SitesBLAST

P40939 Trifunctional enzyme subunit alpha, mitochondrial; 78 kDa gastrin-binding protein; Monolysocardiolipin acyltransferase; TP-alpha; EC 2.3.1.-; EC 4.2.1.17; EC 1.1.1.211 from Homo sapiens (Human) (see 5 papers)
30% identity, 65% coverage: 36:214/276 of query aligns to 64:234/763 of P40939

query
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P40939

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Sites not aligning to the query:

282 V → D: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852773
305 I → N: in MTPD1; mild phenotype with slowly progressive myopathy and sensorimotor polyneuropathy; dbSNP:rs137852774
342 L → P: in LCHAD deficiency; dbSNP:rs137852772
510 active site, For hydroxyacyl-coenzyme A dehydrogenase activity; E → Q: in AFLP and LCHAD deficiency; loss of long-chain-3-hydroxyacyl-CoA dehydrogenase activity; dbSNP:rs137852769

3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis (see paper)
29% identity, 58% coverage: 45:204/276 of query aligns to 29:180/256 of 3h81A

query
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active site: A64 (≠ G79), M69 (≠ F84), T79 (≠ R94), F83 (≠ L96), G107 (= G131), E110 (= E134), P129 (= P153), E130 (= E154), V135 (≠ L159), P137 (= P161), G138 (= G162)

Sites not aligning to the query:

active site: 223, 233
binding calcium ion: 233, 238

3q0jC Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
29% identity, 58% coverage: 45:204/276 of query aligns to 30:181/255 of 3q0jC

query
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3q0jC

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active site: A65 (≠ G79), M70 (≠ F84), T80 (≠ R94), F84 (≠ L96), G108 (= G131), E111 (= E134), P130 (= P153), E131 (= E154), V136 (≠ L159), P138 (= P161), G139 (= G162)
binding acetoacetyl-coenzyme a: A63 (≠ L77), G64 (= G78), A65 (≠ G79), D66 (= D80), I67 (≠ L81), K68 (≠ D82), M70 (≠ F84), F84 (≠ L96), G107 (= G130), G108 (= G131), E111 (= E134), P130 (= P153), E131 (= E154), P138 (= P161), G139 (= G162), M140 (= M163)

Sites not aligning to the query:

active site: 224, 234
binding acetoacetyl-coenzyme a: 23, 24, 25, 27

3q0gC Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
29% identity, 58% coverage: 45:204/276 of query aligns to 30:181/255 of 3q0gC

query
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3q0gC

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active site: A65 (≠ G79), M70 (≠ F84), T80 (≠ R94), F84 (≠ L96), G108 (= G131), E111 (= E134), P130 (= P153), E131 (= E154), V136 (≠ L159), P138 (= P161), G139 (= G162)
binding coenzyme a: A63 (≠ L77), I67 (≠ L81), K68 (≠ D82), Y104 (≠ D127), P130 (= P153), E131 (= E154), L134 (≠ F157)

Sites not aligning to the query:

active site: 224, 234
binding coenzyme a: 25

3q0gD Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
40% identity, 31% coverage: 120:204/276 of query aligns to 92:176/250 of 3q0gD

query
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3q0gD

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active site: G103 (= G131), E106 (= E134), P125 (= P153), E126 (= E154), V131 (≠ L159), P133 (= P161), G134 (= G162)

Sites not aligning to the query:

active site: 64, 69, 75, 79, 219, 229
binding Butyryl Coenzyme A: 225, 241

5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid (see paper)
27% identity, 66% coverage: 25:207/276 of query aligns to 18:188/261 of 5jbxB

query
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5jbxB

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active site: A67 (≠ G79), R72 (≠ F84), L84 (≠ V97), R88 (≠ Q101), G112 (= G131), E115 (= E134), T134 (≠ P153), E135 (= E154), I140 (≠ L159), P142 (= P161), G143 (= G162)
binding coenzyme a: S24 (≠ H31), R25 (≠ P32), R26 (= R33), A28 (≠ C35), A65 (≠ L77), D68 (= D80), L69 (= L81), K70 (≠ D82), L110 (= L129), G111 (= G130), T134 (≠ P153), E135 (= E154), L138 (≠ F157), R168 (≠ L187)

Sites not aligning to the query:

active site: 228, 238

6eqoA Tri-functional propionyl-coa synthase of erythrobacter sp. Nap1 with bound NADP+ and phosphomethylphosphonic acid adenylate ester (see paper)
37% identity, 46% coverage: 121:248/276 of query aligns to 955:1095/1804 of 6eqoA

query
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6eqoA

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V

active site: G965 (= G131), E968 (= E134), E988 (= E154), G996 (= G162)

