SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_013843393.1 NCBI__GCF_000215085.1:WP_013843393.1 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)

6ktqA Crystal structure of catalytic domain of homocitrate synthase from sulfolobus acidocaldarius (sahcs(dram)) in complex with alpha- ketoglutarate/zn2+/coa (see paper)
36% identity, 93% coverage: 3:269/288 of query aligns to 21:297/399 of 6ktqA

query
sites
6ktqA

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binding 2-oxoglutaric acid: R30 (= R12), R154 (≠ T132), T156 (≠ G134), E158 (= E136), S184 (≠ R162), T188 (= T166), H216 (= H193), H218 (= H195)
binding coenzyme a: V67 (≠ M49), R96 (= R74), A97 (≠ T75), F116 (≠ S94), H128 (≠ L106), E158 (= E136)
binding zinc ion: E31 (≠ D13), H216 (= H193), H218 (= H195)

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)
34% identity, 94% coverage: 2:273/288 of query aligns to 5:287/517 of Q9JZG1

query
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Q9JZG1

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D16 (= D13) binding Mn(2+)
H204 (= H193) binding Mn(2+)
H206 (= H195) binding Mn(2+)
N240 (= N229) 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)
34% identity, 94% coverage: 2:273/288 of query aligns to 2:284/308 of 3rmjB

query
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3rmjB

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active site: Q16 (= Q16)
binding manganese (ii) ion: D13 (= D13), H201 (= H193), H203 (= H195), N237 (= N229)

6e1jA Crystal structure of methylthioalkylmalate synthase (bjumam1.1) from brassica juncea (see paper)
37% identity, 81% coverage: 8:240/288 of query aligns to 22:272/409 of 6e1jA

query
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6e1jA

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binding coenzyme a: Q30 (= Q16), F60 (≠ I46), S63 (≠ M49), I95 (≠ W72), R97 (= R74), F121 (≠ S94), K132 (= K105), L133 (= L106)
binding 4-(methylsulfanyl)-2-oxobutanoic acid: P192 (≠ A164), T194 (= T166), H225 (= H193), H227 (= H195)
binding manganese (ii) ion: D27 (= D13), V82 (vs. gap), E84 (vs. gap), H225 (= H193), H227 (= H195)

Sites not aligning to the query:

binding coenzyme a: 322, 323, 324, 327, 331, 359, 362, 363

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)
36% identity, 81% coverage: 7:240/288 of query aligns to 88:339/503 of Q9FN52

query
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Q9FN52

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N

R

L

V

H

M

I

L

S

F

A

T

P

S

V

T

S

S

D

E

I

I

H

H

I

M

R

K

Y

Y

K

K

L

L

N

K

R

K

S

T

R

K

E

E

W

E

V

V

L

I

D

E

C

M

M

A

K

V

R

N

A

S

V

V

A

K

Y

Y

A

A

R

K

D

S

A

L

G

G

-

F

A

K

T

D

V

I

T

Q

V

F

G

G

A

C

E

E

D

D

A

G

S

G

R

R

A

T

D

E

M

K

E

D

F

F

L

I

L

C

Q

K

F

I

A

L

R

G

E

E

A

S

K

I

K

K

E

A

G

G

A

A

V

T

Y

T

L

V

R

G

F

F

A

A

D

D

T

T

L

V

G
|
G

V

I

M

N

D

M

P

P

F

Q

T

E

T

F

R

G

N

E

R

L

V

V

E

A

Q

Y

I

V

I

I

R

E

R

N

T

T

-

P

G

G

I

A

D

D

-

D

-

I

-

V

V

F

E

A

M

I

H

H

G

C

H

H

N

N

D

D

F

L

G

G

M

V

A

A

T

T

A

A

N

N

S

T

L

I

A

S

A

G

Y

I

K

C

A

A

G

G

A

A

R

R

Y

Q

L

V

S

E

T

V

T

T

V

I

L

N

G

G

M

I

G

G

E

E

R

R

A

S

G

G

N

N

S

A

P

P

Y

L

E

E

V

V

E

M

M

A

L

L

R

K

G263 (= G168) mutation to E: In gsm2-1; loss of activity and lack of C6, C7 and C8 aliphatic glucosinolates.

P0DO78 Methylthioalkylmalate synthase 1-2, chloroplastic; EjMAM1-2; EC 2.3.3.17 from Eutrema japonicum (Wasabi plant) (Eutrema wasabi) (see paper)
36% identity, 81% coverage: 8:240/288 of query aligns to 89:339/503 of P0DO78

