SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_027180538.1 NCBI__GCF_000429985.1:WP_027180538.1 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 17 hits to proteins with known functional sites (download)

Q58667 Methanogen homoaconitase small subunit; HACN; Homoaconitate hydratase; EC 4.2.1.114 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
53% identity, 97% coverage: 1:161/166 of query aligns to 1:159/170 of Q58667

query
sites
Q58667

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R26 (≠ V26) mutation R->K,V: Allows the recognition of substrates of IPMI enzymes since it becomes able to efficiently catalyze citraconate hydration and 3-isopropylmalate dehydration. Largely decreases substrate affinity for cis-homo(1-3)-aconitate.
T27 (= T27) mutation to A: Largely decreases substrate affinity for cis-homo(1-3)-aconitate while slightly increases activity on these substrates, and also decreases substrate affinity for maleate. Gains the ability to hydrate citraconate, an IPMI substrate.

2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
53% identity, 97% coverage: 1:161/166 of query aligns to 1:159/167 of 2pkpA

query
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2pkpA

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binding zinc ion: D13 (≠ H13), C63 (= C63)

O14289 3-isopropylmalate dehydratase; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
32% identity, 85% coverage: 12:152/166 of query aligns to 553:706/758 of O14289

query
sites
O14289

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Sites not aligning to the query:

486 modified: Phosphoserine
488 modified: Phosphoserine

P9WK95 3-isopropylmalate dehydratase small subunit; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
35% identity, 58% coverage: 12:108/166 of query aligns to 17:118/198 of P9WK95

query
sites
P9WK95

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Sites not aligning to the query:

154 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
37% identity, 51% coverage: 54:138/166 of query aligns to 658:740/780 of P20004

query
sites
P20004

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SR 670:671 (= SR 66:67) binding substrate

Sites not aligning to the query:

99 binding substrate
192:194 binding substrate
385 binding [4Fe-4S] cluster
448 binding [4Fe-4S] cluster
451 binding [4Fe-4S] cluster
474 binding substrate
479 binding substrate
607 binding substrate

8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
33% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 8acnA

query
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8acnA

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active site: S641 (= S65), R643 (= R67)
binding nitroisocitric acid: S641 (= S65), S642 (= S66), R643 (= R67)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding nitroisocitric acid: 71, 74, 100, 164, 165, 446, 451, 579
binding iron/sulfur cluster: 100, 164, 166, 356, 357, 420, 423, 424

1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
33% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 1fghA

query
sites
1fghA

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active site: S641 (= S65), R643 (= R67)
binding 4-hydroxy-aconitate ion: S641 (= S65), S642 (= S66), R643 (= R67)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding 4-hydroxy-aconitate ion: 71, 74, 100, 164, 165, 446, 451, 579
binding iron/sulfur cluster: 100, 164, 166, 356, 357, 420, 423, 424, 451

1amjA Steric and conformational features of the aconitase mechanism (see paper)
33% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 1amjA

query
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1amjA

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active site: S641 (= S65), R643 (= R67)
binding sulfate ion: R643 (= R67)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding iron/sulfur cluster: 144, 166, 357, 420, 423
binding sulfate ion: 71, 579

1amiA Steric and conformational features of the aconitase mechanism (see paper)
33% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 1amiA

query
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1amiA

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active site: S641 (= S65), R643 (= R67)
binding alpha-methylisocitric acid: S641 (= S65), S642 (= S66), R643 (= R67)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding alpha-methylisocitric acid: 71, 74, 100, 164, 165, 446, 451, 579
binding iron/sulfur cluster: 100, 144, 164, 166, 356, 357, 420, 423, 445

1acoA Crystal structure of aconitase with transaconitate bound (see paper)
33% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 1acoA

query
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1acoA

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D

I

F

T

A

T

P

G

G

E

K

T

P

I

L

T

T

C

C

active site: S641 (= S65), R643 (= R67)
binding aconitate ion: S641 (= S65), S642 (= S66), R643 (= R67)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding iron/sulfur cluster: 100, 144, 164, 166, 356, 357, 420, 423, 445
binding aconitate ion: 71, 164, 165, 446, 451, 579