Sites not aligning to the query:

active site: 918
binding phosphomethylphosphonic acid adenylate ester: 456, 458, 535, 536, 537, 538, 558, 559, 560, 561, 562, 688, 714
binding nadp nicotinamide-adenine-dinucleotide phosphate: 1261, 1265, 1379, 1400, 1403, 1404, 1405, 1424, 1425, 1429, 1444, 1492, 1493, 1497, 1514, 1517, 1713, 1730, 1731, 1774

Q08426 Peroxisomal bifunctional enzyme; PBE; PBFE; L-bifunctional protein; LBP; Multifunctional enzyme 1; MFE1; EC 4.2.1.17; EC 5.3.3.8; EC 1.1.1.35 from Homo sapiens (Human) (see 5 papers)
30% identity, 50% coverage: 120:258/276 of query aligns to 90:220/723 of Q08426

query
sites
Q08426

T

V

I

V

A

A

L

A

V

I

Q

Q

G

G

D

M

A

A

L

F

G

G

F

L

E

E

A

L

A

A

L

L

A

G

A

C

H

H

V

Y

L

R

I

I

A

A

E

H

E

A

G

E

T

A

K

Q

L

V

G

G

F

L

P

P

E

E

V

V

L

T

F

L

N

G

L

L

F

L

P

P

G

G

M

A

G

R

A

G

Y

T

H

Q

M

L

L

L

S

P

R

R

R

L

L

T

P

G

V

V

K

P

R

A

A

A

E

L

Q

D

L

L

M

I

L

T

S

S

G

G

E

R

L

R

Y

I

S

L

A

A

E

D

D

E

L

A

H

L

A
x
K

R

L

G

G

V

I

V

L

D

D

V
x
K

L

V

A

V

P

-

R

-

G

-

Q

-

G

N

S

S

E

D

A

P

V

V

E

E

Y

A

I

I

R

R

S

F

E

A

R

Q

A

R

Y

V

A

S

R

D

G

Q

A

P

A

L

A

E

I

S

R

R

I

-

G

-

H

-

L

L

D

C

Q

N

V

K

P

P

A

I

S

Q

S

S

L

L

S

P

D

N

V

M

V

D

T

S

L

I

W

F

V

S

D

E

S

A

A

L

M

L

R

K

L

M

K165 (≠ A195) modified: N6-acetyllysine; alternate; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-171; Q-346 and Q-584.
K171 (≠ V201) modified: N6-acetyllysine; mutation to Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-346 and Q-584.

Sites not aligning to the query:

3 E → K: in FRTS3; the mutant is mistargeted to mitochondria; results in impaired mitochondrial oxidative phosphorylation and defects in the transport of fluids across the epithelium of renal proximal tubular cells; dbSNP:rs398124646
40 V → G: in dbSNP:rs1062551
41 I → R: in dbSNP:rs1062552
75 T → I: in dbSNP:rs1062553
274 A → T: in dbSNP:rs2302819
325 A → G: in dbSNP:rs1062555
346 modified: N6-acetyllysine; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-584.
584 modified: N6-acetyllysine; alternate; K→Q: Greatly reduced acetylation and insensitive to treatment with TSA and NAM; when associated with Q-165; Q-171 and Q-346.
598 K → T: in dbSNP:rs1042437
606 T → P: in dbSNP:rs1042438

2dubA Enoyl-coa hydratase complexed with octanoyl-coa (see paper)
34% identity, 39% coverage: 121:229/276 of query aligns to 95:200/254 of 2dubA