query
sites
P0DO78

D

D

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

S

A

V

P

G

G

V

G

A

A

F

L

S

T

A

P

K

P

E

Q

K

K

V

L

H

E

I

I

A

A

G

R

L

K

L

L

D

A

A

K

V

L

G

R

V

V

Y

D

Q

V

I

M

E

E

A

V

G

G

I

F

P

P

A

G

M

S

G

S

Q

E

L

E

E

E

M

F

E

E

A

T

I

V

Y

K

S

T

I

I

L

A

A

K

L

T

-

V

-

G

-

N

-

E

-

V

-

D

-

E

-

T

N

G

L

Y

K

I

A

P

K

V

I

I

S

C

T

A

W

I

N

A

R

R

T

S

N

K

L

Q

D

R

D

D

I

I

K

E

A

A

S

A

L

W

D

E

C

A

-

V

-

K

-

Y

-

A

G

K

A

R

R

P

N

K

L

I

H

L

I

I

S

F

A

T

P

S

V

T

S

S

D

D

I

I

H

H

I

M

R

K

Y

Y

K

K

L

L

N

K

R

K

S

T

R

K

E

E

W

E

V

V

L

I

D

E

C

M

M

A

K

T

R

S

A

S

V

I

A

R

Y

F

A

A

R

K

D

S

A

L

G

G

-

F

A

I

T

D

V

V

T

Q

V

L

G

G

A

C

E

E

D

D

A

G

S

G

R

R

A

S

D

E

M

K

E

E

F

F

L

L

L

C

Q

K

F

I

A

L

R

G

E

E

A

A

K

I

K

K

E

A

G

G

A

A

V

T

Y

A

L

V

R

N

F

V

A

A

D

D

T

T

L

V

G

G

V

I

M

N

D

M

P

P

F

E

T

E

T

Y

R

G

N

E

R

L

V

V

E

R

Q

Y

I

L

I

K

R

A

R

N

T

T

-

P

G

G

I

I

D

D

-

D

-

I

-

V

V

F

E

S

M

V

H
|
H

G

C

H
|
H

N

N

D

D

F

L

G

G

M

V

A

A

T

T

A

A

N

N

S

T

L

I

A

A

A

G

Y

V

K

C

A

A

G

G

A

A

R

R

Y

Q

L

V

S

E

T

V

T

T

V

V

L

N

G

G

M

I

G

G

E

E

R

R

A

S

G

G

N

N

S

A

P

P

Y

L

E

E

V

V

E

M

M

A

L

L

R

K

R93 (= R12) mutation to A: Lost catalytic activity.
D94 (= D13) mutation to A: Lost catalytic activity.
H292 (= H193) mutation to A: Lost catalytic activity.
H294 (= H195) mutation to A: Lost catalytic activity.

Sites not aligning to the query:

392 H→A: Lost catalytic activity.

Q9FG67 Methylthioalkylmalate synthase 1, chloroplastic; 2-isopropylmalate synthase 3; EC 2.3.3.17 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 81% coverage: 8:240/288 of query aligns to 89:339/506 of Q9FG67

query
sites
Q9FG67

D

D

T

T

L

L

R

R

D

D

G

G

E

E

Q

Q

S

S

V

P

G

G

V

G

A
x
S

F

L

S

T

A

P

K

P

E

Q

K

K

V

L

H

E

I

I

A

A

G

R

L

Q

L

L

D

A

A

K

V

L

G

R

V

V

Y

D

Q

I

I

M

E

E

A

V

G

G

I

F

P

P

A

G

M

S

G

S

Q

E

L

E

E

E

M

L

E

E

A

T

I

I

Y

K

S

T

I

I

L

A

A

K

L

T

-

V

-

G

-

N

-

E

-

V

-

D

-

E

-

T

N

G

L

Y

K

V

A

P

K

V

I

I

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C

T

A

W

I

N

A

R

R

T

C

N

K

L

H

D

R

D

D

I

I

K

E

A

A

S

T

-

W

-

E

-

A

L

L

D

K

C

Y

G

A

A

K

R

R

-

P

N

R

L

I

H

L

I

V

S

F

A

T

P

S

V

T

S

S

D

D

I

I

H

H

I

M

R

K

Y

Y

K

K

L

L

N

K

R

K

S

T

R

Q

E

E

W

E

V

V

L

I

D

E

C

M

M

A

K

V

R

S

A

S

V

I

A

R

Y

F

A

A

R

K

D

S

A

L

G

G

A

F

T

N

-

D

V

I

T

Q

V

F

G

G

A

C

E

E

D

D

A

G

S

G

R

R

A

S

D

D

M

K

E

D

F

F

L

L

L

C

Q

K

F

I

A

L

R

G

E

E

A

A

K

I

K

K

E

A

G

G

A

V

V

T

Y

V

L

V

R

T

F

I

A

G

D

D

T

T

L

V

G

G

V

I

M

N

D

M

P

P

F

H

T

E

T

Y

R

G

N

E

R

L

V

V

E

T

Q

Y

I

L

I

K

R

A

R

N

T

T

-

P

G

G

I

I

D

D

-

D

-

V

V

V

E
x
A

M

V

H

H

G

C

H

H

N

N

D

D

F

L

G

G

M

L

A

A

T

T

A

A

N

N

S

S

L

I

A

A

A

G

Y

I

K

R

A

A

G

G

A

A

R

R

Y

Q

L

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S

E

T

V

T

T

V

I

L

N

G

G

M

I

G

G

E

E

R

R

A

S

G

G

N

N

S

A

P

S

Y

L

E

E

V

V

E

M

M

A

L

L

R

K

S102 (≠ A21) mutation to F: In gsm1-1; loss of conversion of C3 to C4 glucosinolates.
A290 (≠ E191) mutation to T: In gsm1-2; loss of conversion of C3 to C4 glucosinolates.

3ivtB Homocitrate synthase lys4 bound to 2-og (see paper)
31% identity, 78% coverage: 6:231/288 of query aligns to 32:257/400 of 3ivtB

query
sites
3ivtB

F

I

V

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

V

A

G

N

V

A

A

F

F

F

S

D

A

T

K

E

E

K

K

K

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I

H

Q

I

I

A

A

G

K

L

A

L

L

D

D

A

N

V

F

G

G

V

V

Y

D

Q

Y

I

I

E

E

A

L

G

T

I

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P

P

A

V

M

A

G

S

Q

E

L

Q

E

S

M

R

E

Q

A

D

I

C

Y

E

S

A

I

I

L

C

A

K

L

L

N

G

L

L

K

K

A

C

K

K

I

I

S

L

T

T

W
x
H

N

I

R

R

T

C

N

H

L

M

D

D

I

A

K

R

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

D

N

G

L

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V

A

I

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G

V

T

S

S

D

Q

I

Y

H

L

I

R

R

K

Y

Y

K

S

L

H

N

G

R

K

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D

R

M

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W

Y

V

I

L

I

D

D

C

S

M

A

K

T

R

E

A

V

V

I

A

N

Y

F

A

V

R

K

D

S

A

K

G

G

A

I

T

E

V

V

T
x
R

V

F

G
x
S

A

S

E

E

D

D

A

S

S

F

R

R

A

S

D

D

M

L

E

V

F

D

L

L

Q

S

F

L

A

Y

R

K

E

A

A

V

K

D

K

K

E

I

G

G

A

V

V

N

Y

R

L

V

R

G

F

I

A

A

D

D

T
|
T

L

V

G

G

V

C

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

D

R

L

V

I

E

R

Q

T

I

L

I

R

R

G

R

V

T

V

G

S

I

C

D

D

V

I

E

E

M

C

H
|
H

G

F

H
|
H

N

N

D

D

F

T

G

G

M

M

A

A

T

I

A

A

N

N

S

A

L

Y

A

C

A

A

Y

L

K

E

A

A

G

G

A

A

R

T

Y

H

L

I

S

D

T

T

T

S

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

active site: Q42 (= Q16)
binding 2-oxoglutaric acid: R38 (= R12), H98 (≠ W72), R158 (≠ T132), S160 (≠ G134), T192 (= T166), H219 (= H193), H221 (= H195)
binding zinc ion: E39 (≠ D13), H219 (= H193), H221 (= H195)

