SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_010876462.1 NCBI__GCF_000008645.1:WP_010876462.1 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)

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)
55% identity, 92% coverage: 4:159/170 of query aligns to 2:157/170 of Q58667

query
sites
Q58667

I

I

R

K

G

G

R

R

V

A

W

H

R

K

F

F

G

G

D

D

N

D

V

V

D

D

T

T

D

D

M

A

I

I

P

P

G

G

R

P

Y

Y

L

L

R
|
R

T
|
T

F

T

S

D

L

P

D

Y

E

E

L

L

A

A

S

S

H

H

V

C

M

M

E

A

G

G

A

I

R

D

P

E

E

N

F

F

A

P

S

K

Q

K

V

V

R

K

K

E

G

G

D

D

I

V

I

I

V

V

A

A

G

G

R

E

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

Q

Q

A

A

P

V

V

I

A

A

L

I

K

K

H

Y

A

C

G

G

V

I

V

K

A

A

I

V

I

I

A

A

E

K

S

S

F

F

A

A

R

R

I

I

F

F

Y

Y

R

R

N

N

A

A

I

I

N

N

I

V

G

G

L

L

P

I

V

P

I

I

M

I

A

A

K

N

V

T

D

D

A

E

-

I

D

K

D

D

G

G

D

D

E

I

V

V

S

E

I

I

D

D

L

L

R

D

S

K

G

E

Q

E

I

I

R

V

N

I

L

T

T

N

A

K

G

N

S

K

E

T

Y

I

R

K

M

C

K

E

P

T

F

P

N

K

D

G

Y

L

M

E

L

R

S

E

I

I

L

L

E

A

D

A

G

G

L

L

V

V

N

N

H

-

Y

Y

L

L

K

K

R26 (= R28) 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 (= T29) 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)
55% identity, 92% coverage: 4:159/170 of query aligns to 2:157/167 of 2pkpA

query
sites
2pkpA

I

I

R

K

G

G

R

R

V

A

W

H

R

K

F

F

G

G

D

D

N
x
D

V

V

D

D

T

T

D

D

M

A

I

I

P

P

G

G

R

P

Y

Y

L

L

R

R

T

T

F

T

S

D

L

P

D

Y

E

E

L

L

A

A

S

S

H

H

V

C

M

M

E

A

G

G

A

I

R

D

P

E

E

N

F

F

A

P

S

K

Q

K

V

V

R

K

K

E

G

G

D

D

I

V

I

I

V

V

A

A

G

G

R

E

N

N

F

F

G

G

C
|
C

G

G

S

S

R

R

E

E

Q

Q

A

A

P

V

V

I

A

A

L

I

K

K

H

Y

A

C

G

G

V

I

V

K

A

A

I

V

I

I

A

A

E

K

S

S

F

F

A

A

R

R

I

I

F

F

Y

Y

R

R

N

N

A

A

I

I

N

N

I

V

G

G

L

L

P

I

V

P

I

I

M

I

A

A

K

N

V

T

D

D

A

E

-

I

D

K

D

D

G

G

D

D

E

I

V

V

S

E

I

I

D

D

L

L

R

D

S

K

G

E

Q

E

I

I

R

V

N

I

L

T

T

N

A

K

G

N

S

K

E

T

Y

I

R

K

M

C

K

E

P

T

F

P

N

K

D

G

Y

L

M

E

L

R

S

E

I

I

L

L

E

A

D

A

G

G

L

L

V

V

N

N

H

-

Y

Y

L

L

K

K

binding zinc ion: D13 (≠ N15), C63 (= C65)

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, 87% coverage: 15:162/170 of query aligns to 554:721/758 of O14289

