SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing 208496 MicrobesOnline__882:208496 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 15 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)
48% identity, 96% coverage: 1:161/167 of query aligns to 1:159/170 of Q58667

query
sites
Q58667

M

M

R

I

Y

I

A

K

G

G

T

R

A

A

H

H

K

K

V

F

G

G

D

D

H

D

I

V

D

D

T

T

D

D

A

A

I

I

P

P

A

G

R

P

F

Y

L

L

V
x
R

T
|
T

T

T

D

D

A

P

Q

Y

K

E

L

L

G

A

E

S

N

H

C

C

M

M

E

A

G

G

L

I

E

D

H

E

G

N

W

F

V

P

A

K

R

K

V

V

K

K

S

E

G

G

D

D

I

V

M

I

V

V

G

A

G

G

R

E

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

H

Q

A

A

P

V

I

I

A

A

I

I

L

K

G

Y

A

C

G

G

M

I

P

K

V

A

V

V

V

I

A

A

H

K

S

S

F

F

A

A

R

R

I

I

F

F

Y

Y

R

R

N

N

G

A

F

I

N

N

M

V

G

G

L

-

L

L

L

I

E

P

V

I

G

I

D

A

D

N

V

T

D

D

K

E

I

I

A

K

D

D

G

G

D

D

-

I

-

V

D

E

I

I

E

D

V

L

D

D

A

K

A

E

S

E

G

I

V

V

I

I

T

T

N

N

R

K

T

N

T

K

G

-

A

-

T

T

I

I

T

K

C

C

A

E

P

T

V

P

P

K

Q

G

S

L

M

E

R

R

E

E

L

I

L

L

D

A

T

A

G

G

L

L

V

V

P

N

Y

Y

V

L

R

K

A

K

R

R

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)
48% identity, 96% coverage: 1:161/167 of query aligns to 1:159/167 of 2pkpA

query
sites
2pkpA

M

M

R

I

Y

I

A

K

G

G

T

R

A

A

H

H

K

K

V

F

G

G

D

D

H
x
D

I

V

D

D

T

T

D

D

A

A

I

I

P

P

A

G

R

P

F

Y

L

L

V

R

T

T

D

D

A

P

Q

Y

K

E

L

L

G

A

E

S

N

H

C

C

M

M

E

A

G

G

L

I

E

D

H

E

G

N

W

F

V

P

A

K

R

K

V

V

K

K

S

E

G

G

D

D

I

V

M

I

V

V

G

A

G

G

R

E

N

N

F

F

G

G

C
|
C

G

G

S

S

R

R

E

E

H

Q

A

A

P

V

I

I

A

A

I

I

L

K

G

Y

A

C

G

G

M

I

P

K

V

A

V

V

V

I

A

A

H

K

S

S

F

F

A

A

R

R

I

I

F

F

Y

Y

R

R

N

N

G

A

F

I

N

N

M

V

G

G

L

-

L

L

L

I

E

P

V

I

G

I

D

A

D

N

V

T

D

D

K

E

I

I

A

K

D

D

G

G

D

D

-

I

-

V

D

E

I

I

E

D

V

L

D

D

A

K

A

E

S

E

G

I

V

V

I

I

T

T

N

N

R

K

T

N

T

K

G

-

A

-

T

T

I

I

T

K

C

C

A

E

P

T

V

P

P

K

Q

G

S

L

M

E

R

R

E

E

L

I

L

L

D

A

T

A

G

G

L

L

V

V

P

N

Y

Y

V

L

R

K

A

K

R

R

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)
34% identity, 69% coverage: 13:128/167 of query aligns to 554:685/758 of O14289

query
sites
O14289

H

N

I

V

D

D

T

T

D

D

A

K

I

I

P

P

A

K

R

Q

F

F

L

L

V

K

T

T

T

I

D

K

A

R

Q

T

K

G

L

L

G

G

E

Q

N

F

C

A

M

F

E

Y

G

E

L

I

E

R

H

Y

G

D

W

A

V

D

A

G

R

K

-

E

-

I

-

P

-

D

-

F

-

V

-

L

-

N

-

R

-

E

-

P

V

Y

K

R

S

H

G

A

D

T

I

V

M

L

V

V

G

A

G

H

R

D

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

H

H

A

A

P

P

I

W

A

A

I

L

L

N

G

D

A

F

G

G

M

I

P

R

V

V

V

I

A

A

H

P

S

S

F

F

A

A

R

D

I

I

F

F

Y

F

R

N

N

N

G

C

F

F

N

K

M

N

G

G

L

M

L

L

-

P

-

I

-

P

-

T

L

P

L

I

E

E

V

Q

G

V

D

N

D

D

V

M

D

M

K

K

I

A

A

A

D

E

G

N

D

Q

-

V

D

K

I

F

E

S

V

V

D

D

A

L

A

V

S

N

G

Q

V

T

I

I

T

T

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)
38% identity, 57% coverage: 13:108/167 of query aligns to 18:118/198 of P9WK95

query
sites
P9WK95

H

N

I

V

D

D

T

T

D

D

A

Q

I

I

P

P

A

A

R

V

F

F

L

L

V

-

T

-

D

-

A

-

Q

K

K

R

L

V

G

T

E

R

N

T

C

G

M

F

E

E

-

D

G

G

L

L

E

F

H

A

G

G

W

W

-

R

-

S

-

D

-

P

-

A

-

F

-

V

-

L

-

N

V

L

A

S

R

P

V

F

K

D

S

R

G

G

D

S

I

V

M

L

V

V

G

A

G

G

R

P

N

D

F

F

G

G

C

T

G

G

S

S

R

R

E

E

H

H

A

A

P

V

I

W

A

A

I

L

L

M

G

D

A

Y

G

G

M

F

P

R

V

V

V

I

A

S

H

S

S

R

F

F

A

G

R

D

I

I

F

F

Y

R

R

G

N

N

G

A

F

G

N

K

M

A

G

G

L

L

L

A

E

E

V

V

G

A

D

Q

D

D

Sites not aligning to the query:

