SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF1851 PS417_09415 3-isopropylmalate dehydratase 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 6 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)
45% identity, 98% coverage: 6:204/204 of query aligns to 540:735/758 of O14289

query
sites
O14289

F

F

T

T

L

V

V

V

T

E

G

G

K

I

A

A

P

P

M

L

L

P

A

M

A

A

N

N

I

V

D

D

T

T

D

D

V

K

I

I

M

I

P

P

K

K

Q

Q

F

F

L

L

K

K

G

T

I

I

D

K

R

R

S

T

G

G

L

L

D

G

R

Q

G

F

L

A

F

F

F

Y

D

E

L

I

R

R

F

Y

L

D

S

A

S

D

G

G

E

K

P

E

N

I

P

P

E

D

F

F

V

V

L

L

N

N

Q

R

P

E

A

P

W

Y

Q

R

G

H

A

A

S

T

F

V

M

L

V

V

V

A

G

H

P

D

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

H

H

A

A

V

P

W

W

G

A

L

L

K

N

Q

D

M

F

G

G

I

I

R

R

A

V

L

I

I

I

G

A

S

P

S

S

F

F

A

A

G

D

I

I

F

F

Y

F

D

N

N

N

C

C

Q

F

R

K

N

N

G

G

V

M

L

L

L

P

I

I

T

P

L

T

D

P

E

I

A

E

V

Q

L

V

Q

N

T

D

L

M

G

M

K

K

T

A

V

A

S

E

Q

-

A

-

D

N

Q

Q

A

V

Q

K

I

F

S

S

V

V

D

D

L

L

E

V

A

N

Q

Q

Q

T

I

I

R

T

L

Y

A

G

D

D

G

K

E

Q

V

V

I

-

A

K

F

F

Q

D

I

V

D

E

T

P

L

F

R

R

K

K

S

H

A

C

L

L

L

V

L

N

G

G

L

L

D

D

A

D

I

I

G

G

S

L

T

T

L

L

Q

Q

R

K

S

E

D

T

E

M

I

I

K

D

A

A

F

F

E

E

R

A

H

R

L

E

Q

E

A

N

N

F

P

P

W

W

L

M

N

N

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)
39% identity, 94% coverage: 3:193/204 of query aligns to 1:184/198 of P9WK95

query
sites
P9WK95

L

M

Q

E

P

A

F

F

T

H

L

T

V

H

T

S

G

G

K

I

A

G

A

V

P

P

M

L

L

R

A

R

A

S

N

N

I

V

D

D

T

T

D

D

V

Q

I

I

M

I

P

P

K

A

Q

V

F

F

L

L

K

K

G

R

I

V

D

T

R

R

S

T

G

G

L

F

D

E

R

D

G

G

L

L

F

F

F

A

D

G

L

W

R

R

F

-

L

-

S

-

G

-

E

-

P

S

N

D

P

P

E

A

F

F

V

V

L

L

N

N

Q

L

P

S

A

P

W

F

Q

D

G

R

A

G

S

S

F

V

M

L

V

V

V

A

G

G

P

P

N

D

F

F

G

G

C

T

G

G

S

S

R

R

E

E

H

H

A

A

V

V

W

W

G

A

L

L

K

M

Q

D

M

Y

G

G

I

F

R

R

A

V

L

V

I

I

G

S

S

S

S

R

F

F

A

G

G

D

I

I

F

F

Y

R

D

G

N

N

C

A

Q

G

R

K

N

A

G

G

V

L

L

L

L

A

I

A

T

E

L

V

D

A

E

Q

A

D

V

D

L

V

Q

E

T

L

L

L

G

W

K

K

T

L

V

I

S

E

Q

Q

A

S

D

P

Q

G

A

L

Q

E

I

I

S

T

V

A

D

N

L

L

E

Q

A

-

Q

D

Q

R

I

I

R

I

L

T

A

A

D

A

G

T

E

V

V

V

I

L

A

P

F

F

Q
x
K

I

I

D

D

T

D

L

H

R

S

K

A

S

W

A

R

L

L

L

E

G

G

L

L

D

D

A

D

I

I

G

A

S

L

T

T

L

L

Q

R

R

K

S

L

D

D

E

E

I

I

K

E

A

A

F

F

E

E

K154 (≠ Q163) 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)
30% identity, 73% coverage: 8:156/204 of query aligns to 2:129/170 of Q58667