query
sites
2dubA

I

I

A

A

L

A

V

V

Q

N

G

G

D

Y

A

A

L

L

G

G

G
|
G

G

G

F

C

E
|
E

A

L

A

A

L

M

A

M

A

C

H

D

V

I

L

I

I

Y

A

A

E

G

E

E

G

K

T

A

K

Q

L

F

G

G

F

Q

P
|
P

E
|
E

V

I

L

L

F

L

N

G

L
x
T

F

I

P
|
P

G
|
G

M
x
A

G

G

A

G

Y

T

H

Q

M

R

L

L

S

T

R

R

R

A

L

V

P

G

V

K

K

S

R

L

A

A

E

M

Q

E

L

M

M

V

L

L

S

T

G

G

E

D

L

R

Y

I

S

S

A

A

E

Q

D

D

L

A

H

K

A

Q

R

A

G

G

V

L

V

V

D

S

V

K

L

I

A

F

P

P

R

V

G

-

Q

-

G

-

S

E

E

T

A

L

V

V

E

E

Y

A

I

I

R

Q

S

C

E

A

R

E

A

K

Y

I

A

A

R

N

G

N

A

S

A

K

A

I

I

I

active site: G105 (= G131), E108 (= E134), P127 (= P153), E128 (= E154), T133 (≠ L159), P135 (= P161), G136 (= G162)
binding octanoyl-coenzyme a: G105 (= G131), E108 (= E134), P127 (= P153), E128 (= E154), G136 (= G162), A137 (≠ M163)

Sites not aligning to the query:

active site: 67, 72, 82, 221, 231
binding octanoyl-coenzyme a: 25, 26, 27, 29, 65, 67, 68, 69, 70

1mj3A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa (see paper)
34% identity, 39% coverage: 121:229/276 of query aligns to 99:204/258 of 1mj3A

query
sites
1mj3A

I

I

A

A

L

A

V

V

Q

N

G

G

D

Y

A

A

L

L

G

G

G
|
G

G

G

F

C

E
|
E

A

L

A

A

L

M

A

M

A

C

H

D

V

I

L

I

I

Y

A

A

E

G

E

E

G

K

T

A

K

Q

L

F

G

G

F

Q

P
|
P

E
|
E

V

I

L

L

F
x
L

N

G

L
x
T

F

I

P
|
P

G
|
G

M

A

G

G

A

G

Y

T

H

Q

M

R

L

L

S

T

R

R

R

A

L

V

P

G

V

K

K

S

R

L

A

A

E

M

Q

E

L

M

M

V

L

L

S

T

G

G

E

D

L

R

Y

I

S

S

A

A

E

Q

D

D

L

A

H

K

A

Q

R

A

G

G

V

L

V

V

D

S

V

K

L

I

A

F

P

P

R

V

G

-

Q

-

G

-

S

E

E

T

A

L

V

V

E

E

Y

A

I

I

R

Q

S

C

E

A

R

E

A

K

Y

I

A

A

R

N

G

N

A

S

A

K

A

I

I

I

active site: G109 (= G131), E112 (= E134), P131 (= P153), E132 (= E154), T137 (≠ L159), P139 (= P161), G140 (= G162)
binding hexanoyl-coenzyme a: G109 (= G131), P131 (= P153), E132 (= E154), L135 (≠ F157), G140 (= G162)

Sites not aligning to the query:

active site: 68, 73, 83, 85, 225, 235
binding hexanoyl-coenzyme a: 26, 27, 28, 30, 66, 67, 68, 69, 70

1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5 (see paper)
34% identity, 39% coverage: 121:229/276 of query aligns to 101:206/260 of 1dubA

query
sites
1dubA

I

I

A

A

L

A

V

V

Q

N

G

G

D
x
Y

A

A

L

L

G
|
G

G

G

F

C

E
|
E

A

L

A

A

L

M

A

M

A

C

H

D

V

I

L

I

I

Y

A

A

E

G

E

E

G

K

T

A

K

Q

L

F

G

G

F

Q

P
|
P

E
|
E

V

I

L

L

F
x
L

N

G

L
x
T

F

I

P
|
P

G
|
G

M

A

G

G

A

G

Y

T

H

Q

M

R

L

L

S

T

R

R

R

A

L

V

P

G

V

K

K

S

R

L

A

A

E

M

Q

E

L

M

M

V

L

L

S

T

G

G

E

D

L

R

Y

I

S

S

A

A

E

Q

D

D

L

A

H

K

A

Q

R

A

G

G

V

L

V

V

D

S

V

K

L

I

A

F

P

P

R

V

G

-

Q

-

G

-

S

E

E

T

A

L

V

V

E

E

Y

A

I

I

R

Q

S

C

E

A

R

E

A

K

Y

I

A

A

R

N

G

N

A

S

A

K

A

I

I

I

active site: G111 (= G131), E114 (= E134), P133 (= P153), E134 (= E154), T139 (≠ L159), P141 (= P161), G142 (= G162)
binding acetoacetyl-coenzyme a: Y107 (≠ D127), G110 (= G130), G111 (= G131), E114 (= E134), P133 (= P153), E134 (= E154), L137 (≠ F157), G142 (= G162)

