SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing CA265_RS15840 FitnessBrowser__Pedo557:CA265_RS15840 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)

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)
44% identity, 99% coverage: 1:194/195 of query aligns to 537:727/758 of O14289

query
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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)
42% identity, 98% coverage: 1:191/195 of query aligns to 1:184/198 of P9WK95

query
sites
P9WK95

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

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)
42% identity, 52% coverage: 17:118/195 of query aligns to 12:103/170 of Q58667

query
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Q58667

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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 (≠ A32) 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)
42% identity, 52% coverage: 17:118/195 of query aligns to 12:103/167 of 2pkpA

query
sites
2pkpA

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binding zinc ion: D13 (≠ N18), C63 (= C78)

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
32% identity, 49% coverage: 69:163/195 of query aligns to 658:755/780 of P20004

query
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P20004

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SR 670:671 (= SR 81:82) 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)
41% identity, 28% coverage: 69:122/195 of query aligns to 631:684/754 of 5acnA

query
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5acnA

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active site: S642 (= S80), R644 (= R82)
binding tricarballylic acid: R666 (≠ D104)

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)
41% identity, 28% coverage: 69:122/195 of query aligns to 658:711/781 of P16276

query
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P16276

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SR 670:671 (= SR 81:82) 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

P09339 Aconitate hydratase A; ACN; Aconitase; Aconitate/2-methylaconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.- from Bacillus subtilis (strain 168) (see 2 papers)
41% identity, 28% coverage: 66:119/195 of query aligns to 778:831/909 of P09339

query
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P09339

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Sites not aligning to the query:

1 modified: Initiator methionine, Removed
450 C→S: Loss of aconitase activity. It is glutamate auxotroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of inactive aconitase.
741 R→E: Same aconitase activity compared to the wild-type. It is glutamate prototroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of active aconitase.

1b0kA S642a:fluorocitrate complex of aconitase (see paper)
39% identity, 28% coverage: 69:122/195 of query aligns to 630:683/753 of 1b0kA

query
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active site: A641 (≠ S80), R643 (= R82)
binding citrate anion: A641 (≠ S80), S642 (= S81), R643 (= R82)

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)
31% identity, 49% coverage: 69:163/195 of query aligns to 630:727/753 of 8acnA

query
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8acnA

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active site: S641 (= S80), R643 (= R82)
binding nitroisocitric acid: S641 (= S80), S642 (= S81), R643 (= R82)

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)
31% identity, 49% coverage: 69:163/195 of query aligns to 630:727/753 of 1fghA

query
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1fghA

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T

V

F

S

A

D

D

E

P

F

A

L

D

A

Y

Q

N

I

K

F

I

K

H

A

P

V

V

D

D

N

K

N

L

P

T

K

I

S

Q

A

G

L

L

E

K

V

D

D

F

L

A

E

P

N

G

Q

K

T

P

V

L

T

T

I

C

V

I

-

I

-

K

-

H

E

P

T

N

G

G

A

T

Q

Q

E

E

S

T

F

I

E

L

I

L

N

N

active site: S641 (= S80), R643 (= R82)
binding 4-hydroxy-aconitate ion: S641 (= S80), S642 (= S81), R643 (= R82)

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)
31% identity, 49% coverage: 69:163/195 of query aligns to 630:727/753 of 1amjA

query
sites
1amjA

V

V

L

V

V

I

A

G

G

D

K

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

S

S

R
|
R

E

E

H

H

A

S

A

A

W

L

A

E

I

P

Q

R

D

F

A

L

G

G

F

G

D

R

A

A

V

I

I

I

S

T

S

K

F

S

F

F

A

A

D

R

I

I

F

H

K

E

G

T

N

N

A

L

L

K

N

K

N

Q

G

G

L

L

P

P

I

L

Q

T

V

F

S

A

D

D

E

P

F

A

L

D

A

Y

Q

N

I

K

F

I

K

H

A

P

V

V

D

D

N

K

N

L

P

T

K

I

S

Q

A

G

L

L

E

K

V

D

D

F

L

A

E

P

N

G

Q

K

T

P

V

L

T

T

I

C

V

I

-

I

-

K

-

H

E

P

T

N

G

G

A

T

Q

Q

E

E

S

T

F

I

E

L

I

L

N

N

active site: S641 (= S80), R643 (= R82)
binding sulfate ion: R643 (= R82)

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)
31% identity, 49% coverage: 69:163/195 of query aligns to 630:727/753 of 1amiA

query
sites
1amiA

V

V

L

V

V

I

A

G

G

D

K

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

A

A

W

L

A

E

I

P

Q

R

D

F

A

L

G

G

F

G

D

R

A

A

V

I

I

I

S

T

S

K

F

S

F

F

A

A

D

R

I

I

F

H

K

E

G

T

N

N

A

L

L

K

N

K

N

Q

G

G

L

L

P

P

I

L

Q

T

V

F

S

A

D

D

E

P

F

A

L

D

A

Y

Q

N

I

K

F

I

K

H

A

P

V

V

D

D

N

K

N

L

P

T

K

I

S

Q

A

G

L

L

E

K

V

D

D

F

L

A

E

P

N

G

Q

K

T

P

V

L

T

T

I

C

V

I

-

I

-

K

-

H

E

P

T

N

G

G

A

T

Q

Q

E

E

S

T

F

I

E

L

I

L

N

N

active site: S641 (= S80), R643 (= R82)
binding alpha-methylisocitric acid: S641 (= S80), S642 (= S81), R643 (= R82)