Q9Y823 Homocitrate synthase, mitochondrial; HCS; EC 2.3.3.14 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see 2 papers)
31% identity, 78% coverage: 6:231/288 of query aligns to 37:262/418 of Q9Y823

query
sites
Q9Y823

F

I

V

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

V

A

G

N

V

A

A

F

F

F

S

D

A

T

K

E

E

K

K

K

V

I

H

Q

I

I

A

A

G

K

L

A

L

L

D

D

A

N

V

F

G

G

V

V

Y

D

Q

Y

I

I

E
|
E

A

L

G

T

I

S

P

P

A

V

M

A

G

S

Q

E

L

Q

E

S

M

R

E

Q

A

D

I

C

Y

E

S

A

I

I

L

C

A

K

L

L

N

G

L

L

K

K

A

C

K

K

I

I

S

L

T

T

W
x
H

N

I

R

R

T

C

N

H

L

M

D

D

I

A

K

R

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

D

N

G

L

V

H
x
D

I

V

S

V

A

I

P

G

V

T

S

S

D

Q

I

Y

H

L

I

R

R

K

Y

Y

K

S

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H

N

G

R

K

S

D

R

M

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T

W

Y

V

I

L

I

D

D

C

S

M

A

K

T

R

E

A

V

V

I

A

N

Y

F

A

V

R

K

D

S

A

K

G

G

A

I

T

E

V

V

T
x
R

V

F

G
x
S

A

S

E
|
E

D

D

A

S

S

F

R

R

A

S

D

D

M

L

E

V

F

D

L

L

Q

S

F

L

A

Y

R

K

E

A

A

V

K

D

K

K

E

I

G

G

A

V

V

N

Y

R

L

V

R

G

F

I

A

A

D

D

T
|
T

L

V

G

G

V

C

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

D

R

L

V

I

E

R

Q

T

I

L

I

R

R

G

R

V

T

V

G

S

I

C

D

D

V

I

E
|
E

M

C

H
|
H

G

F

H
|
H

N

N

D

D

F

T

G

G

M

M

A

A

T

I

A

A

N

N

S

A

L

Y

A

C

A

A

Y

L

K

E

A

A

G

G

A

A

R

T

Y

H

L

I

S

D

T

T

T

S

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

R43 (= R12) binding 2-oxoglutarate; mutation R->A,K,Q: Abolishes the catalytic activity.
E44 (≠ D13) binding 2-oxoglutarate; binding L-lysine; binding Zn(2+)
Q47 (= Q16) mutation to A: Abolishes the catalytic activity.
E74 (= E43) 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 (≠ W72) binding 2-oxoglutarate; mutation to A: Substantially impairs catalytic efficiency.
D123 (≠ H92) binding L-lysine; mutation to N: Does not affect the catalytic activity but impairs L-lysine inhibition.
R163 (≠ T132) 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 (≠ G134) binding 2-oxoglutarate; mutation to A: Results in a moderate decrease in catalytic efficiency.
E167 (= E136) mutation E->A,Q: Abolishes the catalytic activity.
T197 (= T166) 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 (= E191) mutation to Q: Does not affect the catalytic activity but impairs L-lysine inhibition.
H224 (= H193) binding 2-oxoglutarate; binding Zn(2+)
H226 (= H195) 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.

3mi3A Homocitrate synthase lys4 bound to lysine (see paper)
30% identity, 90% coverage: 6:264/288 of query aligns to 14:263/370 of 3mi3A

query
sites
3mi3A

F

I

V

I

D

E

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

V

A

G

N

V

A

A

F

F

F

S

D

A

T

K

E

E

K

K

K

V

I

H

Q

I

I

A

A

G

K

L

A

L

L

D

D

A

N

V

F

G

G

V

V

Y

D

Q

Y

I

I

E

E

A

L

G

T

I

S

P

P

A

V

M

A

G

S

Q

E

L

Q

E

S

M

R

E

Q

A

D

I

C

Y

E

S

A

I

I

L

C

A

K

L

L

N

G

L

L

K

K

A

C

K

K

I

I

S

L

T

T

W

H

N

I

R

R

T

C

N

H

L

M

D

D

I

A

K

R

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

D

N

G

L

V

H
x
D

I

V

S

V

A

-

P

-

V

-

S

-

D

-

I

-

H

-

I

-

R

-

Y

-

K

-

L

I

N

G

R

T

S

S

R

M

E

T

W

Y

V

I

L

I

D

D

C

S

M

A

K

T

R

E

A

V

V

I

A

N

Y

F

A

V

R

K

D

S

A

K

G

G

A

I

T

E

V

V

T

R

V

F

G

S

A

S

E

E

D

D

A

S

S

F

R

R

A

S

D

D

M

L

E

V

F

D

L

L

Q

S

F

L

A

Y

R

K

E

A

A

V

K

D

K

K

E

I

G

G

A

V

V

N

Y

R

L

V

R

G

F

I

A

A

D

D

T
|
T

L

V

G

G

V

C

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

D

R

L

V

I

E

R

Q

T

I

L

I

R

R

G

R

V

T

V

G

S

I

C

D

D

V

I

E

E

M

C

H
|
H

G

F

H
|
H

N

N

D

D

F

T

G

G

M

M

A

A

T

I

A

A

N

N

S

A

L

Y

A

C

A

A

Y

L

K

E

A

A

G

G

A

A

R

T

Y

H

L

I

S

D

T

T

T

S

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

Y

L

E

G

E

A

V

L

E

A

M

R

L

M

R

-

Y

Y

V

V

-

T

-

D

-

R

E

E

G

Y

I

I

P

T

L

H

P

K

V

Y

N

K

E

L

T

N

K

Q

L

L

E

R

E

E

L

L

I

E

R

N

F

L

V

V

A

A

G

D

A

A

active site: Q24 (= Q16)
binding lysine: R20 (= R12), D100 (≠ H92), T163 (= T166), H190 (= H193), H192 (= H195)
binding zinc ion: E21 (≠ D13), H190 (= H193), H192 (= H195)

