SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF2540 Psest_2590 3-isopropylmalate dehydratase, small subunit 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)
56% identity, 96% coverage: 4:210/215 of query aligns to 540:734/758 of O14289

query
sites
O14289

F

F

T

T

Q

V

H

V

T

E

G

G

L

I

V

A

C

A

P

P

L

L

D

P

R

M

A

A

N

N

V

V

D

D

T

T

D

D

Q

K

I

I

P

P

K

K

Q

Q

F

F

L

L

K

K

S

T

I

I

K

K

R

R

T

T

G

G

F

L

G

G

P

Q

N

F

L

A

F

F

D

Y

E

E

W

I

R

R

Y

Y

L

-

D

-

V

-

G

-

Q

-

P

-

N

D

Q

A

D

D

C

G

S

K

Q

E

R

I

P

P

V

-

N

-

K

-

D

D

F

F

V

V

L

L

N

N

F

R

P

E

R

P

Y

Y

R

R

G

H

A

A

S

T

V

V

L

L

L

V

A

A

R

H

E

D

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

H

H

A

A

P

P

W

W

A

A

L

L

E

N

E

D

Y

F

G

G

F

I

R

R

T

V

I

I

A

A

P

P

S

S

F

F

A

A

D

D

I

I

F

F

Y

F

N

N

S

C

F

F

K

K

N

N

G

G

L

M

L

L

P

P

I

I

V

P

L

T

K

P

E

I

E

E

E

Q

V

V

D

N

E

D

L

M

F

M

A

K

Q

A

A

A

E

E

A

N

S

Q

E

-

G

-

Y

V

Q

K

L

F

T

S

V

V

D

D

L

L

A

V

A

N

Q

Q

V

T

V

I

T

T

R

Y

P

G

D

D

G

-

K

K

Q

Q

Y

V

S

K

F

F

E

D

V

V

D

E

A

P

F

F

R

R

K

K

H

H

C

C

L

L

L

V

N

N

G

G

L

L

D

D

I

I

G

G

L

L

T

T

L

L

Q

Q

D

K

A

E

E

T

A

M

I

I

K

D

T

A

F

F

E

E

A

A

R

A

H

R

Q

E

N

N

Q

F

P

P

W

W

L

M

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, 97% coverage: 1:208/215 of query aligns to 1:192/198 of P9WK95

query
sites
P9WK95

M

M

K

E

A

A

F

F

T

H

Q

T

H

H

T

S

G

G

L

I

V

G

C

V

P

P

L

L

D

R

R

R

A

S

N

N

V

V

D

D

T

T

D

D

Q

Q

I

I

P

P

K

A

Q

V

F

F

L

L

K

K

S

R

I

V

K

T

R

R

T

T

G

G

F

F

G

E

P

D

N

G

L

L

F

F

D

A

E

G

W

W

R

R

Y

S

L

-

D

-

V

-

G

-

Q

-

P

-

N

-

Q

-

D

-

C

-

S

-

Q

-

R

-

P

-

V

-

N

D

K

P

D

A

F

F

V

V

L

L

N

N

F

L

P

S

R

P

Y

F

R

D

G

R

A

G

S

S

V

V

L

L

L

V

A

A

R

G

E

P

N

D

F

F

G

G

C

T

G

G

S

S

R

R

E

E

H

H

A

A

P

V

W

W

A

A

L

L

E

M

E

D

Y

Y

G

G

F

F

R

R

T

V

I

V

I

I

A

S

P

S

S

R

F

F

A

G

D

D

I

I

F

F

Y

R

N

G

N

N

S

A

F

G

K

K

N

A

G

G

L

L

P

A

I

A

V

E

L

V

K

A

E

Q

E

D

V

V

D

E

E

L

L

L

F

W

A

K

Q

L

A

I

E

E

A

Q

S

S

E

P

G

G

Y

L

Q

E

L

I

T

T

V

A

D

N

L

L

A

Q

A

D

Q

R

V

I

T

T

R

A

P

A

D

T

G

-

K

V

Q

V

Y

L

S

P

F

F

E
x
K

V

I

D

D

A

D

F

H

R

S

K

A

H

W

C

R

L

L

N

E

G

G

L

L

D

D

I

I

G

A

L

L

T

T

L

L

Q

R

D

K

A

L

E

D

A

E

I

I

K

E

T

A

F

F

E

E

A

G

R

A

H

C

Q

A

Q

Y

N

W

Q

K

P

P

K154 (≠ E170) 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)
38% identity, 56% coverage: 18:137/215 of query aligns to 13:112/170 of Q58667

