SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing AZOBR_RS27810 FitnessBrowser__azobra:AZOBR_RS27810 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 14 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)
48% identity, 94% coverage: 8:203/208 of query aligns to 543:735/758 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)
41% identity, 89% coverage: 9:193/208 of query aligns to 8:185/198 of P9WK95

query
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K154 (≠ T162) 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)
34% identity, 67% coverage: 19:158/208 of query aligns to 13:143/167 of 2pkpA

query
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2pkpA

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binding zinc ion: D13 (≠ N19), C63 (= C80)

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)
34% identity, 67% coverage: 19:158/208 of query aligns to 13:143/170 of Q58667

query
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Q58667

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R26 (≠ L32) 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 (= T33) 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)
41% identity, 27% coverage: 71:126/208 of query aligns to 658:713/780 of P20004

query
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P20004

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SR 670:671 (= SR 83:84) 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)
39% identity, 27% coverage: 71:126/208 of query aligns to 631:686/754 of 5acnA

query
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5acnA

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active site: S642 (= S82), R644 (= R84)
binding tricarballylic acid: R666 (≠ S106)

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

8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
39% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 8acnA

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8acnA

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active site: S641 (= S82), R643 (= R84)
binding nitroisocitric acid: S641 (= S82), S642 (= S83), R643 (= R84)

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)
39% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 1fghA

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active site: S641 (= S82), R643 (= R84)
binding 4-hydroxy-aconitate ion: S641 (= S82), S642 (= S83), R643 (= R84)

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)
39% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 1amjA

query
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active site: S641 (= S82), R643 (= R84)
binding sulfate ion: R643 (= R84)

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)
39% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 1amiA

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active site: S641 (= S82), R643 (= R84)
binding alpha-methylisocitric acid: S641 (= S82), S642 (= S83), R643 (= R84)

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)
39% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 1acoA

query
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A

active site: S641 (= S82), R643 (= R84)
binding aconitate ion: S641 (= S82), S642 (= S83), R643 (= R84)

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

P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
39% identity, 27% coverage: 71:126/208 of query aligns to 658:713/781 of P16276

query
sites
P16276

I

V

L

V

L

I

A

G

G

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

V

A

W

L

S

E

L

P

M

R

D

H

F

L

G

G

I

G

R

R

C

A

V

I

I

I

A

T

P

K

S

S

F

F

A

A

S

R

I

I

F

H

H

E

E

T

N

N

C

L

Q

K

K

K

N

Q

G

G

L

L

A

L

A

P

V

L

T

T

L

F

D

A

E

D

A

P

A

A

SR 670:671 (= SR 83:84) 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)
38% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 1b0kA

query
sites
1b0kA

I

V

L

V

L

I

A

G

G

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

V

A

W

L

S

E

L

P

M

R

D

H

F

L

G

G

I

G

R

R

C

A

V

I

I

I

A

T

P

K

S

S

F

F

A

A

S

R

I

I

F

H

H

E

E

T

N

N

C

L

Q

K

K

K

N

Q

G

G

L

L

A

L

A

P

V

L

T

T

L

F

D

A

E

D

A

P

A

A

active site: A641 (≠ S82), R643 (= R84)
binding citrate anion: A641 (≠ S82), S642 (= S83), R643 (= R84)

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

1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
39% identity, 27% coverage: 71:126/208 of query aligns to 630:685/753 of 1nisA

query
sites
1nisA

I

V

L

V

L

I

A

G

G

D

E

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

R

V

A

W

L

S

E

L

P

M

R

D

F

F

L

G

G

I

G

R

R

C

A

V

I

I

I

A

T

P

K

S

S

F

F

A

A

S

R

I

I

F

H

H

E

E

T

N

N

C

L

Q

K

K

K

N

Q

G

G

L

L

A

L

A

P

V

L

T

T

L

F

D

A

E

D

A

P

A

A

active site: S641 (= S82), R643 (= R84)
binding 2-hydroxy-2-nitromethyl succinic acid: S641 (= S82), S642 (= S83)

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

Query Sequence

>AZOBR_RS27810 FitnessBrowser__azobra:AZOBR_RS27810
MPEPVNRITGIAAPLPRANVDTDAIIPKAHLLTIHRSGLGAGLFSEWRFDDDGRERPDFV
LNQAPWREAKILLAGENFGCGSSREHAVWSLMDFGIRCVIAPSFASIFHENCQKNGLAAV
TLDEAALAHLVACAQATPAATTTVDIKASRVTAPDGREFPFTMEAARRQALLEGLDEIGA
SLRHDAAMAAFEARDRAQRPWIHALPTA

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