O87198 Homocitrate synthase; HCS; EC 2.3.3.14 from Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27) (see paper)
35% identity, 78% coverage: 6:231/288 of query aligns to 6:233/376 of O87198

query
sites
O87198

F

I

V

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

S

F

V

E

G

K

V

A

A

N

F

F

S

S

A

T

K

Q

E

D

K

K

V

V

H

E

I

I

A

A

G

K

L

A

L

L

D

D

A

E

V

F

G

G

V

I

Y

E

Q

Y

I

I

E

E

A

V

G

T

I

T

P

P

A

V

M

A

G

S

Q

P

L

Q

E

S

M

R

E

K

A

D

I

A

Y

E

S

V

I

L

L

A

A

S

L

L

N

G

L

L

K

K

A

A

K

K

I

V

S

V

T

T

W
x
H

N

I

R

Q

T

C

N

R

L

L

D

D

D

A

I

A

K

K

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

Q

N

G

L

I

H
x
D

I

L

S

L

A

F

P

G

V

T

S

S

D

K

I

-

H

Y

I

L

R

R

Y

A

K

A

L

H

N

G

R

R

S

D

R

I

E

P

W

R

V

I

L

I

D

E

C

E

M

A

K

K

R

E

A

V

V

I

A

A

Y

Y

A

I

R

R

D

E

A

A

G

A

A

P

T

H

V

V

T

E

V

V

-
x
R

-

F

G
x
S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

M

E

E

Q

F

D

L

L

Q

A

F

-

A

V

R

Y

E

E

A

A

K

V

K

A

E

P

G

Y

A

V

V

D

Y

R

L

V

R

G

F

L

A

A

D

D

T
|
T

L

V

G

G

V

V

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

A

R

L

V

V

E

R

Q

E

I

V

I

R

R

R

R

V

T

V

G

G

-

P

-

R

I

V

D

D

V

I

E

E

M

F

H
|
H

G

G

H
|
H

N

N

D

D

F

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

Y

I

K

E

A

A

G

G

A

A

R

T

Y

H

L

V

S

D

T

T

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

R12 (= R12) binding 2-oxoglutarate
E13 (≠ D13) binding Mg(2+)
H72 (≠ W72) 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 (≠ H92) binding L-lysine
R133 (vs. gap) binding 2-oxoglutarate
S135 (≠ G134) binding L-lysine
T166 (= T166) binding 2-oxoglutarate; binding L-lysine
H195 (= H193) binding Mg(2+)
H197 (= H195) binding Mg(2+)

Q8F3Q1 (R)-citramalate synthase CimA; LiCMS; EC 2.3.3.21 from Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601) (see 2 papers)
32% identity, 90% coverage: 3:261/288 of query aligns to 7:275/516 of Q8F3Q1

query
sites
Q8F3Q1

K

R

I

L

L

E

F

I

V

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q

Q

S

T

V

R

G

G

V

V

A

S

F

F

S

S

A

T

K

S

E

E

K

K

V

L

H

N

I

I

A

A

G

K

-

F

L

L

D

Q

A

K

V

L

G

N

V

V

Y

D

Q

R

I

V

E

E

A

I

G

A

I

S

P

A

A

R

M

V

G

S

Q

K

L

G

E

E

M

L

E

E

A

T

I

V

Y

Q

S

K

I

I

L

M

A

E

L

W

-

A

-

T

-

E

N

Q

L

L

K

T

A

E

K

R

I

I

S

E

T

I

W
x
L

-

G

-
x
F

-

V

-

D

-

G

N

N

R

K

T

T

N

-

L

V

D

D

D

W

I

I

K

K

A

-

S

-

L

-

D

D

C

S

G

G

A

A

R

K

N

V

L

L

H

N

I

L

S
x
L

A

T

P

K

V

G

S

S

D

L

I

H

H

H

I

L

R

E

Y

K

K

Q

L

L

N

G

R

K

S

T

R

P

E

K

W

E

V

F

L

F

D

T

C

D

M

V

K

S

R

F

A

V

V

I

A

E

Y

Y

A

A

R

I

D

K

A

S

G

G

A

L

T

K

V

I

T

N

V

V

G
x
Y

A

L

E
|
E

D

D

A

W

S

S

-

N

-

G

-

F

R

R

A

N

D

S

M

P

E

D

F

Y

L

V

L

K

Q

S

F

L

A

V

R

E

E

H

A

L

K

S

K

K

E

E

G

H

A

I

V

E

Y

R

L

I

R

F

F

L

A

P

D

D

T
|
T

L

L

G

G

V

V

M

L

D

S

P

P

F

E

T

E

T

T

R

F

N

Q

R

G

V

V

E

D

Q

S

I

L

I

I

R

Q

R

K

-

Y

T

P

G

D

I

I

D

H

V

F

E

E

M

F

H

H

G

G

H

H

N

N

D

D

F

Y

G

D

M

L

A

S

T

V

A

A

N

N

S

S

L

L

A

Q

A

A

Y

I

K

R

A

A

G

G

A

V

R

K

Y

G

L

L

S

H

T

A

T

S

V

I

L

N

G

G

M

L

G

G

E

E

R

R

A

A

G

G

N

N

S

T

P

P

Y

L

E

E

E

A

V

L

V

V

E

T

M

T

L

I

R

H

Y

D

V

K

E

S

G

N

I

S

P

K

L

T

P

N

V

I

N

N

E

E

T

I

K

A

L

I

E

T

E

E

L

A

I

S

R

R

F

L

V

V

R16 (= R12) mutation R->K,Q: Loss of activity.
RD 16:17 (= RD 12:13) binding pyruvate
D17 (= D13) 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 (≠ W72) 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 (≠ S94) mutation to V: 1.8-fold increase in Km for pyruvate and 3.4-fold decrease in kcat.
Y144 (≠ G134) 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 (= E136) mutation E->D,Q: Minor effects on the binding of acetyl-CoA, but causes a strong decrease in kcat.
T179 (= T166) binding pyruvate; mutation to A: 16.4-fold increase in Km for pyruvate and 186-fold decrease in kcat.