query
sites
Q58667

N

D

V

V

D

D

T

T

D

D

Q

A

I

I

P

P

K

-

Q

-

F

-

L

-

K

-

S

-

I

-

K

-

R

-

T

-

G

-

F

-

G

G

P

P

N

-

L

-

F

-

D

-

E

-

W

-

R

-

Y

Y

L

L

D
x
R

V
x
T

G

T

Q

D

P

P

N

Y

Q

E

D

L

C

A

S

S

Q

H

R

C

P

M

V

A

N

G

K

I

D

D

F

E

V

-

L

-

N

N

F

F

P

P

R

K

-

K

Y

V

R

K

G

E

A

G

S

D

V

V

L

I

L

V

A

A

R

G

E

E

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

H

Q

A

A

P

V

W

I

A

A

L

I

E

K

E

Y

Y

C

G

G

F

I

R

K

T

A

I

V

I

I

A

A

P

K

S

S

F

F

A

A

D

R

I

I

F

F

Y

Y

N

R

N

N

S

A

F

I

K

N

N

V

G

G

L

L

L

I

P

P

I

I

V

I

L

A

K

N

E

T

E

D

E

E

V

I

D

K

E

D

R26 (≠ D50) 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 (≠ V51) 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)
38% identity, 56% coverage: 18:137/215 of query aligns to 13:112/167 of 2pkpA

query
sites
2pkpA

N
x
D

V

V

D

D

T

T

D

D

Q

A

I

I

P

P

K

-

Q

-

F

-

L

-

K

-

S

-

I

-

K

-

R

-

T

-

G

-

F

-

G

G

P

P

N

-

L

-

F

-

D

-

E

-

W

-

R

-

Y

Y

L

L

D

R

V

T

G

T

Q

D

P

P

N

Y

Q

E

D

L

C

A

S

S

Q

H

R

C

P

M

V

A

N

G

K

I

D

D

F

E

V

-

L

-

N

N

F

F

P

P

R

K

-

K

Y

V

R

K

G

E

A

G

S

D

V

V

L

I

L

V

A

A

R

G

E

E

N

N

F

F

G

G

C
|
C

G

G

S

S

R

R

E

E

H

Q

A

A

P

V

W

I

A

A

L

I

E

K

E

Y

Y

C

G

G

F

I

R

K

T

A

I

V

I

I

A

A

P

K

S

S

F

F

A

A

D

R

I

I

F

F

Y

Y

N

R

N

N

S

A

F

I

K

N

N

V

G

G

L

L

L

I

P

P

I

I

V

I

L

A

K

N

E

T

E

D

E

E

V

I

D

K

E

D

binding zinc ion: D13 (≠ N18), C63 (= C88)

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
31% identity, 50% coverage: 79:186/215 of query aligns to 658:778/780 of P20004

query
sites
P20004

V

V

L

V

L

I

A

G

R

D

E

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

W

L

A

E

L

P

E

R

E

H

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

K

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

SR 670:671 (= SR 91:92) 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)
31% identity, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 8acnA

query
sites
8acnA

V

V

L

V

L

I

A

G

R

D

E

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

E

R

E

F

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S641 (= S90), R643 (= R92)
binding nitroisocitric acid: S641 (= S90), S642 (= S91), R643 (= R92)

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, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 1fghA

query
sites
1fghA

V

V

L

V

L

I

A

G

R

D

E

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

E

R

E

F

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S641 (= S90), R643 (= R92)
binding 4-hydroxy-aconitate ion: S641 (= S90), S642 (= S91), R643 (= R92)

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, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 1amjA

query
sites
1amjA

V

V

L

V

L

I

A

G

R

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

W

L

A

E

L

P

E

R

E

F

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S641 (= S90), R643 (= R92)
binding sulfate ion: R643 (= R92)

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, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 1amiA

query
sites
1amiA

V

V

L

V

L

I

A

G

R

D

E

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

E

R

E

F

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S641 (= S90), R643 (= R92)
binding alpha-methylisocitric acid: S641 (= S90), S642 (= S91), R643 (= R92)

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, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 1acoA

query
sites
1acoA

V

V

L

V

L

I

A

G

R

D

E

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

E

R

E

F

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S641 (= S90), R643 (= R92)
binding aconitate ion: S641 (= S90), S642 (= S91), R643 (= R92)

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)
30% identity, 50% coverage: 79:186/215 of query aligns to 631:751/754 of 5acnA

query
sites
5acnA

V

V

L

V

L

I

A

G

R

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

W

L

A

E

L

P

E

R

E

H

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D
x
R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

K

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S642 (= S90), R644 (= R92)
binding tricarballylic acid: R666 (≠ D114)

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)
31% identity, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 1nisA

query
sites
1nisA

V

V

L

V

L

I

A

G

R

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

W

L

A

E

L

P

E

R

E

F

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

T

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: S641 (= S90), R643 (= R92)
binding 2-hydroxy-2-nitromethyl succinic acid: S641 (= S90), S642 (= S91)