query
sites
Q58667

L

I

V

I

T

K

G

G

K

R

A

A

A

H

P

K

M

-

L

F

A

G

A

D

N

D

I

V

D

D

T

T

D

D

V

A

I

I

M

I

P

P

K

G

Q

P

F

Y

L

L

K
x
R

G
x
T

I

T

D

D

R

P

S

Y

G

E

L

L

D

A

R

S

G

H

L

C

F

M

F

A

D

G

L

I

R

-

F

-

L

-

S

-

G

D

E

E

P

N

N

F

P

P

E

K

F

K

V

V

L

-

N

-

Q

-

P

-

A

-

W

-

Q

K

G

E

A

G

S

D

F

V

M

I

V

V

V

A

G

G

P

E

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

H

Q

A

A

V

V

W

I

G

A

L

I

K

K

Q

Y

M

C

G

G

I

I

R

K

A

A

L

V

I

I

G

A

S

K

S

S

F

F

A

A

G

R

I

I

F

F

Y

Y

D

R

N

N

C

A

Q

I

R

N

N

V

G

G

V

L

L

I

L

P

I

I

T

-

L

-

D

-

E

-

A

-

V

-

L

-

Q

-

T

-

L

I

G

A

K

N

T

T

V

D

S

E

Q

I

A

K

D

D

Q

G

A

D

Q

I

I

V

S

E

V

I

D

D

L

L

E

D

A

K

Q

E

I

I

R

V

L

I

A

T

D

N

R26 (≠ K33) 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 (≠ G34) 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)
30% identity, 73% coverage: 8:156/204 of query aligns to 2:129/167 of 2pkpA

query
sites
2pkpA

L

I

V

I

T

K

G

G

K

R

A

A

A

H

P

K

M

-

L

F

A

G

A

D

N
x
D

I

V

D

D

T

T

D

D

V

A

I

I

M

I

P

P

K

G

Q

P

F

Y

L

L

K

R

G

T

I

T

D

D

R

P

S

Y

G

E

L

L

D

A

R

S

G

H

L

C

F

M

F

A

D

G

L

I

R

-

F

-

L

-

S

-

G

D

E

E

P

N

N

F

P

P

E

K

F

K

V

V

L

-

N

-

Q

-

P

-

A

-

W

-

Q

K

G

E

A

G

S

D

F

V

M

I

V

V

V

A

G

G

P

E

N

N

F

F

G

G

C
|
C

G

G

S

S

R

R

E

E

H

Q

A

A

V

V

W

I

G

A

L

I

K

K

Q

Y

M

C

G

G

I

I

R

K

A

A

L

V

I

I

G

A

S

K

S

S

F

F

A

A

G

R

I

I

F

F

Y

Y

D

R

N

N

C

A

Q

I

R

N

N

V

G

G

V

L

L

I

L

P

I

I

T

-

L

-

D

-

E

-

A

-

V

-

L

-

Q

-

T

-

L

I

G

A

K

N

T

T

V

D

S

E

Q

I

A

K

D

D

Q

G

A

D

Q

I

I

V

S

E

V

I

D

D

L

L

E

D

A

K

Q

E

I

I

R

V

L

I

A

T

D

N

binding zinc ion: D13 (≠ N20), C63 (= C81)

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
42% identity, 27% coverage: 68:123/204 of query aligns to 653:709/780 of P20004

query
sites
P20004

Q

H

G

G

A

I

S

R

F

W

M

V

V

V

V

I

G

G

-

D

P

E

N

N

F

Y

G

G

C

E

G

G

S

S

S
|
S

R
|
R

E

E

H

H

A

A

V

A

W

L

G

E

L

P

K

R

Q

H

M

L

G

G

I

G

R

R

A

A

L

I

I

I

G

T

S

K

S

S

F

F

A

A

G

R

I

I

F

H

Y

E

D

T

N

N

C

L

Q

K

R

K

N

Q

G

G

V

L

L

L

L

P

I

L

T

T

L

F

SR 670:671 (= SR 84:85) binding

Sites not aligning to the query:

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

5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
40% identity, 27% coverage: 68:123/204 of query aligns to 626:682/754 of 5acnA

query
sites
5acnA

Q

H

G

G

A

I

S

R

F

W

M

V

V

V

V

I

G

G

-

D

P

E

N

N

F

Y

G

G

C

E

G

G

S
|
S

S

S

R
|
R

E

E

H

H

A

S

V

A

W

L

G

E

L

P

K

R

Q

H

M

L

G

G

I

G

R

R

A

A

L

I

I

I

G

T

S

K

S

S

F

F

A

A

G
x
R

I

I

F

H

Y

E

D

T

N

N

C

L

Q

K

R

K

N

Q

G

G

V

L

L

L

L

P

I

L

T

T

L

F

active site: S642 (= S83), R644 (= R85)
binding tricarballylic acid: R666 (≠ G107)

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

Query Sequence

>GFF1851 PS417_09415 3-isopropylmalate dehydratase
MSLQPFTLVTGKAAPMLAANIDTDVIMPKQFLKGIDRSGLDRGLFFDLRFLSSGEPNPEF
VLNQPAWQGASFMVVGPNFGCGSSREHAVWGLKQMGIRALIGSSFAGIFYDNCQRNGVLL
ITLDEAVLQTLGKTVSQADQAQISVDLEAQQIRLADGEVIAFQIDTLRKSALLLGLDAIG
STLQRSDEIKAFERRHLQANPWLN

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