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

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)
41% identity, 40% coverage: 54:120/167 of query aligns to 655:723/778 of P19414

query
sites
P19414

I

V

M

V

V

I

G

G

G

D

R

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

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

N

V

F

G

K

D

N

-

P

-

A

D

D

V

Y

D

D

K

K

I

I

A

N

D

P

G

D

D

D

D

R

I

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)
28% identity, 67% coverage: 54:165/167 of query aligns to 864:990/990 of Q9SIB9

query
sites
Q9SIB9

I

I

M

I

V

L

G

A

G

G

R

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

A

G

I

P

L

M

G

L

A

Q

G

G

M

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

-

P

L

L

L

C

L

F

E

K

V

S

G

G

D

E

D

D

V

A

D

D

K

T

I

L

A

G

-

L

-

T

-

G

-

H

-

E

-

R

-

Y

-

T

-

I

-

H

-

L

D

P

G

T

D

D

D

I

I

S

E

E

V

I

D

R

A

P

A

G

S

Q

G

D

V

V

I

T

T

V

N

T

R

T

T

D

T

N

G

G

A

K

T

S

I

F

T

T

C

C

A

T

P

V

V

R

P

F

Q

D

S

T

M

E

R

V

E

E

L

L

-

A

-

Y

L

F

D

N

T

H

G

G

L

I

V

L

P

P

Y

Y

V

V

R

I

A

R

R

N

L

L

E

S

R

K

E

Q

Sites not aligning to the query:

91 modified: Phosphoserine

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
33% identity, 51% coverage: 54:138/167 of query aligns to 658:740/780 of P20004

query
sites
P20004

I

V

M

V

V

I

G

G

G

D

R

E

N

N

F

Y

G

G

C

E

G

G

S

S

S
|
S

R
|
R

E

E

H

H

A

A

P

A

I

L

A

E

I

P

L

R

G

H

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

K

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

K

T

P

I

L

T

T

C

C

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

Sites not aligning to the query:

99 binding
192:194 binding
385 binding
448 binding
451 binding
474 binding
479 binding
607 binding

8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
32% identity, 51% coverage: 54:138/167 of query aligns to 630:712/753 of 8acnA

query
sites
8acnA

I

V

M

V

V

I

G

G

G

D

R

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

I

L

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

Q

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

K

T

P

I

L

T

T

C

C

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)
32% identity, 51% coverage: 54:138/167 of query aligns to 630:712/753 of 1fghA

query
sites
1fghA

I

V

M

V

V

I

G

G

G

D

R

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

I

L

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

Q

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

K

T

P

I

L

T

T

C

C

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)
32% identity, 51% coverage: 54:138/167 of query aligns to 630:712/753 of 1amjA

query
sites
1amjA

I

V

M

V

V

I

G

G

G

D

R

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

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

Q

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

K

T

P

I

L

T

T

C

C

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)
32% identity, 51% coverage: 54:138/167 of query aligns to 630:712/753 of 1amiA

query
sites
1amiA

I

V

M

V

V

I

G

G

G

D

R

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

I

L

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

Q

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

K

T

P

I

L

T

T

C

C

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)
32% identity, 51% coverage: 54:138/167 of query aligns to 630:712/753 of 1acoA

query
sites
1acoA

I

V

M

V

V

I

G

G

G

D

R

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

R
|
R

E

E

H

H

A

S

P

A

I

L

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

Q

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

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

5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
36% identity, 40% coverage: 54:120/167 of query aligns to 631:699/754 of 5acnA

query
sites
5acnA

I

V

M

V

V

I

G

G

G

D

R

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

A

E

I

P

L

R

G

H

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

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

1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
32% identity, 51% coverage: 54:138/167 of query aligns to 630:712/753 of 1nisA

query
sites
1nisA

I

V

M

V

V

I

G

G

G

D

R

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

A

E

I

P

L

R

G

F

A

L

G

G

M

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

L

P

L

L

E

T

V

F

G

A

D

D

-

P

-

A

D

D

V

Y

D

N

K

K

I

I

A

H

D

P

G

V

D

D

D

K

I

L

E

T

V

I

D

Q

A

G

A

-

S

-

G

-

V

-

I

L

T

K

N

D

R

F

T

A

T

P

G

G

A

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

P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
37% identity, 39% coverage: 55:119/167 of query aligns to 661:727/789 of P39533

query
sites
P39533

M

V

V

I

G

A

G

E

R

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

A

S

I

P

L

R

G

F

A

L

G

G

M

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

L

L

L

P

L

L

E

T

V

F

G

A

D

N

-

E

-

S

D

D

V

Y

D

D

K

K

I

I

A

S

D

S

G

G

D

D

D

V

I

L

E

E

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

>208496 MicrobesOnline__882:208496
MRYAGTAHKVGDHIDTDAIIPARFLVTTDAQKLGENCMEGLEHGWVARVKSGDIMVGGRN
FGCGSSREHAPIAILGAGMPVVVAHSFARIFYRNGFNMGLLLLEVGDDVDKIADGDDIEV
DAASGVITNRTTGATITCAPVPQSMRELLDTGGLVPYVRARLERENG

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