SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_084276501.1 NCBI__GCF_900176045.1:WP_084276501.1 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)

Q9JZG1 2-isopropylmalate synthase; Alpha-IPM synthase; Alpha-isopropylmalate synthase; EC 2.3.3.13 from Neisseria meningitidis serogroup B (strain MC58) (see 2 papers)
58% identity, 96% coverage: 4:497/516 of query aligns to 6:500/517 of Q9JZG1

query
sites
Q9JZG1

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D16 (= D14) binding Mn(2+)
H204 (= H200) binding Mn(2+)
H206 (= H202) binding Mn(2+)
N240 (= N236) binding Mn(2+)

Sites not aligning to the query:

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

3rmjB Crystal structure of truncated alpha-isopropylmalate synthase from neisseria meningitidis (see paper)
65% identity, 61% coverage: 4:320/516 of query aligns to 3:307/308 of 3rmjB

query
sites
3rmjB

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active site: Q16 (= Q17)
binding manganese (ii) ion: D13 (= D14), H201 (= H200), H203 (= H202), N237 (= N236)

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
48% identity, 73% coverage: 2:379/516 of query aligns to 15:408/409 of 6e1jA

query
sites
6e1jA

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T

T

binding coenzyme a: Q30 (= Q17), F60 (= F47), S63 (≠ A50), I95 (≠ L73), R97 (= R75), F121 (= F99), K132 (= K110), L133 (= L111), S322 (= S296), G323 (= G297), I324 (= I298), D327 (= D301), K331 (= K305), L359 (≠ H330), R362 (= R333), H363 (= H334)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (= P169), T194 (= T171), H225 (= H200), H227 (= H202)
binding manganese (ii) ion: D27 (= D14), V82 (vs. gap), E84 (vs. gap), H225 (= H200), H227 (= H202)

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 73% coverage: 5:380/516 of query aligns to 85:476/506 of Q9FG67

query
sites
Q9FG67

V

V

K

R

I

V

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F

D

D

T

T

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L

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G

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P

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S

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K

I

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Q

E

I

I

A

A

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K

L

L

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R

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F

F

A

P

A

G

A

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E

A

T

I

I

R

K

K

T

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N

G

K

N

-

E

-

V

-

D

-

E

-

T

-

G

-

Y

-

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S

P

T

V

V

I

C

C

S

A

L

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A

A

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A

C

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E

H

K

R

D

D

I

I

K

E

A

A

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G

W

E

E

A

A

I

L

A

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P

Y

A

A

K

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F

F

I

T

A

S

T

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D

I

I

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H

M

M

K

K

Y

Y

K

K

L

L

R

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E

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M

A

A

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E

S

A

S

V

I

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R

Y

F

A

A

K

K

T

S

F

L

-

G

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F

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N

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G

C

C

E

E

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D

A

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A

D

F

F

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A

I

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A

A

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G

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T

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I

V

N

T

I

I

P

G

D

D

T

T

V

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Y

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K

-

A

D

N

F

T

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G

-

I

E

D

R

D

A

V

I

V

S
x
A

V

V

H

H

C

C

H

H

N

N

D

D

L

L

G

G

L

L

A

A

V

T

A

A

N

N

S

S

L

I

Y

A

S

G

V

I

L

R

N

A

G

G

A

A

R

R

Q

Q

V

V

E

E

C

V

T

T

I

I

N

N

G

G

L

I

G

G

E

E

R

R

A

S

G

G

N

N

A

A

A

S

L

L

E

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I

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M

A

A

I

L

K

K

T

C

R

R

K

G

D

A

-

Y

I

V

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I

D

N

G

G

I

V

D

Y

T

T

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K

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I

N

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A

T

T

S

S

R

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M

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A

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A

E

I

Y

T

T

G

G

I

L

E

Y

P

V

Q

Q

P

A

N

H

K

K

A

P

I

I

V

V

G

G

K

A

N

N

A

C

F

F

A

V

H

H

E

E

S

S

G

G

I

I

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H

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D

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K

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T

Y

Y

E

E

I

I

M

L

R

S

A

P

E

E

D

D

I

I

G

G

L

I

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-

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-

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D

Q

R

N

N

S

A

G

I

L

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V

L

L

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G

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K

H

L

S

S

G

G

R

R

H

H

A

A

F

V

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D

R

R

I

L

E

K

D

E

L

L

G

G

F

Y

T

E

L

L

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D

E

D

E

E

E

K

I

L

N

N

K

A

A

V

F

F

E

S

R

L

F

F

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D

L

L

A

T

D

K

K

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I

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D

D

A

D

D

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M

A

L

L

I

V

T

T

N

S

S102 (= S22) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ S198) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