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)
31% identity, 49% coverage: 69:163/195 of query aligns to 630:727/753 of 1acoA

query
sites
1acoA

V

V

L

V

V

I

A

G

G

D

K

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

A

A

W

L

A

E

I

P

Q

R

D

F

A

L

G

G

F

G

D

R

A

A

V

I

I

I

S

T

S

K

F

S

F

F

A

A

D

R

I

I

F

H

K

E

G

T

N

N

A

L

L

K

N

K

N

Q

G

G

L

L

P

P

I

L

Q

T

V

F

S

A

D

D

E

P

F

A

L

D

A

Y

Q

N

I

K

F

I

K

H

A

P

V

V

D

D

N

K

N

L

P

T

K

I

S

Q

A

G

L

L

E

K

V

D

D

F

L

A

E

P

N

G

Q

K

T

P

V

L

T

T

I

C

V

I

-

I

-

K

-

H

E

P

T

N

G

G

A

T

Q

Q

E

E

S

T

F

I

E

L

I

L

N

N

active site: S641 (= S80), R643 (= R82)
binding aconitate ion: S641 (= S80), S642 (= S81), R643 (= R82)

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

D9X0I3 Aconitate hydratase A; ACN; Aconitase; EC 4.2.1.3 from Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) (see paper)
41% identity, 26% coverage: 69:119/195 of query aligns to 805:855/931 of D9X0I3

query
sites
D9X0I3

V

V

L

V

V

L

A

A

G

G

K

K

N

E

F

Y

G

G

C

S

G

G

S

S

R

R

E

D

H

W

A

A

W

K

A

G

I

T

Q

A

D

L

A

L

G

G

F

V

D

K

A

A

V

V

I

I

S

A

S

E

F

S

F

Y

A

E

D

R

I

I

F

H

K

R

G

S

N

N

A

L

L

I

N

G

N

M

G

G

L

V

L

L

P

P

I

L

Q

Q

Sites not aligning to the query:

125:129 mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
538 C→A: Loss of aconitase activity. Cannot rescue the growth defect of a disruption mutant and results in only a slight increase in PTT production in the mutant. Shows weak IRE-binding activity.
763 R→E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
767 Q→E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.

1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
31% identity, 49% coverage: 69:163/195 of query aligns to 630:727/753 of 1nisA

query
sites
1nisA

V

V

L

V

V

I

A

G

G

D

K

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

R

A

A

W

L

A

E

I

P

Q

R

D

F

A

L

G

G

F

G

D

R

A

A

V

I

I

I

S

T

S

K

F

S

F

F

A

A

D

R

I

I

F

H

K

E

G

T

N

N

A

L

L

K

N

K

N

Q

G

G

L

L

P

P

I

L

Q

T

V

F

S

A

D

D

E

P

F

A

L

D

A

Y

Q

N

I

K

F

I

K

H

A

P

V

V

D

D

N

K

N

L

P

T

K

I

S

Q

A

G

L

L

E

K

V

D

D

F

L

A

E

P

N

G

Q

K

T

P

V

L

T

T

I

C

V

I

-

I

-

K

-

H

E

P

T

N

G

G

A

T

Q

Q

E

E

S

T

F

I

E

L

I

L

N

N

active site: S641 (= S80), R643 (= R82)
binding 2-hydroxy-2-nitromethyl succinic acid: S641 (= S80), S642 (= S81)

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

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)
46% identity, 26% coverage: 69:118/195 of query aligns to 655:704/778 of P19414

query
sites
P19414

V

V

L

V

V

I

A

G

G

D

K

E

N

N

F

F

G

G

C

E

G

G

S

S

R

R

E

E

H

H

A

A

W

L

A

E

I

P

Q

R

D

F

A

L

G

G

F

G

D

F

A

A

V

I

I

I

S

T

S

K

F

S

F

F

A

A

D

R

I

I

F

H

K

E

G

T

N

N

A

L

L

K

N

K

N

Q

G

G

L

L

P

P

I

L

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.

Query Sequence

>CA265_RS15840 FitnessBrowser__Pedo557:CA265_RS15840
MKKFTKLTSAVVPLNIENIDTDQIIPARFLKATTREGFGENLFRDWRYENDNQPKADFVM
NNPTYSGQVLVAGKNFGCGSSREHAAWAIQDAGFDAVISSFFADIFKGNALNNGLLPIQV
SDEFLAQIFKAVDNNPKSALEVDLENQTVTIVETGAQESFEINPYKKSCLINGYDDIDFI
LNQKQLIEEFEEGRR

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