

Q

S

V

I

T

A

G

R

D

M

L

L

V

L

K

A

A

V

L

R

R

E

E

R

A

V

V

P

S

V

L

T

P

R

-

L

I

A

H

G

L

H
|
H

Y

A

H
|
H

D

A

T

T

A

S

G

G

R

L

A

A

I

S

D

M

N

S

I

I

D

Q

A

R

S

A

L

V

S

D

L

N

G

G

V

V

R

A

V

I

F

V

D

D

A

G

A

C

V

I

G

S

L

-

G

-

C

-

P

-

Y

F

A

A

P

E

G

G

A

A

A

S

G

L

N

P

V

-

A

A

T

T

E

E

A

S

V

I

H

V

E

E

H

-

L

-

T

-

R

-

L

-

G

-

Y

Y

E

D

T

T

G

G

L

L

K

D

G

I

D

G

V

L

L

L

T

Q

D

E

A

I

A

S

A

A

M

Y

A

F

R

R

A

E

M

V

R

R

active site: K172 (≠ G175), H201 (= H205), H203 (= H207)
binding manganese (ii) ion: K172 (≠ G175), M174 (≠ T177), H201 (= H205), H203 (= H207)

Sites not aligning to the query:

active site: 11, 115
binding manganese (ii) ion: 11

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
26% identity, 79% coverage: 13:236/283 of query aligns to 11:219/347 of 3a9iA

query
sites
3a9iA

R
|
R

D
x
E

G

G

L

E

Q

Q

N

F

E

E

K

K

R

A

D

N

I

F

P

S

V

T

A

Q

E

D

K

K

I

V

A

E

L

I

I

A

D

K

R

A

L

L

T

D

D

E

A

F

G

G

F

I

R

E

R

Y

I

I

E

E

V

V

A

T

S

T

F

P

V

V

S

A

P

S

R

-

W

-

V

-

P

P

Q

Q

M

S

A

R

G

K

S

D

G

A

E

E

V

V

L

L

A

A

G

S

I

L

R

G

R

L

N

K

S

A

D

K

V

V

R

-

Y

V

A

T

A

H

L

I

T

Q

P

C

N

R

M

L

R

D

G

A

Y

A

E

K

D

V

A

A

L

V

T

E

A

T

K

G

A

V

D

Q

E

G

I

I

A
x
D

I

L

F

L

A

F

S

G

A

T

S

S

E

K

G

Y

F

L

S

-

K

-

A

-

N

D

I

I

N

P

A

R

S

I

V

I

A

E

E

E

S

A

I

K

E

E

R

V

F

I

T

A

P

Y

I

I

I

R

E

E

A

A

R

P

H

H

I

V

D

E

M

V

P

R

V

F

R
x
S

G

A

Y

E

I

D

S

T

C

F

V

R

T

S

E

E

C

E

P

Q

F

-

D

D

G

L

P

L

T

A

D

V

P

Y

D

E

A

A

V

V

A

A

A

P

L

Y

A

V

D

D

R

R

L

-

F

-

S

-

M

-

G

-

C

-

Y

-

E

-

I

V

S

G

L

L

G

A

D

D

T
|
T

I

V

G

G

Q

V

A

A

T

T

P

P

D

R

S

Q

I

V

A

Y

R

A

M

L

L

V

L

R

A

E

V

V

R

R

E

R

R

V

V

V

-

G

P

P

V

R

T

V

R

D

L

I

A

E

G

F

H
|
H

Y

G

H
|
H

D

N

T

D

A

T

G

G

R

C

A

A

I

I

D

A

N

N

I

A

D

Y

A

E

S

A

L

I

S

E

L

A

G

G

V

A

R

T

V

H

F

V

D

D

A

T

V

I

G

L

G

G

L

I

G

G

binding cobalt (ii) ion: E12 (≠ D14), H188 (= H205), H190 (= H207)
binding lysine: R11 (= R13), D91 (≠ A97), S128 (≠ R137), T159 (= T177), H188 (= H205), H190 (= H207)

2nx9B Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase na+ pump from vibrio cholerae (see paper)
31% identity, 43% coverage: 160:282/283 of query aligns to 162:277/453 of 2nx9B