Q9FN52 Methylthioalkylmalate synthase 3, chloroplastic; 2-isopropylmalate synthase 2; Methylthioalkylmalate synthase-like; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
48% identity, 74% coverage: 2:384/516 of query aligns to 82:482/503 of Q9FN52

query
sites
Q9FN52

K

K

E

N

Q

Y

V

V

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E

A

A

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A

E

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T

V

V

N

G

K

N

-

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-

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-

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-

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G

-

Y

-

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V

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C

L

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D

I

I

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A

A

A

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G

W

E

E

A

A

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A

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Y

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A

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V

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K

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Y

A

A

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|
G

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A

D

I

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C

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H

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N

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D

L

L

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A

A

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A

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G

A

A

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I

I

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G

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E

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A

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G

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N

A

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A

E

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Q

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K

A

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D

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N

A

C

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F

A

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H

E

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G

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Y

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E

E

D

D

I

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G

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I

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K

-

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A

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N

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-

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S

G263 (= G173) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
38% identity, 70% coverage: 1:360/516 of query aligns to 18:370/399 of 6ktqA

query
sites
6ktqA

M

L

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R

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x
E

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A

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x
V

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R

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R

A
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A

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E

A

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A

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G

A

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I

E

A

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A

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F

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H

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A

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R

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E

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D

A

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A

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Y

A

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F

Y

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V

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A

A

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G

A

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x
S

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A

D

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T

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D

L

L

K

T

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S

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A

E

I

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I

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I

H
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H

C

A

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

V

A

A

N

N

S

V

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Y

A

S

A

V

A

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E

N

G

G

G

A

A

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C

T

T

T

I

L

N

N

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G

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L

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E

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R

A

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G

G

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I

A

A

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I

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V

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M

A

A

A

I

L

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K

T

Y

R

H

K

F

D

-

I

-

F

-

D

-

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G

I

I

D

E

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V

N

-

I

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D

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L

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A

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I

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I

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A

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L

Q

P

P

P

N

N

K

F

A

P

I

I

V

T

G

G

K

D

N

Y

A

A

F

F

A

V

H

H

E

K

S

A

G

G

I

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D

A

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A

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-

I

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L

I

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D

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K

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T

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H

H

A

A

F

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G

F

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K

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A

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F

L

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K

F

I

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K

binding 2-oxoglutaric acid: R30 (= R13), R154 (≠ E137), T156 (≠ S139), E158 (= E141), S184 (≠ N167), T188 (= T171), H216 (= H200), H218 (= H202)
binding coenzyme a: V67 (≠ A50), R96 (= R75), A97 (= A76), F116 (= F99), H128 (≠ L111), E158 (= E141)
binding zinc ion: E31 (≠ D14), H216 (= H200), H218 (= H202)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
35% identity, 72% coverage: 5:377/516 of query aligns to 4:377/379 of 4ov4A

