SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing WP_005347177.1 NCBI__GCF_000173975.1:WP_005347177.1 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 2 hits to proteins with known functional sites (download)

P0A9J8 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 from Escherichia coli (strain K12)
23% identity, 35% coverage: 185:284/287 of query aligns to 285:378/386 of P0A9J8

query
sites
P0A9J8

R

R

K

K

V

A

V

I

T

N

F

V

T

S

D

D

K

Q

L

V

V

-

L

-

P

P

S

A

H

-

N

-

R

K

V

T

K

T

V

L

M

L

F

M

E

A

C

T

P

G

N

Q

H

Q

S

A

G

G

S

A

I

L

S

V

S

E

I

A

L

L

S

L

M

V

I

L

S

R

D

N

Y

H

G

N

V

L

N

I

L

M

T

T

E

R

I

L

H

E

S

S

R

R

P

P

F

I

W

-

K

H

D

G

N

N

S

P

W

W

N

E

Y

E

K

M

F

F

F

Y

V

L

E

D

M

I

N

Q

A

A

N

N

I

L

D

E

T

S

K

A

E

E

I

M

R

Q

A

K

L

A

I

L

Y

K

Q

E

L

L

S

G

Q

E

E

I

T

T

A

R

Y

S

L

M

K

K

I

V

L

L

G

G

S

C

Y

Y

A

P

C

S

E

E

Sites not aligning to the query:

11 mutation R->A,K: Important decrease in catalytic efficiency and affinity.
28 mutation R->A,K: Important decrease in catalytic efficiency and affinity.
39 mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
52 mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
88 mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

2qmxA The crystal structure of l-phe inhibited prephenate dehydratase from chlorobium tepidum tls (see paper)
26% identity, 29% coverage: 199:282/287 of query aligns to 192:274/278 of 2qmxA

query
sites
2qmxA

S

A

H

R

N

Q

R

K

V

T

K

S

V

I

M

V

F

F

E

A

C

L

P

P

N
|
N

H
x
E

S

Q

G

G

S

S

I
x
L

S

F

S

R

I

A

L

L

S

A

M

T

I

F

S

A

D

L

Y

R

G

G

V

I

N
x
D

L
|
L

T
|
T

E
x
K

I

I

H

E

S
|
S

R

R

P

P

F

S

W

R

K

K

D

-

N

K

S

A

W

F

N

E

Y
|
Y

K

L

F
|
F

F

Y

V

A

E

D

M

F

N

I

A

G

N

H

I

R

D

E

T

D

K

Q

E

N

I

V

R

H

A

N

L

A

I

L

Y

E

Q

N

L

L

S

R

Q

E

E

F

T

A

A

T

Y

M

L

V

K

K

I

V

L

L

G

G

S

S

Y

Y

A

G

binding phenylalanine: N204 (= N211), E205 (≠ H212), L209 (≠ I216), D222 (≠ N229), L223 (= L230), T224 (= T231), K225 (≠ E232), S228 (= S235), Y238 (= Y246), F240 (= F248)

Sites not aligning to the query:

active site: 169, 171

Query Sequence

>WP_005347177.1 NCBI__GCF_000173975.1:WP_005347177.1
MDLSDVRKNIDRVDAEIRKLFVERMTLADQVACIKAETEDKIYKPDREEIIIKKQTEGMK
PELVREYTALIKRIMEVSRKYQYGRTLELRQCFPFEYSKMPAVILKPTMVKEELYICEDF
SKDKVITVSSYEEIGNYIKEGKADAGIGIIEEVGIGVSDELHNLLAEKDLYITHCKVQED
GGVRRKVVTFTDKLVVLPSHNRVKVMFECPNHSGSISSILSMISDYGVNLTEIHSRPFWK
DNSWNYKFFVEMNANIDTKEIRALIYQLSQETAYLKILGSYACEGDF

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