Sites not aligning to the query:

302 mutation H->A,N: Loss of activity.
304 D→A: 5.2-fold increase in Km for acetyl-CoA and 16.6-fold decrease in kcat.
310 N→A: 2.2-fold increase in Km for acetyl-CoA and 1.7-fold decrease in kcat.
311 L→A: 8-fold increase in Km for acetyl-CoA and 6-fold decrease in kcat.
312 Y→A: Loss of activity.
430 Y→L: No change in Km for acetyl-CoA and 2.3-fold decrease in kcat. Severely impairs inhibition by isoleucine.
431 D→A: 1.8-fold decrease in Km for acetyl-CoA and 5-fold decrease in kcat.
451 L→V: 1.5-fold increase in Km for acetyl-CoA and 4.3 decrease in kcat.
454 Y→A: 1.4 decrease in Km for acetyl-CoA and 17-fold decrease in kcat. Still inhibited by isoleucine and weakly inhibited by leucine.
458 I→A: 1.3-fold decrease in Km for acetyl-CoA and 14-fold decrease in kcat. Abolishes inhibition by isoleucine.
464 T→A: 1.8-fold decrease in Km for acetyl-CoA and 4.3-fold decrease in kcat.
468 V→A: No change in Km for acetyl-CoA and 2-fold decrease in kcat. Increases inhibition by isoleucine and leucine becomes an effective inhibitor.
493 P→A: 1.5-fold decrease in Km for acetyl-CoA and 2.6-fold decrease in kcat.
495 Q→A: 1.6-fold decrease in Km for acetyl-CoA and 2.8-fold decrease in kcat.

3bliA Crystal structure of the catalytic domain of licms in complexed with pyruvate and acetyl-coa (see paper)
32% identity, 90% coverage: 3:261/288 of query aligns to 1:269/311 of 3bliA

query
sites
3bliA

K

R

I

L

L

E

F

I

V

L

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

E

Q
|
Q

S

T

V

R

G

G

V

V

A

S

F

F

S

S

A

T

K

S

E

E

K

K

V

L

H

N

I

I

A

A

G

K

-

F

L

L

D

Q

A

K

V

L

G

N

V

V

Y

D

Q

R

I

V

E

E

A

I

G

A

I

S

P

A

A
x
R

M
x
V

G

S

Q

K

L

G

E

E

M

L

E

E

A

T

I

V

Y

Q

S

K

I

I

L

M

A

E

L

W

-

A

-

T

-

E

N

Q

L

L

K

T

A

E

K

R

I

I

S

E

T

I

W

L

-

G

-

F

-

V

-

D

-

G

N

N

R

K

T

T

N

-

L

V

D

D

D

W

I

I

K

K

A

-

S

-

L

-

D

D

C

S

G

G

A

A

R

K

N

V

L

L

H

N

I

L

S

L

A

T

P

K

V

G

S

S

D

L

I

H

H

H

I

L

R

E

Y

K

K

Q

L

L

N

G

R

K

S

T

R

P

E

K

W

E

V

F

L

F

D

T

C

D

M

V

K

S

R

F

A

V

V

I

A

E

Y

Y

A

A

R

I

D

K

A

S

G

G

A

L

T

K

V

I

T

N

V

V

G
x
Y

A

L

E
|
E

D

D

A

W

S

S

-

N

-

G

-

F

R

R

A

N

D

S

M

P

E

D

F

Y

L

V

L

K

Q

S

F

L

A

V

R

E

E

H

A

L

K

S

K

K

E

E

G

H

A

I

V

E

Y

R

L

I

R

F

F

L

A
x
P

D

D

T
|
T

L

L

G

G

V

V

M

L

D

S

P

P

F

E

T

E

T

T

R

F

N

Q

R

G

V

V

E

D

Q

S

I

L

I

I

R

Q

R

K

-

Y

T

P

G

D

I

I

D

H

V

F

E

E

M

F

H
|
H

G

G

H
|
H

N

N

D

D

F

Y

G

D

M

L

A

S

T

V

A

A

N

N

S

S

L

L

A

Q

A

A

Y

I

K

R

A

A

G

G

A

V

R

K

Y

G

L

L

S

H

T

A

T

S

V

I

L

N

G

G

M

L

G

G

E

E

R

R

A

A

G

G

N

N

S

T

P

P

Y

L

E

E

E

A

V

L

V

V

E

T

M

T

L

I

R

H

Y

D

V

K

E

S

G

N

I

S

P

K

L

T

P

N

V

I

N

N

E

E

T

I

K

A

L

I

E

T

E

E

L

A

I

S

R

R

F

L

V

V

active site: Q14 (= Q16)
binding acetyl coenzyme *a: Q14 (= Q16), R47 (≠ A48), V48 (≠ M49), E140 (= E136)
binding pyruvic acid: R10 (= R12), Y138 (≠ G134), P171 (≠ A164), T173 (= T166)
binding zinc ion: D11 (= D13), H201 (= H193), H203 (= H195)

3ivsA Homocitrate synthase lys4 (see paper)
30% identity, 78% coverage: 6:231/288 of query aligns to 14:226/364 of 3ivsA

query
sites
3ivsA

F

I

V

I

D

E

T

S

T

T

L

L

R

R

D
x
E

G

G

E

E

Q
|
Q

S

F

V

A

G

N

V

A

A

F

F

F

S

D

A

T

K

E

E

K

K

K

V

I

H

Q

I

I

A

A

G

K

L

A

L

L

D

D

A

N

V

F

G

G

V

V

Y

D

Q

Y

I

I

E

E

A

L

G

T

I

S

P

P

A

V

M

A

G

S

Q

E

L

Q

E

S

M

R

E

Q

A

D

I

C

Y

E

S

A

I

I

L

C

A

K

L

L

N

G

L

L

K

K

A

C

K

K

I

I

S

L

T

T

W

H

N

I

R

R

T

C

N

H

L

M

D

D

I

A

K

R

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

D

N

G

L

V

H

D

I

V

S

V

A

I

P

G

V

T

S

T

D

-

I

-

H

-

I

-

R

-

Y

-

K

-

L

-

N

-

R

-

S

-

R

-

E

-

W

Y

V

I

L

I

D

D

C

S

M

A

K

T

R

E

A

V

V

I

A

N

Y

F

A

V

R

K

D

S

A

K

G

G

A

I

T

E

V

V

T

R

V

F

G

S

A

S

E

E

D

D

A

S

S

F

R

R

A

S

D

D

M

L

E

V

F

D

L

L

Q

S

F

L

A

Y

R

K

E

A

A

V

K

D

K

K

E

I

G

G

A

V

V

N

Y

R

L

V

R

G

F

I

A

A

D

D

T

T

L

V

G

G

V

C

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

D

R

L

V

I

E

R

Q

T

I

L

I

R

R

G

R

V

T

V

G

S

I

C

D

D

V

I

E

E

M

C

H
|
H

G

F

H
|
H

N

N

D

D

F

T

G

G

M

M

A

A

T

I

A

A

N

N

S

A

L

Y

A

C

A

A

Y

L

K

E

A

A

G

G

A

A

R

T

Y

H

L

I

S

D

T

T

T

S

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

active site: Q24 (= Q16)
binding cobalt (ii) ion: E21 (≠ D13), H188 (= H193), H190 (= H195)