query
sites
4ov4A

V

I

K

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I

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D

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N

T

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D

I

G

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G

-

K

T

P

V

I

C

A

S

A

L

L

A

S

R

R

A

A

L

N

E

Q

K

N

D

E

I

I

K

A

A

V

A

T

G

W

E

E

A

A

I

I

A

Q

P

K

A

A

K

D

F

C

K

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

P

D

I

F

H

S

M

I

K

K

Y

H

K

V

L

L

R

K

M

I

E

S

P

E

E

K

E

E

V

V

I

L

K

Q

R

K

A

I

I

R

E

N

A

S

V

I

K

S

Y

F

A

A

K

R

T

S

F

I

V

V

N

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

C

G

E

E

D

H

A

F

G

G

R

D

S

A

-

I

-

E

E

N

M

F

A

A

F

F

L

T

K

K

E

E

I

A

I

F

A

L

A

T

V

A

I

I

E

E

A

A

G

G

A

A

K

N

T

I

I

I

N

N

I

L

P
|
P

D

N

T
|
T

V

V

G

E

Y

R

R

Y

F

R

P

P

H

M

E

V

M

F

G

V

E

N

M

M

I

V

K

K

E

E

L

I

K

K

D

D

F

V

I

V

G

K

E

D

R

K

A

A

I

I

S

S

V

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

S

S

L

V

Y

E

S

S

V

V

L

Y

N

V

G

G

A

A

R

E

Q

Q

V

I

E

E

C

V

T

A

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

N

L

L

E

Y

E

E

I

T

V

A

M

I

A

A

I

L

K

H

T

Q

R

-

K

-

D

-

I

-

F

-

D

N

G

G

I

E

D

N

T

L

N

N

I

I

N

N

T

F

K

Q

E

R

I

I

Y

Y

P

P

T

T

S

A

R

K

L

R

V

I

A

S

A

E

I

L

T

T

G

G

I

I

E

P

P

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

K

E

N

D

A

I

F

F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

D

-

G

-

V

-

L

-

K

-

H

H

Q

Q

E

S

-

K

-

G

T

A

Y

Y

E

R

I

T

M

F

R

S

A

P

E

E

D

F

I

V

G

G

-

R

L

M

D

D

R

K

N

E

A

T

I

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

H

K

A

A

F

I

K

E

K

F

R

L

I

L

E

H

D

Q

L

R

G

G

F

I

T

Q

L

V

S

S

E

K

E

E

E

G

I

I

N

H

K

H

A

L

F

F

E

S

R

L

F

A

K

K

V

S

L

I

A

S

D

S

K

R

K

E

-

N

K

R

E

E

I

I

T

T

D

E

D

A

D

E

I

L

R

V

M

A

L

L

active site: Q16 (= Q17)
binding 3-methyl-2-oxobutanoic acid: R12 (= R13), P174 (= P169), T176 (= T171), H205 (= H200), H207 (= H202)
binding zinc ion: D13 (= D14), H205 (= H200), H207 (= H202)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
35% identity, 72% coverage: 5:377/516 of query aligns to 4:379/380 of 4ov9A