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

P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
30% identity, 50% coverage: 79:186/215 of query aligns to 658:778/781 of P16276

query
sites
P16276

V

V

L

V

L

I

A

G

R

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

W

L

A

E

L

P

E

R

E

H

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

K

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

SR 670:671 (= SR 91:92) binding

Sites not aligning to the query:

28 modified: Pyrrolidone carboxylic acid
99 binding
192:194 binding
385 binding
448 binding
451 binding
474 binding
479 binding
607 binding

1b0kA S642a:fluorocitrate complex of aconitase (see paper)
29% identity, 50% coverage: 79:186/215 of query aligns to 630:750/753 of 1b0kA

query
sites
1b0kA

V

V

L

V

L

I

A

G

R

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

W

L

A

E

L

P

E

R

E

H

Y

L

G

G

F

G

R

R

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

T

L

F

-

A

-

D

-

P

-

A

-

D

-

Y

-

N

K

K

E

I

E

H

E

P

V

V

D

D

E

K

L

L

F

T

A

I

Q

Q

A

G

-

L

-

K

E

D

A

F

S

A

E

P

G

G

Y

K

Q

P

L

L

T

K

V

C

D

-

L

-

A

-

Q

-

V

I

T

K

R

H

P

P

D

N

G

G

K

T

Q

Q

Y

E

S

T

F

I

-

L

-

N

-

H

-

T

-

F

-

N

-

E

-

T

E

Q

V

I

D

E

A

W

F

F

R

R

K

A

H

G

C

S

L

A

L

L

N

N

G

R

L

M

D

K

D

E

I

L

active site: A641 (≠ S90), R643 (= R92)
binding citrate anion: A641 (≠ S90), S642 (= S91), R643 (= R92)

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)
25% identity, 50% coverage: 79:186/215 of query aligns to 660:785/789 of P39533

query
sites
P39533

V

T

L

V

L

I

A

A

R

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

W

L

A

S

L

P

E

R

E

F

Y

L

G

G

F

G

R

E

T

I

I

L

A

V

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

V

L

L

P

P

I

L

V

T

L

F

K

A

E

N

E

E

E

S

V

D

D

Y

E

D

L

K

F

I

A

S

Q

S

A

G

E

D

A

V

S

L

E

E

G

T

Y

L

Q

N

L

L

T

-

V

V

D

D

L

M

A

I

A

A

Q

K

-

D

-

G

-

N

-

G

-

E

-

I

-

D

-

V

V

K

V

I

T

T

R

K

P

P

D

N

G

G

K

E

Q

S

Y

F

S

T

F

I

-

K

-

A

-

K

-

H

-

T

-

M

-

S

-

K

-

D

E

Q

V

I

D

D

A

F

F

F

R

K

K

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.

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)
49% identity, 25% coverage: 79:131/215 of query aligns to 655:707/778 of P19414

query
sites
P19414

V

V

L

V

L

I

A

G

R

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

W

L

A

E

L

P

E

R

E

F

Y

L

G

G

F

G

R

F

T

A

I

I

A

T

P

K

S

S

F

F

A

A

D

R

I

I

F

H

Y

E

N

T

N

N

S

L

F

K

K

K

N

Q

G

G

L

L

P

P

I

L

V

N

L

F

K

K

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.

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)
35% identity, 32% coverage: 66:134/215 of query aligns to 768:836/909 of P09339

query
sites
P09339

D

D

F

A

V

C

L

M

N

K

F

Y

P

K

R

E

Y

D

R

K

G

T

A

G

S

L

V

V

L

V

L

L

A

A

R

G

E

K

N

D

F

Y

G

G

C

M

G

G

S

S

R

R

E

D

H

W

A

A

P

A

W

K

A

G

L

T

E

N

E

L

Y

L

G

G

F

I

R

R

T

T

I

V

I

I

A

A

P

E

S

S

F

F

A

E

D

R

I

I

F

H

Y

R

N

S

N

N

S

L

F

V

K

F

N

M

G

G

L

V

L

L

P

P

I

L

V

Q

L

F

K

K

E

Q

E

G

E

E

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.

Query Sequence

>GFF2540 Psest_2590 3-isopropylmalate dehydratase, small subunit
MKAFTQHTGLVCPLDRANVDTDQIIPKQFLKSIKRTGFGPNLFDEWRYLDVGQPNQDCSQ
RPVNKDFVLNFPRYRGASVLLARENFGCGSSREHAPWALEEYGFRTIIAPSFADIFYNNS
FKNGLLPIVLKEEEVDELFAQAEASEGYQLTVDLAAQVVTRPDGKQYSFEVDAFRKHCLL
NGLDDIGLTLQDAEAIKTFEARHQQNQPWLFGAIK

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