1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
33% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 1nisA

query
sites
1nisA

I

V

M

V

V

I

A

G

D

D

E

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

R

P

A

I

L

S

E

I

P

L

R

G

F

A

L

G

G

I

G

P

R

V

A

V

I

A

T

H

K

S

S

F

F

A

A

R

R

I

I

F

H

Y

E

R

T

N

N

G

L

F

K

N

K

M

Q

G

G

L

L

I

L

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

N

D

V

Y

S

N

K

K

I

I

S

H

D

P

G

V

D

D

E

K

L

L

E

T

V

I

D

Q

A

G

D

-

K

-

G

-

E

-

I

L

K

K

N

D

I

F

T

A

T

P

G

G

E

K

T

P

I

L

T

T

C

C

active site: S641 (= S65), R643 (= R67)
binding 2-hydroxy-2-nitromethyl succinic acid: S641 (= S65), S642 (= S66)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding 2-hydroxy-2-nitromethyl succinic acid: 71, 100, 164, 165, 446, 451, 579
binding iron/sulfur cluster: 100, 144, 166, 356, 357, 420, 423

5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
32% identity, 51% coverage: 54:138/166 of query aligns to 631:713/754 of 5acnA

query
sites
5acnA

I

V

M

V

V

I

A

G

D

D

E

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

S

S

R
|
R

E

E

H

H

A

S

P

A

I

L

S

E

I

P

L

R

G

H

A

L

G

G

I

G

P

R

V

A

V

I

A

T

H

K

S

S

F

F

A

A

R
|
R

I

I

F

H

Y

E

R

T

N

N

G

L

F

K

N

K

M

Q

G

G

L

L

I

L

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

N

D

V

Y

S

N

K

K

I

I

S

H

D

P

G

V

D

D

E

K

L

L

E

T

V

I

D

Q

A

G

D

-

K

-

G

-

E

-

I

L

K

K

N

D

I

F

T

A

T

P

G

G

E

K

T

P

I

L

T

K

C

C

active site: S642 (= S65), R644 (= R67)
binding tricarballylic acid: R666 (= R89)

Sites not aligning to the query:

active site: 100, 101, 165, 447
binding fe3-s4 cluster: 145, 147, 167, 358, 421, 424, 446
binding tricarballylic acid: 198, 235

P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
32% identity, 51% coverage: 54:138/166 of query aligns to 658:740/781 of P16276

query
sites
P16276

I

V

M

V

V

I

A

G

D

D

E

E

N

N

F

Y

G

G

C

E

G

G

S

S

S
|
S

R
|
R

E

E

H

H

A

R

P

A

I

L

S

E

I

P

L

R

G

H

A

L

G

G

I

G

P

R

V

A

V

I

A

T

H

K

S

S

F

F

A

A

R

R

I

I

F

H

Y

E

R

T

N

N

G

L

F

K

N

K

M

Q

G

G

L

L

I

L

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

N

D

V

Y

S

N

K

K

I

I

S

H

D

P

G

V

D

D

E

K

L

L

E

T

V

I

D

Q

A

G

D

-

K

-

G

-

E

-

I

L

K

K

N

D

I

F

T

A

T

P

G

G

E

K

T

P

I

L

T

K

C

C

SR 670:671 (= SR 66:67) binding substrate

Sites not aligning to the query:

28 modified: Pyrrolidone carboxylic acid
99 binding substrate
192:194 binding substrate
385 binding [4Fe-4S] cluster
448 binding [4Fe-4S] cluster
451 binding [4Fe-4S] cluster
474 binding substrate
479 binding substrate
607 binding substrate

1b0kA S642a:fluorocitrate complex of aconitase (see paper)
31% identity, 51% coverage: 54:138/166 of query aligns to 630:712/753 of 1b0kA

query
sites
1b0kA

I

V

M

V

V

I

A

G

D

D

E

E

N

N

F

Y

G

G

C

E

G

G

S
x
A

S
|
S

R
|
R

E

E

H

H

A

S

P

A

I

L

S

E

I

P

L

R

G

H

A

L

G

G

I

G

P

R

V

A

V

I

A

T

H

K

S

S

F

F

A

A

R

R

I

I

F

H

Y

E

R

T

N

N

G

L

F

K

N

K

M

Q

G

G

L

L

I

L

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

N

D

V

Y

S

N

K

K

I

I

S

H

D

P

G

V

D

D

E

K

L

L

E

T

V

I

D

Q

A

G

D

-

K

-

G

-

E

-

I

L

K

K

N

D

I

F

T

A

T

P

G

G

E

K

T

P

I

L

T

K

C

C

active site: A641 (≠ S65), R643 (= R67)
binding citrate anion: A641 (≠ S65), S642 (= S66), R643 (= R67)

