SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing Dsui_3199 FitnessBrowser__PS:Dsui_3199 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 7 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)
52% identity, 98% coverage: 4:210/212 of query aligns to 540:734/758 of O14289

query
sites
O14289

F

F

T

T

K

V

L

V

D

E

G

G

L

I

V

A

A

A

P

P

L

L

D

P

R

M

N

A

N

N

V

V

D

D

T

T

D

D

A

K

I

I

P

P

K

K

Q

Q

F

F

L

L

K

K

S

T

I

I

K

K

R

R

S

T

G

G

F

L

G

G

P

Q

N

F

A

A

F

F

D

Y

E

E

W

I

R

R

Y

Y

M

D

D

A

H

D

G

G

E

K

P

E

G

-

M

-

D

-

N

-

S

-

K

-

R

-

P

-

L

-

N

I

P

P

N

D

F

F

V

V

L

L

N

N

Q

R

Q

E

R

P

Y

Y

Q

R

G

H

A

A

S

T

V

V

L

L

L

V

T

A

R

H

S

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

L

N

D

D

Y

F

G

G

F

I

R

R

V

V

V

I

I

I

A

A

E

P

S

S

F

F

A

A

D

D

I

I

F

F

N

N

C

C

F

F

K

K

N

N

G

G

I

M

L

L

P

P

I

I

V

P

L

T

P

P

K

I

T

E

E

Q

I

V

D

N

A

D

L

M

F

M

G

K

L

A

T

A

E

E

Y

N

T

Q

P

-

G

-

F

V

K

K

L

F

V

S

V

V

D

D

L

L

E

V

Q

N

Q

Q

K

T

V

I

V

T

R

Y

P

G

D

D

G

K

H

Q

A

-

I

V

P

K

F

F

E

D

V

V

D

E

A

P

F

F

R

R

R

K

E

H

C

C

L

L

L

V

N

N

G

G

W

L

D

D

I

I

G

G

L

L

T

T

L

L

R

Q

H

K

A

E

D

T

K

M

I

I

K

D

A

A

F

F

E

E

E

A

R

A

R

R

R

E

A

E

E

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)
43% identity, 94% coverage: 1:200/212 of query aligns to 1:184/198 of P9WK95

query
sites
P9WK95

M

M

Q

E

A

A

F

F

T

H

K

T

L

H

D

S

G

G

L

I

V

G

A

V

P

P

L

L

D

R

R

R

N

S

N

N

V

V

D

D

T

T

D

D

A

Q

I

I

P

P

K

A

Q

V

F

F

L

L

K

K

S

R

I

V

K

T

R

R

S

T

G

G

F

F

G

E

P

D

N

G

A

L

F

F

D

A

E

G

W

W

R

R

Y

S

M

-

D

-

H

-

G

-

E

-

P

-

G

-

M

-

D

-

N

-

S

-

K

-

R

-

P

-

L

-

N

D

P

P

N

A

F

F

V

V

L

L

N

N

Q

L

Q

S

R

P

Y

F

Q

D

G

R

A

G

S

S

V

V

L

L

L

V

T

A

R

G

S

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

L

M

D

D

Y

Y

G

G

F

F

R

R

V

V

I

I

A

S

E

S

S

R

F

F

A

G

D

D

I

I

F

F

F

R

N

G

N

N

C

A

F

G

K

K

N

A

G

G

I

L

L

L

P

A

I

A

V

E

L

V

P

A

K

Q

T

D

E

D

I

V

D

E

A

L

L

L

F

W

G

K

L

L

T

I

E

E

Y

Q

T

S

P

P

G

G

F

L

K

E

L

I

V

T

V

A

D

N

L

L

E

-

Q

Q

Q

D

K

R

V

I

R

T

P

A

D

A

G

T

H

V

A

V

I

L

P

P

F

F

E
x
K

V

I

D

D

A

D

F

H

R

S

R

A

E

W

C

R

L

L

N

E

G

G

W

L

D

D

I

I

G

A

L

L

T

T

L

L

R

R

H

K

A

L

D

D

K

E

I

I

K

E

A

A

F

F

E

E

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)
32% identity, 68% coverage: 17:160/212 of query aligns to 12:126/170 of Q58667

query
sites
Q58667

N

D

V

V

D

D

T

T

D

D

A

A

I

I

P

P

K

G

Q

P

F

Y

L

L

K
x
R

S
x
T

I

T

K

-

R

-

S

-

G

-

F

-

G

-

P

-

N

-

A

-

F

-

D

D

E

P

W

Y

R

E

Y

L

M

A

D

S

H

H

G

C

E

M

P

A

G

G

M

I

D

D

N

E

S

-

K

-

R

-

P

-

L

-

N

-

P

-

N

N

F

F

V

-

L

-

N

-

Q

P

Q

K

R

K

Y

V

Q

K

G

E

A

G

S

D

V

V

L

I

L

V

T

A

R

G

S

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

L

K

D

Y

Y

C

G

G

F

I

R

K

V

A

V

V

I

I

A

A

E

K

S

S

F

F

A

A

D

R

I

I

F

F

F

Y

N

R

N

N

C

A

F

I

K

N

N

V

G

G

I

L

L

I

P

P

I

I

V

I

L

A

P

N

K

T

T

D

E

E

I

I

D

-

A

-

L

-

F

-

G

-

L

-

T

-

E

-

Y

-

T

K

P

D

G

G

F

D

K

I

L

V

V

E

V

I

D

D

L

L

E

D

Q

K

Q

E

K

E

V

I

V

V

R26 (≠ K31) 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 (≠ S32) 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)
32% identity, 68% coverage: 17:160/212 of query aligns to 12:126/167 of 2pkpA

