SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_012709642.1 NCBI__GCF_000018545.1:WP_012709642.1 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 16 hits to proteins with known functional sites (download)

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)
57% identity, 99% coverage: 3:200/201 of query aligns to 539:733/758 of O14289

query
sites
O14289

K

K

F

F

V

T

K

V

L

V

T

E

G

G

V

I

A

A

P

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D

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W

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)
42% identity, 99% coverage: 1:199/201 of query aligns to 1:192/198 of P9WK95

query
sites
P9WK95

M

M

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-

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P

K154 (≠ E161) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
37% identity, 67% coverage: 18:151/201 of query aligns to 13:126/167 of 2pkpA

query
sites
2pkpA

N
x
D

I

V

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D

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binding zinc ion: D13 (≠ N18), C63 (= C79)

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)
37% identity, 67% coverage: 18:151/201 of query aligns to 13:126/170 of Q58667

query
sites
Q58667

N

D

I

V

D

D

T

T

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D

M

A

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D

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x
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T

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R26 (≠ K31) 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 (= T32) 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.

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
35% identity, 38% coverage: 54:129/201 of query aligns to 642:718/780 of P20004

query
sites
P20004

P

P

N

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D

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SR 670:671 (= SR 82:83) 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

5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
34% identity, 38% coverage: 54:129/201 of query aligns to 615:691/754 of 5acnA

query
sites
5acnA

P

P

N

V

P

P

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x
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active site: S642 (= S81), R644 (= R83)
binding tricarballylic acid: R666 (≠ D105)

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)
34% identity, 38% coverage: 54:129/201 of query aligns to 642:718/781 of P16276

query
sites
P16276

P

P

N

V

P

P

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D

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SR 670:671 (= SR 82:83) 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

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)
45% identity, 33% coverage: 66:132/201 of query aligns to 650:718/778 of P19414

query
sites
P19414

Q

Q

N

G

A

I

K

K

I

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L

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N

N

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D

D

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.

1b0kA S642a:fluorocitrate complex of aconitase (see paper)
32% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 1b0kA

query
sites
1b0kA

P

P

N

V

P

P

D

D

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N

N

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G

G

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E

H

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A

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A

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S

S

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A

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F

H

Y

E

N

T

N

N

C

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F

K

K

K

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G

G

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L

L

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P

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A

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D

L

Y

D

N

K

K

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I

active site: A641 (≠ S81), R643 (= R83)
binding citrate anion: A641 (≠ S81), S642 (= S82), R643 (= R83)

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

8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
34% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 8acnA

query
sites
8acnA

P

P

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V

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P

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D

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A

G

G

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E

N

N

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G

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H

H

A

S

P

A

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A

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F

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T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

V

F

S

A

Q

D

-

P

A

A

D

D

L

Y

D

N

K

K

L

I

active site: S641 (= S81), R643 (= R83)
binding nitroisocitric acid: S641 (= S81), S642 (= S82), R643 (= R83)

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)
34% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 1fghA

query
sites
1fghA

P

P

N

V

P

P

D

D

F

T

V

A

L

R

N

Y

K

Y

P

K

A

Q

Y

H

Q

G

N

I

A

R

K

W

I

V

L

V

V

I

A

G

G

D

D

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

W

L

A

E

L

P

L

R

D

F

F

L

G

G

I

G

R

R

C

A

V

I

I

I

S

T

T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

V

F

S

A

Q

D

-

P

A

A

D

D

L

Y

D

N

K

K

L

I

active site: S641 (= S81), R643 (= R83)
binding 4-hydroxy-aconitate ion: S641 (= S81), S642 (= S82), R643 (= R83)

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)
34% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 1amjA

query
sites
1amjA

P

P

N

V

P

P

D

D

F

T

V

A

L

R

N

Y

K

Y

P

K

A

Q

Y

H

Q

G

N

I

A

R

K

W

I

V

L

V

V

I

A

G

G

D

D

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

W

L

A

E

L

P

L

R

D

F

F

L

G

G

I

G

R

R

C

A

V

I

I

I

S

T

T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

V

F

S

A

Q

D

-

P

A

A

D

D

L

Y

D

N

K

K

L

I

active site: S641 (= S81), R643 (= R83)
binding sulfate ion: R643 (= R83)