Sites not aligning to the query:

active site: 68, 73, 83, 87, 227, 237
binding acetoacetyl-coenzyme a: 26, 27, 28, 30, 66, 68, 69, 70, 233, 249

1ey3A Structure of enoyl-coa hydratase complexed with the substrate dac-coa (see paper)
34% identity, 39% coverage: 121:229/276 of query aligns to 99:204/258 of 1ey3A

query
sites
1ey3A

I

I

A

A

L

A

V

V

Q

N

G

G

D

Y

A

A

L

L

G

G

G
|
G

G

G

F

C

E
|
E

A

L

A

A

L

M

A

M

A

C

H

D

V

I

L

I

I

Y

A

A

E

G

E

E

G

K

T

A

K

Q

L

F

G

G

F

Q

P
|
P

E
|
E

V

I

L

L

F
x
L

N

G

L
x
T

F

I

P
|
P

G
|
G

M

A

G

G

A

G

Y

T

H

Q

M

R

L

L

S

T

R

R

R

A

L

V

P

G

V

K

K

S

R

L

A

A

E

M

Q

E

L

M

M

V

L

L

S

T

G

G

E

D

L

R

Y

I

S

S

A

A

E

Q

D

D

L

A

H

K

A

Q

R

A

G

G

V

L

V

V

D

S

V

K

L

I

A

F

P

P

R

V

G

-

Q

-

G

-

S

E

E

T

A

L

V

V

E

E

Y

A

I

I

R

Q

S

C

E

A

R

E

A

K

Y

I

A

A

R

N

G

N

A

S

A

K

A

I

I

I

active site: G109 (= G131), E112 (= E134), P131 (= P153), E132 (= E154), T137 (≠ L159), P139 (= P161), G140 (= G162)
binding 4-(n,n-dimethylamino)cinnamoyl-coa: G109 (= G131), P131 (= P153), L135 (≠ F157), G140 (= G162)

Sites not aligning to the query:

active site: 66, 71, 81, 85, 225, 235
binding 4-(n,n-dimethylamino)cinnamoyl-coa: 24, 26, 28, 64, 65, 66, 67, 68, 85, 88

P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 from Rattus norvegicus (Rat) (see 3 papers)
34% identity, 40% coverage: 120:229/276 of query aligns to 130:236/290 of P14604

query
sites
P14604

T

V

I

I

A

A

L

A

V

V

Q

N

G

G

D

Y

A

A

L

L

G

G

F

C

E
|
E

A

L

A

A

L

M

A

M

A

C

H

D

V

I

L

I

I

Y

A

A

E

G

E

E

G

K

T

A

K

Q

L

F

G

G

F

Q

P

P

E
|
E

V

I

L

L

F

L

N

G

L

T

F

I

P

P

G

G

M

A

G

G

A

G

Y

T

H

Q

M

R

L

L

S

T

R

R

R

A

L

V

P

G

V

K

K

S

R

L

A

A

E

M

Q

E

L

M

M

V

L

L

S

T

G

G

E

D

L

R

Y

I

S

S

A

A

E

Q

D

D

L

A

H

K

A

Q

R

A

G

G

V

L

V

V

D

S

V

K

L

I

A

F

P

P

R

V

G

-

Q

-

G

-

S

E

E

T

A

L

V

V

E

E

Y

A

I

I

R

Q

S

C

E

A

R

E

A

K

Y

I

A

A

R

N

G

N

A

S

A

K

A

I

I

I

E144 (= E134) mutation to D: Reduces activity 50-fold.; mutation to Q: Reduces activity 3300-fold.
E164 (= E154) mutation to D: Reduces activity 1250-fold.; mutation to Q: Reduces activity 330000-fold.

Sites not aligning to the query:

1:29 modified: transit peptide, Mitochondrion

Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
29% identity, 62% coverage: 30:200/276 of query aligns to 29:186/270 of Q4WF54