query
sites
4ov9A

V

I

K

H

I

I

F

Q

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

S

A

P

L

G

K

A

R

S

P

M

W

N

T

T

I

E

D

E

E

K

K

I

I

Q

E

I

V

A

F

K

D

Q

L

L

L

E

V

K

E

L

L

G

N

V

V

D

D

I

G

I

I

E

E

A

V

G

G

F

F

A

P

A

S

S

N

P

E

G

T

D

E

F

F

E

H

A

T

I

C

R

Q

K

V

I

L

S

S

E

K

V

R

V

A

N

P

K

K

S

G

-

K

T

P

V

I

C

A

S

A

L
|
L

A

S

R

R

A

A

L

N

E

Q

K

N

D

E

I

I

K

A

A

V

A

T

G

W

E

E

A

A

I

I

A

Q

P

K

A

A

K

D

F

C

K

P

R

R

I

M

H

H

T

I

F

V

I

Y

A

P

T

V

S

S

P

D

I

F

H

S

M

I

K

K

Y

H

K

V

L

L

R

K

M

I

E

S

P

E

E

K

E

E

V

V

I

L

K

Q

R

K

A

I

I

R

E

N

A

S

V

I

K

S

Y

F

A

A

K

R

T

S

F

I

V

V

N

G

-

P

-

G

-

I

D

E

V

I

E

Q

F

F

S

S

C

G

E

E

D

H

A

F

G

G

R

D

S

A

-

I

-

E

E

N

M

F

A

A

F

F

L

T

K

K

E

E

I

A

I

F

A

L

A

T

V

A

I

I

E

E

A

A

G

G

A

A

K

N

T

I

I

I

N

N

I

L

P

P

D

N

T
|
T

V

V

G

E

Y

R

R

Y

F

R

P

P

H

M

E

V

M

F

G

V

E

N

M

M

I

V

K

K

E

E

L

I

K

K

D

D

F

V

I

V

G

K

E

D

R

K

A

A

I

I

S

S

V

I

H
|
H

C

T

H
|
H

N

N

D

D

L

L

G

G

L

M

A

A

V

T

A

A

N

T

S

S

L

V

Y

E

S

S

V

V

L

Y

N

V

G

G

A

A

R

E

Q

Q

V

I

E

E

C

V

T

A

I

L

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

N

L

L

E

Y

E

E

I

T

V

A

M

I

A

A

I

L

K

H

T

Q

R

-

K

-

D

-

I

-

F

-

D

N

G

G

I

E

D

N

T

L

N

N

I

I

N

N

T

F

K

Q

E

R

I

I

Y

Y

P

P

T

T

S

A

R

K

L

R

V

I

A

S

A

E

I

L

T

T

G

G

I

I

E

P

P

I

Q

G

P

E

N

K

K

T

A

P

I

I

V

I

G

G

K

E

N

D

A

I

F

F

A

S

H

H

E

R

S

S

G

G

I

I

H

H

Q

Q

D

T

G

-

V

L

L

H

K

Q

H

S

Q

K

E

G

T

A

Y

Y

E

R

I

T

M

F

R

S

A

P

E

E

D

F

I

V

G

G

-

R

L

M

D

D

R

K

N

E

A

T

I

I

V

S

L

F

G

T

K

N

H

Q

S

S

G

G

R

H

H

K

A

A

F

I

K

E

K

F

R

L

I

L

E

H

D

Q

L

R

G

G

F

I

T

Q

L

V

S

S

E

K

E

E

E

G

I

I

N

H

K

H

A

L

F

F

E

S

R

L

F

A

K

K

V

S

L

I

A

S

D

S

K

R

K

E

-

N

K

R

E

E

I

I

T

T

D

E

D

A

D

E

I

L

R

V

M

A

L

L

active site: Q16 (= Q17)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R13), L73 (= L73), T176 (= T171), H205 (= H200), H207 (= H202)
binding zinc ion: D13 (= D14), H205 (= H200), H207 (= H202)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
30% identity, 96% coverage: 4:500/516 of query aligns to 7:511/516 of Q8F3Q1