query
sites
O14289

N

N

V

V

D

D

T

T

D

D

M

K

I

I

P

P

G

K

R

Q

Y

F

L

L

R

K

T

T

F

I

S

K

L

R

D

T

E

G

L

L

A

G

S

Q

H

F

V

A

M

F

E

Y

G

E

A

I

R

R

-

Y

-

D

-

A

-

D

-

G

-

K

-

E

-

I

P

P

E

D

F

F

A

V

-

L

-

N

-

R

S

E

Q

P

V

Y

R

R

K

H

G

A

D

T

I

V

I

L

V

V

A

A

G

H

R

D

N

N

F

F

G

G

C

C

G

G

S

S

R

R

E

E

Q

H

A

A

P

P

V

W

A

A

L

L

K

N

H

D

A

F

G

G

V

I

V

R

A

V

I

I

A

A

E

P

S

S

F

F

A

A

R

D

I

I

F

F

Y

F

R

N

N

N

A

C

I

F

N

K

I

N

G

G

L

M

-

L

-

P

-

I

P

P

V

T

I

P

M

I

A

E

K

Q

V

V

D

N

-

D

-

M

-

K

-

A

A

A

D

E

D

N

G

Q

D

V

E

K

V

F

S

S

I

V

D

D

L

L

R

V

S

N

G

Q

Q

T

I

I

R

T

N

Y

L

G

T

D

A

K

G

Q

S

V

E

K

Y

F

R

D

M

V

K

E

P

P

F

F

N

R

D

K

Y

H

M

C

L

L

-

V

S

N

I

G

L

L

E

D

D

D

G

I

G

G

L

L

V

T

N

L

H

Q

Y

K

L

E

K

T

T

M

I

I

D

D

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, 58% coverage: 15:113/170 of query aligns to 18:119/198 of P9WK95

query
sites
P9WK95

N

N

V

V

D

D

T

T

D

D

M

Q

I

I

P

P

G

A

R

V

Y

F

L

L

R

K

T

R

F

V

S

T

L

R

D

T

E

G

L

F

A

E

S

D

H

G

V

L

M

F

E

A

G

G

A

W

R

R

-

S

-

D

P

P

E

A

F

F

A

V

-

L

-

N

-

L

S

S

Q

P

V

F

R

D

K

R

G

G

D

S

I

V

I

L

V

V

A

A

G

G

R

P

N

D

F

F

G

G

C

T

G

G

S

S

R

R

E

E

Q

H

A

A

P

V

V

W

A

A

L

L

K

M

H

D

A

Y

G

G

V

F

V

R

A

V

I

V

I

I

A

S

E

S

S

R

F

F

A

G

R

D

I

I

F

F

Y

R

R

G

N

N

A

A

I

G

N

K

I

A

G

G

L

L

P

-

V

-

I

L

M

A

A

A

K

E

V

V

D

A

A

Q

D

D

Sites not aligning to the query:

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

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
32% identity, 55% coverage: 14:107/170 of query aligns to 611:710/780 of P20004

query
sites
P20004

D

D

N

N

V

I

D

S

T

N

D

N

M

L

I

L

I

I

P

G

G

A

R

I

Y

N

L

V

R

E

T

N

F

G

S

K

L

A

D

N

E

S

L

V

A

R

S

N

H

A

V

V

M

T

E

Q

-

E

-

F

G

G

A

P

R

V

P

P

E

D

F

T

A

A

S

R

Q

Y

V

Y

R

K

K

K

G

H

D

G

I

I

-

R

-

W

-

V

I

V

V

I

A

G

G

D

R

E

N

N

F

Y

G

G

C

E

G

G

S

S

S
|
S

R
|
R

E

E

Q

H

A

A

P

A

V

L

A

E

L

P

K

R

H

H

A

L

G

G

V

G

V

R

A

A

I

I

A

T

E

K

S

S

F

F

A

A

R

R

I

I

F

H

Y

E

R

T

N

N

A

L

I

K

N

K

I

Q

G

G

-

L

L

L

P

P

V

L

I

T

M

F

A

A

SR 670:671 (= SR 68:69) binding

Sites not aligning to the query:

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

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)
39% identity, 31% coverage: 52:104/170 of query aligns to 777:830/909 of P09339

query
sites
P09339

R

K

K

T

G

G

D

L

I

V

V

L

A

A

G

G

R

K

N

D

F

Y

G

G

C

M

G

G

S

S

R

R

E

D

Q

W

A

A

P

A

V

K

A

G

L

T

K

N

H

L

A

L

G

G

V

I

V

R

A

T

I

V

I

I

A

A

E

E

S

S

F

F

A

E

R

R

I

I

F

H

Y

R

R

S

N

N

A

L

I

V

N

F

I

M

G

G

-

V

L

L

P

P

V

L

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

>WP_010876462.1 NCBI__GCF_000008645.1:WP_010876462.1
MEGIIRGRVWRFGDNVDTDMIIPGRYLRTFSLDELASHVMEGARPEFASQVRKGDIIVAG
RNFGCGSSREQAPVALKHAGVVAIIAESFARIFYRNAINIGLPVIMAKVDADDGDEVSID
LRSGQIRNLTAGSEYRMKPFNDYMLSILEDGGLVNHYLKTIDTGISGDEG

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