query
sites
Q4WF54

P

P

H

E

P

K

R

R

P

N

C

C

F

I

S

S

S

L

E

-

L

-

G

-

E

-

L

-

S

-

Q

A

V

T

S

S

T

A

R

E

I

I

P

Q

K

R

E

L

V

W

T

T

T

W

L

F

Q

D

S

T

E

Q

P

P

H

A

-

L

Y

Y

F

V

V

A

L

I

C

I

S

T

D

G

I

T

P

G

G

E

V

S

F

F

N

C

L

A

G

G

G

A

D

D

L

L

D

K

L

E

F

W

A

N

Q

D

L

L

V

-

R

-

E

-

R

-

N

N

Y

A

R

R

G

G

L

I

V

T

E

N

Y

-

G

-

Q

-

K

-

C

-

L

-

R

E

M

M

V

T

T

A

A

P

N

G

S

L

S

A

G

G

L

L

-

P

-

R

Q

R

G

G

H

S

A

K

T

P

T

I

I

I

A

A

L

A

V

V

Q

N

G

G

D

Y

A

C

L

L

G

G

F

F

E

E

A

M

A

V

L

A

A

N

A

C

H

D

V

I

L

V

I

V

A

A

E

S

E

E

G

N

T

A

K

T

L

F

G

G

F

L

P

P

E

E

V

V

L

Q

F

R

N

G

L

I

F

A

P

A

G

V

M

A

G

G

A

S

Y

L

H

P

M

R

L

L

S

V

R

R

R

V

L

L

P

G

V

K

K

Q

R

R

A

A

E

A

Q

E

L

I

M

A

L

L

S

S

G

G

E

L

L

S

Y

F

S

S

A

A

E

S

D

Q

L

L

H

E

A

R

R

W

G

G

V

L

V

V

D

N

Sites not aligning to the query:

268:270 PTS1-type peroxisomal targeting signal

1wdlA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form ii (native4) (see paper)
31% identity, 44% coverage: 117:237/276 of query aligns to 103:211/715 of 1wdlA

query
sites
1wdlA

H

N

A

V

T

P

T

T

I

V

A

A

L

A

V

I

Q

N

G

G

D

I

A

A

L

L

G

G

G
|
G

G

G

F

L

E
|
E

A

M

A

C

L

L

A

A

H

D

V

F

L

R

I

V

A

M

E

A

E

D

G

S

T

A

K

K

L

I

G

G

F

L

P
|
P

E
|
E

V

V

L

K

F

L

N

G

L

I

F

Y

P
|
P

G
|
G

M

F

G

G

A

G

Y

T

H

V

M

R

L

L

S

P

R

R

R

L

L

I

P

G

V

V

K

D

R

N

A

A

E

V

Q

E

L

W

M

I

L

A

S

S

G

G

E

K

L

E

Y

N

S

R

A

A

E

E

D

D

L

A

H

L

A

K

R

V

G

S

V

A

V

V

D

D

V

A

L

V

A

V

P

T

R

A

G

D

Q

K

G

L

S

G

E

A

A

A

V

A

E

L

E

D

Y

L

I

I

R

K

S

-

E

-

R

-

A

-

Y

-

A

-

R

-

G

-

A

-

I

-

R

R

R

A

I

I

G

S

G

G

H

E

L

L

D

D

active site: G117 (= G131), E120 (= E134), P139 (= P153), E140 (= E154), P147 (= P161), G148 (= G162)

Sites not aligning to the query:

active site: 69, 89, 93, 430, 451, 463, 501
binding nicotinamide-adenine-dinucleotide: 322, 324, 325, 344, 345, 400, 401, 403, 428, 429, 430

P28793 Fatty acid oxidation complex subunit alpha; EC 4.2.1.17; EC 5.1.2.3; EC 5.3.3.8; EC 1.1.1.35 from Pseudomonas fragi (see paper)
31% identity, 44% coverage: 117:237/276 of query aligns to 103:211/715 of P28793

query
sites
P28793

H

N

A

V

T

P

T

T

I

V

A

A

L

A

V

I

Q

N

G

G

D

I

A

A

L

L

G

G

F

L

E

E

A

M

A

C

L

L

A

A

H

D

V

F

L

R

I

V

A

M

E

A

E

D

G

S

T

A

K

K

L

I

G

G

F

L

P

P

E

E

V

V

L

K

F

L

N

G

L

I

F

Y

P

P

G

G

M

F

G

G

A

G

Y

T

H

V

M

R

L

L

S

P

R

R

R

L

L

I

P

G

V

V

K

D

R

N

A

A

E

V

Q

E

L

W

M

I

L

A

S

S

G

G

E

K

L

E

Y

N

S

R

A

A

E

E

D

D

L

A

H

L

A

K

R

V

G

S

V

A

V

V

D

D

V

A

L

V

A

V

P

T

R

A

G

D

Q

K

G

L

S

G

E

A

A

A

V

A

E

L

E

D

Y

L

I

I

R

K

S

-

E

-

R

-

A

-

Y

-

A

-

R

-

G

-

A

-

I

-

R

R

R

A

I

I

G

S

G

G

H

E

L

L

D

D

Sites not aligning to the query:

297 binding substrate
325 binding NAD(+)
344 binding NAD(+)
401:403 binding NAD(+)
408 binding NAD(+)
430 binding NAD(+)
454 binding NAD(+)
501 binding substrate
660 binding substrate

1wdmA Fatty acid beta-oxidation multienzyme complex from pseudomonas fragi, form i (native3) (see paper)
31% identity, 44% coverage: 117:237/276 of query aligns to 103:211/707 of 1wdmA

query
sites
1wdmA

H

N

A

V

T

P

T

T

I

V

A

A

L

A

V

I

Q

N

G

G

D

I

A

A

L

L

G

G

G
|
G

G

G

F

L

E
|
E

A

M

A

C

L

L

A

A

H

D

V

F

L

R

I

V

A

M

E

A

E

D

G

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T

A

K

K

L

I

G

G

F

L

P
|
P

E
|
E

V

V

L
x
K

F

L

N

G

L

I

F

Y

P
|
P

G
|
G

M

F

G

G

A

G

Y

T

H

V

M

R

L

L

S

P

R

R

R

L

L

I

P

G

V

V

K

D

R

N

A

A

E

V

Q

E

L

W

M

I

L

A

S

S

G

G

E

K

L

E

Y

N

S

R

A

A

E

E

D

D

L

A

H

L

A

K

R

V

G

S

V

A

V

V

D

D

V

A

L

V

A

V

P

T

R

A

G

D

Q

K

G

L

S

G

E

A

A

A

V

A

E

L

E

D

Y

L

I

I

R

K

S

-

E

-

R

-

A

-

Y

-

A

-

R

-

G

-

A

-

I

-

R

R

R

A

I

I

G

S

G

G

H

E

L

L

D

D

active site: G117 (= G131), E120 (= E134), P139 (= P153), E140 (= E154), P147 (= P161), G148 (= G162)
binding acetyl coenzyme *a: K142 (≠ L156)

Sites not aligning to the query:

active site: 69, 89, 93, 430, 451, 463, 501
binding acetyl coenzyme *a: 297, 459, 501, 534, 652, 658
binding nicotinamide-adenine-dinucleotide: 321, 322, 324, 325, 344, 401, 403, 428, 430, 454

2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
35% identity, 30% coverage: 121:204/276 of query aligns to 101:184/260 of 2hw5C

query
sites
2hw5C

I

I

A

A

L

A

V

V

Q

N

G

G

D

Y

A

A

L
x
F

G

G

G
|
G

G

G

F

C

E
|
E

A

L

A

A

L

M

A

M

A

C

H

D

V

I

L

I

I

Y

A

A

E

G

E

E

G

K

T

A

K

Q

L

F

G

A

F

Q

P
|
P

E
|
E

V

I

L

L

F

I

N

G

L
x
T

F

I

P
|
P

G
|
G

M

A

G

G

A

G

Y

T

H

Q

M

R

L

L

S

T

R

R

R

A

L

V

P

G

V

K

K

S

R

L

A

A

E

M

Q

E

L

M

M

V

L

L

S

T

G

G

E

D

L

R

Y

I

S

S

A

A

E

Q

D

D

L

A

H

K

A

Q

R

A

G

G

V

L

V

V

D

S

V

K

L

I

A

C

P

P

active site: G111 (= G131), E114 (= E134), P133 (= P153), E134 (= E154), T139 (≠ L159), P141 (= P161), G142 (= G162)
binding crotonyl coenzyme a: F109 (≠ L129)

Sites not aligning to the query:

active site: 68, 73, 83, 87, 227, 237
binding crotonyl coenzyme a: 26, 27, 28, 30, 62, 70

Query Sequence

>WP_018234152.1 NCBI__GCF_000378965.1:WP_018234152.1
MSTTNNKNTFKHLTLSYDDKRRTYWCRLHPHPRPCFSSELLGELSQVSTRIPKEVTTLQS
EPHYFVLCSDIPGVFNLGGDLDLFAQLVRERNYRGLVEYGQKCLRMVTANSSGLQGHATT
IALVQGDALGGGFEAALAAHVLIAEEGTKLGFPEVLFNLFPGMGAYHMLSRRLPVKRAEQ
LMLSGELYSAEDLHARGVVDVLAPRGQGSEAVEEYIRSERAYARGAAAIRRIGGHLDQVP
ASSLSDVVTLWVDSAMRLTERDLKLMGRIVSRQNHL

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