query
sites
2pkpA

N

D

N
x
D

V

V

D

D

T

T

D

D

A

A

I

I

P

P

K

G

Q

P

F

Y

L

L

K

R

S

T

I

T

K

-

R

-

S

-

G

-

F

-

G

-

P

-

N

-

A

-

F

-

D

D

E

P

W

Y

R

E

Y

L

M

A

D

S

H

H

G

C

E

M

P

A

G

G

M

I

D

D

N

E

S

-

K

-

R

-

P

-

L

-

N

-

P

-

N

N

F

F

V

-

L

-

N

-

Q

P

Q

K

R

K

Y

V

Q

K

G

E

A

G

S

D

V

V

L

I

L

V

T

A

R

G

S

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

L

K

D

Y

Y

C

G

G

F

I

R

K

V

A

V

V

I

I

A

A

E

K

S

S

F

F

A

A

D

R

I

I

F

F

F

Y

N

R

N

N

C

A

F

I

K

N

N

V

G

G

I

L

L

I

P

P

I

I

V

I

L

A

P

N

K

T

T

D

E

E

I

I

D

-

A

-

L

-

F

-

G

-

L

-

T

-

E

-

Y

-

T

K

P

D

G

G

F

D

K

I

L

V

V

E

V

I

D

D

L

L

E

D

Q

K

Q

E

K

E

V

I

V

V

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

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)
33% identity, 43% coverage: 79:170/212 of query aligns to 781:878/909 of P09339

query
sites
P09339

V

V

L

V

L

L

T

A

R

G

S

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

L

N

D

L

Y

L

G

G

F

I

R

R

V

T

V

V

I

I

A

A

E

E

S

S

F

F

A

E

D

R

I

I

F

H

F

R

N

S

N

N

C

L

F

V

K

F

N

M

G

G

I

V

L

L

P

P

I

L

V

Q

L

F

P

K

K

Q

T

G

E

E

I

N

D

A

A

D

L

T

F

L

G

G

L

L

T

T

E

G

Y

-

T

-

P

-

G

-

F

-

K

K

L

E

V

V

V

I

D

E

L

V

E

D

Q

V

Q

D

K

E

V

T

V

V

R

R

P

P

-

R

-

D

-

L

-

V

-

T

-

V

-

R

-

A

-

I

-

N

-

E

D

D

G

G

H

N

A

V

I

T

P

T

F

F

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.

P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
33% identity, 37% coverage: 79:156/212 of query aligns to 658:744/780 of P20004

query
sites
P20004

V

V

L

V

L

I

T

G

R

D

S

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

L

R

D

H

Y

L

G

G

F

G

R

R

V

A

V

I

I

I

A

T

E

K

S

S

F

F

A

A

D

R

I

I

F

H

F

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

V

T

L

F

P

A

K

D

T

P

E

A

-

D

-

Y

-

N

-

K

-

I

-

H

-

P

I

V

D

D

A

K

L

L

F

T

-

I

-

K

G

G

L

L

T

K

E

D

Y

F

T

A

P

P

G

G

F

K

K

P

L

L

V

T

V

C

D

I

L

I

E

K

Q

H

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

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)
38% identity, 35% coverage: 73:147/212 of query aligns to 648:732/778 of P19414

query
sites
P19414

R

R

Y

D

Q

Q

G

G

A

I

S

K

-

W

V

V

L

V

L

I

T

G

R

D

S

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

L

R

D

F

Y

L

G

G

F

G

R

F

V

A

V

I

I

I

A

T

E

K

S

S

F

F

A

A

D

R

I

I

F

H

F

E

N

T

N

N

C

L

F

K

K

K

N

Q

G

G

I

L

L

L

P

P

I

L

-

N

-

F

-

K

-

N

-

P

-

A

-

D

-

Y

-

D

-

K

V

I

L

N

P

P

K

D

T

D

E

R

I

I

D

D

A

-

L

I

F

L

G

G

L

L

T

A

E

E

Y

L

T

A

P

P

G

G

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.

Query Sequence

>Dsui_3199 FitnessBrowser__PS:Dsui_3199
MQAFTKLDGLVAPLDRNNVDTDAIIPKQFLKSIKRSGFGPNAFDEWRYMDHGEPGMDNSK
RPLNPNFVLNQQRYQGASVLLTRSNFGCGSSREHAPWALLDYGFRVVIAESFADIFFNNC
FKNGILPIVLPKTEIDALFGLTEYTPGFKLVVDLEQQKVVRPDGHAIPFEVDAFRRECLL
NGWDDIGLTLRHADKIKAFEERRRAEQPWLFS

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