2ztjA Crystal structure of homocitrate synthase from thermus thermophilus complexed with alpha-ketoglutarate (see paper)
35% identity, 78% coverage: 6:231/288 of query aligns to 6:225/312 of 2ztjA

query
sites
2ztjA

F

I

V

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

V

E

G

K

V

A

A

N

F

F

S

S

A

T

K

Q

E

D

K

K

V

V

H

E

I

I

A

A

G

K

L

A

L

L

D

D

A

E

V

F

G

G

V

I

Y

E

Q

Y

I

I

E

E

A

V

G

T

I

T

P

P

A

V

M

A

G

S

Q

P

L

Q

E

S

M

R

E

K

A

D

I

A

Y

E

S

V

I

L

L

A

A

S

L

L

N

G

L

L

K

K

A

A

K

K

I

V

S

V

T

T

W
x
H

N

I

R

Q

T

C

N

R

L

L

D

D

D

A

I

A

K

K

A

V

S

A

L

V

D

E

C

T

G

G

A

-

R

-

N

-

L

-

H

-

I

-

S

-

A

-

P

-

V

V

S

Q

D

G

I

I

H

D

I

L

R
x
L

Y

F

K

G

L

T

N

G

R

R

S

D

R

I

E

P

W

R

V

I

L

I

D

E

C

E

M

A

K

K

R

E

A

V

V

I

A

A

Y

Y

A

I

R

R

D

E

A

A

G

A

A

P

T

H

V

V

T

E

V

V

-
x
R

-

F

G

S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

M

E

E

Q

F

D

L

L

Q

A

F

-

A

V

R

Y

E

E

A

A

K

V

K

A

E

P

G

Y

A

V

V

D

Y

R

L

V

R

G

F

L

A
|
A

D

D

T
|
T

L

V

G

G

V

V

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

A

R

L

V

V

E

R

Q

E

I

V

I

R

R

R

R

V

T

V

G

G

-

P

-

R

I

V

D

D

V

I

E

E

M

F

H
|
H

G

G

H
|
H

N

N

D

D

F

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

Y

I

K

E

A

A

G

G

A

A

R

T

Y

H

L

V

S

D

T

T

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

active site: Q16 (= Q16)
binding 2-oxoglutaric acid: R12 (= R12), H72 (≠ W72), L94 (≠ R103), R125 (vs. gap), A156 (= A164), T158 (= T166), H187 (= H193), H189 (= H195)
binding copper (ii) ion: E13 (≠ D13), H187 (= H193), H189 (= H195)

2zyfA Crystal structure of homocitrate synthase from thermus thermophilus complexed with magnesuim ion and alpha-ketoglutarate (see paper)
34% identity, 78% coverage: 6:231/288 of query aligns to 6:227/314 of 2zyfA

query
sites
2zyfA

F

I

V

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q
|
Q

S

F

V

E

G

K

V

A

A

N

F

F

S

S

A

T

K

Q

E

D

K

K

V

V

H

E

I

I

A

A

G

K

L

A

L

L

D

D

A

E

V

F

G

G

V

I

Y

E

Q

Y

I

I

E

E

A

V

G

T

I

T

P

P

A

V

M

A

G

S

Q

P

L

Q

E

S

M

R

E

K

A

D

I

A

Y

E

S

V

I

L

L

A

A

S

L

L

N

G

L

L

K

K

A

A

K

K

I

V

S

V

T

T

W
x
H

N

I

R

Q

T

C

N

R

L

L

D

D

D

A

I

A

K

K

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

Q

N

G

L

I

H

-

I

-

S

-

A

-

P

-

V

-

S

-

D

D

I

L

H
x
L

I

F

R

G

Y

T

K

S

L

K

N

G

R

R

S

D

R

I

E

P

W

R

V

I

L

I

D

E

C

E

M

A

K

K

R

E

A

V

V

I

A

A

Y

Y

A

I

R

R

D

E

A

A

G

A

A

P

T

H

V

V

T

E

V

V

-
x
R

-

F

G

S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

M

E

E

Q

F

D

L

L

Q

A

F

-

A

V

R

Y

E

E

A

A

K

V

K

A

E

P

G

Y

A

V

V

D

Y

R

L

V

R

G

F

L

A

A

D

D

T
|
T

L

V

G

G

V

V

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

A

R

L

V

V

E

R

Q

E

I

V

I

R

R

R

R

V

T

V

G

G

-

P

-

R

I

V

D

D

V

I

E

E

M

F

H
|
H

G

G

H
|
H

N

N

D

D

F

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

Y

I

K

E

A

A

G

G

A

A

R

T

Y

H

L

V

S

D

T

T

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

active site: Q16 (= Q16)
binding 2-oxoglutaric acid: R12 (= R12), H72 (≠ W72), L94 (≠ H101), R127 (vs. gap), T160 (= T166), H189 (= H193)
binding magnesium ion: E13 (≠ D13), H189 (= H193), H191 (= H195)