query
sites
2nx9B

L

V

A

A

D

Q

R

Q

L

L

F

A

S

E

M

L

G

G

C

V

Y

D

E

S

I

I

S

A

L

L

G
x
K

D

D

T

M

I

A

G

G

Q

I

A

L

T

T

P

P

D

Y

S

A

I

A

A

E

R

E

M

L

L

V

L

S

A

T

V

L

R

K

E

K

R

Q

V

V

P

D

V

V

T

-

R

E

L

L

A

H

G

L

H
|
H

Y

C

H
|
H

D

S

T

T

A

A

G

G

R

L

A

A

I

D

D

M

N

T

I

L

D

L

A

K

S

A

L

I

S

E

L

A

G

G

V

V

R

D

V

R

F

V

D

D

A

T

A

A

V

I

G

S

L

M

G

S

G

-

C

-

P

-

Y

-

A

-

P

-

G

G

A

T

A

Y

G

G

N

H

V

P

A

A

T

T

E

E

A

S

V

L

H

V

E

A

H

T

L

L

T

Q

R

G

L

T

G

G

Y

Y

E

D

T

T

G

G

L

L

K

D

G

I

D

A

V

K

L

L

T

E

D

Q

A

I

A

A

M

Y

A

F

R

R

A

D

M

V

R

R

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

P11154 Pyruvate carboxylase 1; Pyruvic carboxylase 1; PCB 1; EC 6.4.1.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
25% identity, 37% coverage: 155:260/283 of query aligns to 714:826/1178 of P11154

query
sites
P11154

D

D

A

Y

V

Y

A

L

A

E

L

I

A

A

D

E

R

K

L

I

F

V

S

Q

M

M

G

G

C

T

Y

H

E

I

I

L

S

G

L

I

G

K

D

D

T

M

I

A

G

G

Q

T

A

M

T

K

P

P

D

A

S

A

I

A

A

K

R

L

M

L

L

I

L

G

A

S

V

L

R

R

E

A

R

K

V

Y

P

P

V

D

T

L

R

P

L

I

A

H

G

V

H

H

Y

T

H

H

D

D

T

S

A

A

G

G

R

T

A

A

I

V

D

A

N

S

I

M

D

T

A

A

S

C

L

A

S

L

L

A

G

G

V

A

R

D

V

V

F

V

D

D

A

V

A

A

V

I

G

N

G

S

L

M

G

S

G

G

C

L

P

T

Y

S

A

Q

P

P

-

S

-

I

-

N

-

A

-

L

-

A

G

S

A

L

A

E

G

G

N

N

V

I

A

D

T

T

E

G

A

I

V

N

H

V

E

E

H

H

L

V

T

R

R

E

L

L

Sites not aligning to the query:

1135 modified: N6-biotinyllysine

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
23% identity, 54% coverage: 85:236/283 of query aligns to 174:323/506 of Q9FG67

query
sites
Q9FG67

Y

W

E

E

D

A

A

L

L

K

T

Y

A

A

K

K

A

R

D

P

E

R

I

I

A

L

I

V

F

F

A

T

S

S

A

T

S

S

E

D

G

I

F

H

S

M

K

K

A

Y

N

K

I

L

N

K

A

K

S

T

V

Q

A

E

E

E

S

V

I

I

E

E

R

M

F

A

T

V

P

S

I

S

I

I

E

R

A

F

A

A

R

K

H

S

I

L

D

-

M

-

P

-

V

-

R

-

G

G

Y

F

I

N

S

D

C

I

V

Q

T

F

E

G

C

C

P

E

F

D

D

G

G

G

P

R

T

S

D

D

P

K

D

D

A

F

V

L

A

C

A

K

L

I

A

L

D

G

R

E

L

A

F

I

S

K

M

A

G

G

C

V

Y

T

E

V

I

V

S

T

L

I

G

G

D

D

T

T

I

V

G

G

Q

I

A

N

T

M

P

P

D

H

S

E

I

Y

A

G

R

E

M

L

L

V

L

T

A

Y

V

L

R

K

E

A

R

N

V

T

P

P

-

G

-

I

-

D

V

D

T

V

R

V

L

V

A
|
A

G

V

H

H

Y

C

H

H

D

N

T

D

A

L

G

G

R

L

A

A

I

T

D

A

N

N

I

S

D

I

A

A

S

G

L

I

S

R

L

A

G

G

V

A

R

R

V

Q

F

V

D

E

A

V

A

T

V

I

G

N

G

G

L

I

G

G

A290 (= A203) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

Sites not aligning to the query:

102 S→F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.

Query Sequence

>GFF1017 FitnessBrowser__Phaeo:GFF1017
MSESVEIFEVGPRDGLQNEKRDIPVAEKIALIDRLTDAGFRRIEVASFVSPRWVPQMAGS
GEVLAGIRRNSDVRYAALTPNMRGYEDALTAKADEIAIFASASEGFSKANINASVAESIE
RFTPIIEAARHIDMPVRGYISCVTECPFDGPTDPDAVAALADRLFSMGCYEISLGDTIGQ
ATPDSIARMLLAVRERVPVTRLAGHYHDTAGRAIDNIDASLSLGVRVFDAAVGGLGGCPY
APGAAGNVATEAVHEHLTRLGYETGLKGDVLTDAAAMARAMRG

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