query
sites
Q8F3Q1

Q

R

V

L

K

E

I

I

F

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

S

T

P

R

G

G

A

V

S

S

M

F

N

S

T

T

E

S

E

E

K

K

I

L

Q

N

I

I

A

A

K

K

-

F

Q

L

L

L

E

Q

K

K

L

L

G

N

V

V

D

D

I

R

I

V

E

E

A

I

G

A

F

S

A

A

A

R

A

V

S

S

P

K

G

G

D

E

F

L

E

E

A

T

I

V

R

Q

K

K

I

I

S

M

E

E

V

W

V

A

N

A

K

T

S

E

T

Q

V

L

C

T

S

E

L

R

A

I

R

E

A

I

L
|
L

E

G

-
x
F

K

V

D

D

I

G

K

N

A

K

A

T

G

V

E

D

A

W

I

I

A

K

P

D

A

S

K

G

F

A

K

K

R

V

I

L

H

N

T

L

F
x
L

I

T

A

K

T

G

S

S

P

L

I

H

H

H

M

L

K

E

Y

K

K

Q

L

L

R

G

M

K

E

T

P

P

E

K

E

E

V

F

I

F

K

T

R

D

A

V

I

S

E

F

A

V

V

I

K

E

Y

Y

A

A

K

I

T

K

F

S

V

G

N

L

D

K

V

I

E

N

F

V

S
x
Y

C

L

E
|
E

D

D

A

W

G

S

-

N

-

G

-

F

R

R

S

N

E

S

M

P

A

D

F

Y

L

V

K

K

E

S

I

L

I

V

A

E

A

H

V

L

I

S

E

K

A

E

G

H

A

I

K

E

T

R

I

I

N

F

I

L

P

P

D

D

T
|
T

V

L

G

G

Y

V

R

L

F

S

P

P

H

E

E

E

-

T

-

F

-

Q

-

G

M

V

G

D

E

S

M

L

I

I

K

Q

E

K

L

Y

K

P

D

D

F

I

I

H

G

F

E

E

R

-

A

-

I

-

S

-

V

F

H

H

C

G

H

H

N

N

D

D

L

Y

G

D

L

L

A

S

V

V

A

A

N

N

S

S

L

L

Y

Q

S

A

V

I

L

R

N

A

G

G

A

V

R

K

Q

G

V

L

E

H

C

A

T

S

I

I

N

N

G

G

L

L

G

G

E

E

R

R

A

A

G

G

N

N

A

T

A

P

L

L

E

E

E

A

I

L

V

V

M

T

A

T

I

I

K

H

T

D

R

K

K

S

D

N

I

-

F

-

D

-

G

-

I

S

D

K

T

T

N

N

I

I

N

N

T

E

K

I

E

A

I

I

Y

T

P

E

T

A

S

S

R

R

L

L

V

V

A

E

A

V

I

F

T

S

G

G

I

K

E

R

P

I

Q

S

P

A

N

N

K

R

A

P

I

I

V

V

G

G

K

E

N

D

A

V

F

F

A

T

H

Q

E

T

S

A

G

G

I

V

H
|
H

Q

A

D
|
D

G

G

V

D

L

K

K

K

H

G

Q
x
N

E
x
L

T
x
Y

Y

A

E

N

I

P

M

I

R

L

A

P

E

E

D

R

I

F

G

G

L

R

D

K

R

R

N

-

A

S

I

Y

V

A

L

L

G

G

K

K

H

L

S

A

G

G

R

K

H

A

A

S

F

I

K

S

K

E

R

N

I

V

E

K

D

Q

L

L

G

G

F

M

T

V

L

L

S

S

E

E

E

V

I

L

N

Q

K

K

A

V

F

L

E

E

R

R

F

V

K

I

V

E

L

L

A

G

D

D

K

Q

K

N

K

K

E

L

I

V

T

T

D

P

D

E

D

D

I

L

R

P

M

F

L

I

I

I

T

A

N

D

E

V

I

S

A

G

S

R

A

T

P

G

E

E

V

-

Y

-

K

-

L

-

K

K

K

V

L

L

Q

T

I

I

S

K

D

S

C

C

S

N

-

I

-

H

E

S

G

G

V

I

-

G

-

I

-

R

P

P

S

H

A

A

A

Q

V

I

T

E

I

L

E

E

F

Y

D

Q

G

G

K

K

E

I

I

H

T

K

D

E

A

I

G

S

I

E

G

G

D

D

G

G

T

G

I
x
Y

D
|
D

A

A

I

F

F

M

K

N

T

A

I

L

D

T

R

K

I

I

S

T

G

N

Y

R

K

L

G

G

T

I

-

S

-

I

-

P

-

K

L
|
L

N

I

D

D

Y
|
Y

Q

E

V

V

A

R

A
x
I

V

P

S

P

K

G

G

G

K

K

-
x
T

D

D

A

A

L

L

A
x
V

K

E

V

T

V

R

V

I

-

T

-

W

-

N

K

K

V

S

V

L

F

D

D

L

E

E

K

E

K

D

P

Q

A

T

V

F

I

K

G

T

H

M

G

G

L

V

S

H

I
x
P

D

D

T
x
Q

M

T

I

V

A

A

S

A

A

V

K

H

A

A

Y

T

V

E

S

K

A

M

L

L

N

N

S

Q

Y

I

I

L

R16 (= R13) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 13:14) binding pyruvate
D17 (= D14) mutation to A: 34-fold increase in Km for pyruvate and 315-fold decrease in kcat.; mutation to N: 4.4-fold increase in Km for pyruvate and 480-fold decrease in kcat.
L81 (= L77) mutation to A: 4.7-fold increase in Km for pyruvate and 15.7-fold decrease in kcat.; mutation to V: 3.3-fold increase in Km for pyruvate and 10.1-fold decrease in kcat.
F83 (vs. gap) mutation to A: 5-fold increase in Km for acetyl-CoA and 120-fold decrease in kcat.
L104 (≠ F99) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ S139) binding pyruvate; mutation to L: 259-fold increase in Km for pyruvate and 76-fold decrease in kcat.; mutation to V: 114-fold increase in Km for pyruvate and 5.3-fold decrease in kcat.
E146 (= E141) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T171) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.
H302 (= H299) mutation H->A,N: Loss of activity.
D304 (= D301) mutation to A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
N310 (≠ Q307) mutation to A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
L311 (≠ E308) mutation to A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
Y312 (≠ T309) mutation to A: Loss of activity.
Y430 (≠ I427) mutation to L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
D431 (= D428) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
L451 (= L444) mutation to V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
Y454 (= Y447) mutation to A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
I458 (≠ A451) mutation to A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
T464 (vs. gap) mutation to A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
V468 (≠ A460) mutation to A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
P493 (≠ I482) mutation to A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
Q495 (≠ T484) mutation to A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
32% identity, 72% coverage: 7:377/516 of query aligns to 37:399/418 of Q9Y823

query
sites
Q9Y823

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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 (≠ L73) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H97) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ E137) 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 (= S139) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E141) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T171) 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 (≠ S198) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H200) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H202) binding 2-oxoglutarate; binding Zn(2+)
R288 (≠ Y266) mutation to K: Does not affect the catalytic activity but impairs L-lysine inhibition.
Y332 (= Y310) mutation to A: Abolishes the catalytic activity.; mutation to F: Results in a decrease in catalytic efficiency.
Q364 (≠ D342) mutation to R: Does not affect the catalytic activity but impairs L-lysine inhibition.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
32% identity, 72% coverage: 7:377/516 of query aligns to 32:394/400 of 3ivtB

query
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3ivtB

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