3a9iA Crystal structure of homocitrate synthase from thermus thermophilus complexed with lys (see paper)
35% identity, 78% coverage: 6:231/288 of query aligns to 5:226/347 of 3a9iA

query
sites
3a9iA

F

I

V

I

D

D

T

S

T

T

L

L

R
|
R

D
x
E

G

G

E

E

Q

Q

S

F

V

E

G

K

V

A

A

N

F

F

S

S

A

T

K

Q

E

D

K

K

V

V

H

E

I

I

A

A

G

K

L

A

L

L

D

D

A

E

V

F

G

G

V

I

Y

E

Q

Y

I

I

E

E

A

V

G

T

I

T

P

P

A

V

M

A

G

S

Q

P

L

Q

E

S

M

R

E

K

A

D

I

A

Y

E

S

V

I

L

L

A

A

S

L

L

N

G

L

L

K

K

A

A

K

K

I

V

S

V

T

T

W

H

N

I

R

Q

T

C

N

R

L

L

D

D

D

A

I

A

K

K

A

V

S

A

L

V

D

E

C

T

G

G

A

V

R

Q

N

G

L

I

H
x
D

I

L

S

L

A

F

P

G

V

T

S

S

D

-

I

-

H

-

I

-

R

K

Y

Y

K

-

L

L

N

D

R

I

S

P

R

R

E

-

W

-

V

I

L

I

D

E

C

E

M

A

K

K

R

E

A

V

V

I

A

A

Y

Y

A

I

R

R

D

E

A

A

G

A

A

P

T

H

V

V

T

E

V

V

-

R

-

F

G
x
S

A

A

E

E

D

D

A

T

S

F

R

R

A

S

D

E

M

E

E

Q

F

D

L

L

Q

A

F

-

A

V

R

Y

E

E

A

A

K

V

K

A

E

P

G

Y

A

V

V

D

Y

R

L

V

R

G

F

L

A

A

D

D

T
|
T

L

V

G

G

V

V

M

A

D

T

P

P

F

R

T

Q

T

V

R

Y

N

A

R

L

V

V

E

R

Q

E

I

V

I

R

R

R

R

V

T

V

G

G

-

P

-

R

I

V

D

D

V

I

E

E

M

F

H
|
H

G

G

H
|
H

N

N

D

D

F

T

G

G

M

C

A

A

T

I

A

A

N

N

S

A

L

Y

A

E

A

A

Y

I

K

E

A

A

G

G

A

A

R

T

Y

H

L

V

S

D

T

T

V

I

L

L

G

G

M

I

G

G

E

E

R

R

A

N

G

G

N

I

S

T

P

P

binding cobalt (ii) ion: E12 (≠ D13), H188 (= H193), H190 (= H195)
binding lysine: R11 (= R12), D91 (≠ H92), S128 (≠ G134), T159 (= T166), H188 (= H193), H190 (= H195)

4ov9A Structure of isopropylmalate synthase binding with alpha- isopropylmalate (see paper)
30% identity, 77% coverage: 8:230/288 of query aligns to 8:242/380 of 4ov9A

query
sites
4ov9A

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

S

A

V

L

G

K

V

R

A

P

F

W

S

T

A

I

K

D

E

E

K

K

V

I

H

E

I

V

A

F

G

D

L

L

D

V

A

E

V

L

G

N

V

V

Y

D

Q

G

I

I

E

E

A

V

G

G

I

F

P

P

A

S

M

S

G

N

Q

E

L

T

E

E

M

F

E

H

A

T

I

C

Y

Q

S

V

I

L

L

S

A

K

L

R

N

A

L

P

K

K

A

G

K

K

-

P

I

I

S

A

T

A

W
x
L

N

S

R

R

T

A

N

N

L

Q

D

N

D

E

I

I

K

A

A

V

S

T

-

W

-

E

-

A

-

I

-

Q

-

K

L

A

D

D

C

C

G

P

A

-

R

-

N

R

L

M

H

H

I

I

S

V

A

Y

P

P

V

V

S

S

D

D

I

F

H

S

I

I

R

K

Y

H

K

V

L

L

N

K

R

I

S

S

R

E

E

K

W

E

V

V

L

L

D

Q

C

K

M

I

K

R

R

N

A

S

V

I

A

S

Y

F

A

A

R

R

D

S

-

I

-

V

-

G

A

P

G

G

A

I

T

E

V

I

T

Q

V

F

G

S

A

G

E

E

D

H

A

F

S

G

R

D

A

A

D

I

M

E

E

N

F

F

L

-

Q

A

F

F

A

T

R

K

E

E

A

A

-

F

-

L

-

T

-

A

K

I

K

E

E

A

G

G

A

A

V

N

Y

I

L

I

R

N

F

L

A

P

D

N

T
|
T

L

V

G

E

V

R

M

Y

D

R

P

P

F

M

T

V

T

F

R

V

N

N

R

M

V

V

E

K

Q

E

I

I

-

K

-

D

I

V

R

V

R

K

T

D

G

K

I

A

D

I

V

I

E

S

M

I

H
|
H

G

T

H
|
H

N

N

D

D

F

L

G

G

M

M

A

A

T

T

A

A

N

T

S

S

L

V

A

E

A

S

Y

V

K

Y

A

V

G

G

A

A

R

E

Y

Q

L

I

S

E

T

V

T

A

V

L

L

N

G

G

M

L

G

G

E

E

R

R

A

A

G

G

N

N

S

T

active site: Q16 (= Q16)
binding (2S)-2-hydroxy-2-(propan-2-yl)butanedioic acid: R12 (= R12), L73 (≠ W72), T176 (= T166), H205 (= H193), H207 (= H195)
binding zinc ion: D13 (= D13), H205 (= H193), H207 (= H195)

4ov4A Isopropylmalate synthase binding with ketoisovalerate (see paper)
30% identity, 77% coverage: 8:230/288 of query aligns to 8:242/379 of 4ov4A