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)
34% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 1amiA

query
sites
1amiA

P

P

N

V

P

P

D

D

F

T

V

A

L

R

N

Y

K

Y

P

K

A

Q

Y

H

Q

G

N

I

A

R

K

W

I

V

L

V

V

I

A

G

G

D

D

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

W

L

A

E

L

P

L

R

D

F

F

L

G

G

I

G

R

R

C

A

V

I

I

I

S

T

T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

V

F

S

A

Q

D

-

P

A

A

D

D

L

Y

D

N

K

K

L

I

active site: S641 (= S81), R643 (= R83)
binding alpha-methylisocitric acid: S641 (= S81), S642 (= S82), R643 (= R83)

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)
34% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 1acoA

query
sites
1acoA

P

P

N

V

P

P

D

D

F

T

V

A

L

R

N

Y

K

Y

P

K

A

Q

Y

H

Q

G

N

I

A

R

K

W

I

V

L

V

V

I

A

G

G

D

D

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

W

L

A

E

L

P

L

R

D

F

F

L

G

G

I

G

R

R

C

A

V

I

I

I

S

T

T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

V

F

S

A

Q

D

-

P

A

A

D

D

L

Y

D

N

K

K

L

I

active site: S641 (= S81), R643 (= R83)
binding aconitate ion: S641 (= S81), S642 (= S82), R643 (= R83)

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)
34% identity, 38% coverage: 54:129/201 of query aligns to 614:690/753 of 1nisA

query
sites
1nisA

P

P

N

V

P

P

D

D

F

T

V

A

L

R

N

Y

K

Y

P

K

A

Q

Y

H

Q

G

N

I

A

R

K

W

I

V

L

V

V

I

A

G

G

D

D

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

R

P

A

W

L

A

E

L

P

L

R

D

F

F

L

G

G

I

G

R

R

C

A

V

I

I

I

S

T

T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

V

F

S

A

Q

D

-

P

A

A

D

D

L

Y

D

N

K

K

L

I

active site: S641 (= S81), R643 (= R83)
binding 2-hydroxy-2-nitromethyl succinic acid: S641 (= S81), S642 (= S82)

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

P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
29% identity, 65% coverage: 48:177/201 of query aligns to 636:785/789 of P39533

query
sites
P39533

Y

Y

N

D

E

L

D

D

G

G

T

T

P

E

N

Y

-

D

-

I

P

P

D

G

F

L

V

M

L

M

N

K

K

W

P

K

A

S

Y

D

Q

G

N

R

A

P

K

W

I

T

L

V

V

I

A

A

G

E

D

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

W

L

A

S

L

P

L

R

D

F

F

L

G

G

I

G

R

E

C

I

V

L

I

L

S

V

T

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

V

L

L

P

P

I

L

V

T

-

F

V

A

S

N

Q

E

A

S

D

D

L

Y

D

D

K

K

-

I

-

S

-

G

-

D

-

V

-

L

-

E

-

T

-

L

-

N

L

L

M

V

D

D

D

M

A

I

N

A

R

K

G

D

S

G

N

N

A

N

V

G

L

G

S

E

I

I

D

D

L

V

E

-

A

-

Q

-

E

K

I

I

T

T

G

K

P

P

D

N

G

G

G

E

S

S

I

F

-

T

-

I

-

K

-

A

-

K

-

H

-

T

-

M

-

S

K

K

F

D

E

Q

I

I

D

D

A

F

F

F

K

K

R

A

H

G

C

S

L

A

L

I

N

N

G

Y

L

I

D

G

D

N

I

I

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.

Query Sequence

>WP_012709642.1 NCBI__GCF_000018545.1:WP_012709642.1
MDKFVKLTGVAAPLPVVNIDTDMIIPKDYLKTIKRTGLGTGLFAEARYNEDGTPNPDFVL
NKPAYQNAKILVAGDNFGCGSSREHAPWALLDFGIRCVISTSFADIFYNNCFKNGILPIV
VSQADLDKLMDDANRGSNAVLSIDLEAQEITGPDGGSIKFEIDAFKRHCLLNGLDDIGLT
LEKAGAIDTFEKSTAASRPWA

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