Sites not aligning to the query:

active site: 99, 100, 164, 446
binding citrate anion: 71, 100, 164, 165, 446, 451, 579
binding oxygen atom: 164, 166
binding iron/sulfur cluster: 100, 164, 166, 356, 357, 420, 423

P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
38% identity, 40% coverage: 55:120/166 of query aligns to 661:728/789 of P39533

query
sites
P39533

M

V

V

I

A

A

D

E

E

H

N

N

F

Y

G

G

C

E

G

G

S

S

S

A

R

R

E

E

H

H

A

A

P

A

I

L

S

S

I

P

L

R

G

F

A

L

G

G

I

G

P

E

V

I

V

L

A

V

H

K

S

S

F

F

A

A

R

R

I

I

F

H

Y

E

R

T

N

N

G

L

F

K

N

K

M

Q

G

G

L

V

I

L

L

P

L

L

E

T

V

F

G

A

D

N

-

E

-

S

N

D

V

Y

S

D

K

K

I

I

S

S

D

S

G

G

D

D

E

V

L

L

E

E

V

T

Sites not aligning to the query:

610 K→R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.

P19414 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
31% identity, 54% coverage: 31:120/166 of query aligns to 622:723/778 of P19414

query
sites
P19414

E

E

E

N

L

K

G

K

A

A

N

N

C

C

M

V

E

K

G

N

L

V

E

Y

H

T

G

G

W

E

I

Y

K

K

R

G

V

V

K

P

K

D

N

T

D

A

-

R

-

D

-

Y

-

R

-

D

-

Q

-

G

-

I

-

K

-

W

I

V

M

V

V

I

A

G

D

D

E

E

N

N

F

F

G

G

C

E

G

G

S

S

R

R

E

E

H

H

A

A

P

A

I

L

S

E

I

P

L

R

G

F

A

L

G

G

I

G

P

F

V

A

V

I

A

T

H

K

S

S

F

F

A

A

R

R

I

I

F

H

Y

E

R

T

N

N

G

L

F

K

N

K

M

Q

G

G

L

L

I

L

L

P

L

L

E

N

V

F

G

K

D

N

-

P

-

A

N

D

V

Y

S

D

K

K

I

I

S

N

D

P

G

D

D

D

E

R

L

I

E

D

V

I

Sites not aligning to the query:

1:16 modified: transit peptide, Mitochondrion
604 R→K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.

Q9SIB9 Aconitate hydratase 3, mitochondrial; Aconitase 3; mACO1; Citrate hydro-lyase 3; EC 4.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
30% identity, 72% coverage: 47:165/166 of query aligns to 857:990/990 of Q9SIB9

query
sites
Q9SIB9

K

K

R

S

V

S

K

G

K

E

N

D

D

T

I

I

M

I

V

L

A

A

D

G

E

A

N

E

F

Y

G

G

C

S

G

G

S

S

R

R

E

D

H

W

A

A

P

A

I

K

S

G

I

P

L

M

G

L

A

Q

G

G

I

V

P

K

V

A

V

V

V

I

A

A

H

K

S

S

F

F

A

E

R

R

I

I

F

H

Y

R

R

S

N

N

G

L

F

V

N

G

M

M

G

G

L

I

I

I

L

P

L

L

-

C

-

F

E

K

V

S

G

G

D

E

N

D

V

A

S

D

K

T

I

L

S

G

-

L

D

T

G

G

D

H

E

E

-

R

-

Y

-

T

L

I

E

H

V

L

D

P

A

T

D

D

K

I

G

S

E

E

I

I

K

R

-

P

-

G

-

Q

-

D

-

V

N

T

I

V

T

T

-

D

-

N

G

G

E

K

T

S

I

F

T

T

C

C

N

T

P

V

V

R

P

-

F

F

M

D

K

T

E

E

I

V

-

E

-

L

-

A

-

Y

L

F

N

N

S

H

G

G

L

I

V

L

E

P

Y

Y

V

V

K

I

K

R

R

N

L

L

S

S

E

K

R

Q

Sites not aligning to the query:

91 modified: Phosphoserine

Query Sequence

>WP_027180538.1 NCBI__GCF_000429985.1:WP_027180538.1
MTIKGNVHKVGAHIDTDAIIPARFLVTTDPEELGANCMEGLEHGWIKRVKKNDIMVADEN
FGCGSSREHAPISILGAGIPVVVAHSFARIFYRNGFNMGLILLEVGDNVSKISDGDELEV
DADKGEIKNITTGETITCNPVPPFMKEILNSGGLVEYVKKRLSERN

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