query
sites
4ov4A

D

D

T

V

T

T

L

L

R
|
R

D
|
D

G

G

E

N

Q
|
Q

S

A

V

L

G

K

V

R

A

P

F

W

S

T

A

I

K

D

E

E

K

K

V

I

H

E

I

V

A

F

G

D

L

L

D

V

A

E

V

L

G

N

V

V

Y

D

Q

G

I

I

E

E

A

V

G

G

I

F

P

P

A

S

M

S

G

N

Q

E

L

T

E

E

M

F

E

H

A

T

I

C

Y

Q

S

V

I

L

L

S

A

K

L

R

N

A

L

P

K

K

A

G

K

K

-

P

I

I

S

A

T

A

W

L

N

S

R

R

T

A

N

N

L

Q

D

N

D

E

I

I

K

A

A

V

S

T

-

W

-

E

-

A

-

I

-

Q

-

K

L

A

D

D

C

C

G

P

A

-

R

-

N

R

L

M

H

H

I

I

S

V

A

Y

P

P

V

V

S

S

D

D

I

F

H

S

I

I

R

K

Y

H

K

V

L

L

N

K

R

I

S

S

R

E

E

K

W

E

V

V

L

L

D

Q

C

K

M

I

K

R

R

N

A

S

V

I

A

S

Y

F

A

A

R

R

D

S

-

I

-

V

-

G

A

P

G

G

A

I

T

E

V

I

T

Q

V

F

G

S

A

G

E

E

D

H

A

F

S

G

R

D

A

A

D

I

M

E

E

N

F

F

L

-

Q

A

F

F

A

T

R

K

E

E

A

A

-

F

-

L

-

T

-

A

K

I

K

E

E

A

G

G

A

A

V

N

Y

I

L

I

R

N

F

L

A
x
P

D

N

T
|
T

L

V

G

E

V

R

M

Y

D

R

P

P

F

M

T

V

T

F

R

V

N

N

R

M

V

V

E

K

Q

E

I

I

-

K

-

D

I

V

R

V

R

K

T

D

G

K

I

A

D

I

V

I

E

S

M

I

H
|
H

G

T

H
|
H

N

N

D

D

F

L

G

G

M

M

A

A

T

T

A

A

N

T

S

S

L

V

A

E

A

S

Y

V

K

Y

A

V

G

G

A

A

R

E

Y

Q

L

I

S

E

T

V

T

A

V

L

L

N

G

G

M

L

G

G

E

E

R

R

A

A

G

G

N

N

S

T

active site: Q16 (= Q16)
binding 3-methyl-2-oxobutanoic acid: R12 (= R12), P174 (≠ A164), T176 (= T166), H205 (= H193), H207 (= H195)
binding zinc ion: D13 (= D13), H205 (= H193), H207 (= H195)

4lrsA Crystal and solution structures of the bifunctional enzyme (aldolase/aldehyde dehydrogenase) from thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and coa accommodation whithin the shared cofactor-binding site
25% identity, 89% coverage: 3:259/288 of query aligns to 3:264/337 of 4lrsA

query
sites
4lrsA

K

R

I

V

L

R

F

I

V

T

D

D

T

S

T

T

L

L

R
|
R

D
|
D

G

G

E

S

Q
x
H

S

A

V

M

G

A

V

H

A

Q

F

F

S

T

A

E

K

E

E

Q

K

V

V

R

H

A

I

T

A

V

G

H

L

A

L

L

D

D

A

A

V

A

G

G

V

V

Y

E

Q

V

I

I

E

E

A

V

-

S

-

H

-

G

-

D

-

G

-

L

-

G

-

S

-

F

-

N

-

Y

G

G

I

F

P

S

A

A

M

V

G

D

Q

E

L

I

E

D

M

L

-

V

-

A

-

V

-

D

E

E

A

A

I

V

Y

N

S

A

I

K

L

I

A

A

L

V

N

L

L

L

K

L

A

P

K

G

I

V

S

G

T

T

W

-

N

-

R

-

T

-

N

-

L

V

D

R

D

D

I

L

K

K

A

R

S

A

L

H

D

D

C

A

G

G

A

A

R

S

N

V

L

A

H

R

I

I

S

A

A

T

P

H

V

C

S

T

D

E

I

A

H

-

I

-

R

-

Y

-

K

-

L

-

N

-

R

-

S

-

R

-

E

-

W

-

V

-

L

-

D

D

C

V

M

S

K

C

R

Q

A

H

V

F

A

A

Y

A

A

A

R

R

D

E

A

L

G

G

A

M

T

E

V

T

T

V

V

G

G
x
F

A

L

E
x
M

D

L

A

A

S

H

R

R

A

I

D

G

M

P

E

E

F

E

L

L

L

A

Q

R

F

Q

A

A

R

R

E

I

A

M

K

V

K

D

E

A

G

G

A

A

V

Q

Y

C

L

V

R

Y

F

V

A
x
V

D

D

T
x
S

L

A

G

G

V

A

M

L

D

V

P

L

F

S

T

D

T

V

R

Q

N

A

R

R

V

V

E

Q

Q

A

I

L

I

V

R

R

R

E

T

I

G

G

I

H

D

E

V

A

E

Q

M

V

-

G

-

F

H
|
H

G

G

H
|
H

N

Q

D

N

F

L

G

S

M

L

A

G

T

V

A

A

N

N

S

S

L

V

A

L

A

A

Y

Y

K

Q

A

N

G

G

A

A

R

R

Y

Q

L

I

S

D

T

G

T

A

V

L

L

C

G

A

M

L

G

G

E

A

R

G

A

A

G

G

N

N

S

S

P

P

Y

T

E

E

-

I

-

L

-

A

E

A

V

T

V

F

E

E

M

R

L

L

R

N

Y

I

V

E

E

T

G

G

I

V

P

N

L

V

P

Q

V

A

N

A

E

L

T

A

K

A

L

A

E

E

L

V

I

V

R

R

active site: D13 (= D13), H16 (≠ Q16), H195 (= H193), H197 (= H195)
binding magnesium ion: D13 (= D13), H195 (= H193), H197 (= H195)
binding pyruvic acid: R12 (= R12), D13 (= D13), F134 (≠ G134), M136 (≠ E136), V164 (≠ A164), S166 (≠ T166), H195 (= H193), H197 (= H195)

Sites not aligning to the query:

active site: 286
binding pyruvic acid: 286

Query Sequence

>WP_013843393.1 NCBI__GCF_000215085.1:WP_013843393.1
MDKILFVDTTLRDGEQSVGVAFSAKEKVHIAGLLDAVGVYQIEAGIPAMGQLEMEAIYSI
LALNLKAKISTWNRTNLDDIKASLDCGARNLHISAPVSDIHIRYKLNRSREWVLDCMKRA
VAYARDAGATVTVGAEDASRADMEFLLQFAREAKKEGAVYLRFADTLGVMDPFTTRNRVE
QIIRRTGIDVEMHGHNDFGMATANSLAAYKAGARYLSTTVLGMGERAGNSPYEEVVEMLR
YVEGIPLPVNETKLEELIRFVAGAANWPVKPLKMHGLRKAGVEKISLA

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