SitesBLAST

P77589 3-(3-hydroxy-phenyl)propionate transporter; 3HPP transporter; 3-(3-hydroxy-phenyl)propionate:H(+) symporter; 3HPP:H(+) symporter from Escherichia coli (strain K12) (see paper)
28% identity, 36% coverage: 74:240/458 of query aligns to 56:207/403 of P77589

query
sites
P77589

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D75 (= D93) mutation D->A,E: Lack of 3HPP transport activity.

Sites not aligning to the query:

27 E→A: Lack of 3HPP transport activity.; E→D: Slight decrease in 3HPP transport activity.
272 A→H: 30% increase in 3HPP transport activity.
276 K→D: Lack of 3HPP transport activity.

Q09852 Putative inorganic phosphate transporter C23D3.12 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
25% identity, 39% coverage: 79:256/458 of query aligns to 99:284/559 of Q09852

query
sites
Q09852

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Sites not aligning to the query:

297 modified: Phosphoserine
299 modified: Phosphoserine

Q5EXK5 3-hydroxybenzoate transporter MhbT from Klebsiella oxytoca (see paper)
27% identity, 32% coverage: 89:233/458 of query aligns to 78:208/452 of Q5EXK5

query
sites
Q5EXK5

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D82 (= D93) mutation to A: Loss of activity.

Sites not aligning to the query:

311 V→W: Loss of activity.
314 D→A: Loss of activity.

8fvzA Pipt y150a
26% identity, 41% coverage: 52:237/458 of query aligns to 29:214/433 of 8fvzA

query
sites
8fvzA

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binding phosphate ion: F145 (≠ G171)

Sites not aligning to the query:

binding phosphate ion: 235, 239, 243, 346

Q9R0W2 Solute carrier family 22 member 2; Organic cation transporter 2; rOCT2 from Rattus norvegicus (Rat) (see paper)
29% identity, 26% coverage: 64:184/458 of query aligns to 148:255/555 of Q9R0W2

query
sites
Q9R0W2

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Sites not aligning to the query:

451 Involved in recognition of organic cations and participates in structural changes that occur during translocation of organic cations; C→M: Transport activity strongly reduced.

A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
26% identity, 48% coverage: 50:268/458 of query aligns to 24:231/446 of A0A0H2VG78

query
sites
A0A0H2VG78

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R102 (= R136) mutation to A: Loss of transport activity.
I105 (≠ Q139) mutation to S: Affects symport activity. May function as an uniporter.
E122 (= E156) mutation to A: Loss of transport activity.
Q137 (≠ G171) mutation to A: Loss of transport activity.

Sites not aligning to the query:

22 D→N: Affects symport activity. May function as an uniporter.
250 Q→A: Loss of transport activity.
251 Q→A: Loss of transport activity.
256 N→A: Loss of transport activity.
357 W→A: Loss of transport activity.

Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
25% identity, 37% coverage: 75:244/458 of query aligns to 84:238/444 of Q8NLB7

query
sites
Q8NLB7

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F

D

E

E

R103 (≠ K94) mutation to A: Loss of transport activity.

Sites not aligning to the query:

54 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
57 D→A: Loss of transport activity.; D→E: Retains 50% of its transport activity.
309 W→V: Loss of transport activity.
312 D→A: Loss of transport activity.
313 R→A: Loss of transport activity.
317 mutation I->H,Y: Loss of transport activity.
386 R→A: Loss of transport activity.

Q51955 4-hydroxybenzoate transporter PcaK from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
25% identity, 38% coverage: 2:177/458 of query aligns to 4:165/448 of Q51955

query
sites
Q51955

S

A

E

Q

N

N

N

S

I

V

H

G

T

K

Q

S

A

L

A

D

E

V

A

Q

N

S

F

F

Q

I

T

N

E

Q

G

P

K

L

K

S

D

R

F

Y

-

Q

W

W

R

R

A

V

T

V

I

L

S

L

C

C

W

F

L

L

G

I

T

V

T

F

M

L

E
x
D

Y

G

T

L

D
|
D

F

T

A

A

L

A

Y

M

G

G

L

F

A

I

A

A

G

P

I

A

I

L

F

S

G

Q

E

E

V

W

F

G

F

I

P

D

E

R

S

A

T

S

-

L

-

G

P

P

V

V

M

M

A

-

L

-

Q

-

S

-

F

-

A

-

F

-

S

S

V

A

G

A

F

L

I

I

A

G

R

M

P

V

I

F

G

G

A

A

I

L

V

G

F

S

G
|
G

M

P

L

L

G

A

D
|
D

K

R

M

F

G
|
G

R

R

K

K

F

G

V

V

M

L

V

V

I

G

T

A

I

V

S

L

L

V

M

F

G

G

L

-

A

-

T

-

C

G

I

F

G

S

L

L

I

A

P

S

S

A

Y

Y

E

-

K

-

I

-

G

-

A

A

W

T

S

N

A

V

A

D

L

Q

L

L

V

L

L

V

M

L

R
|
R

F

F

M

L

Q

T

G

G

L

L

G

G

A

L

G

G

A

A

E

G

L

M

S

P

G

N

G

A

A

T

V

T

M

L

L

L

G

S

E
|
E

Y

Y

A

T

P

P

V

E

K

R

R

L

R

K

G

S

V

L

S

V

S

T

I

S

I

M

G

F

L

C

G

G

S

F

N

N

S

L

G

G

D41 (≠ E38) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
D44 (= D41) mutation D->A,N: Abolishes 4-HBA transport.; mutation to E: Decrease in 4-HBA transport.
G85 (= G89) mutation to V: Abolishes 4-HBA transport and chemotaxis.
D89 (= D93) mutation to N: Abolishes 4-HBA transport and chemotaxis.
G92 (= G96) mutation to A: Decrease in 4-HBA transport and chemotaxis.; mutation to C: No change in 4-HBA transport and chemotaxis.; mutation G->L,V: Abolishes 4-HBA transport and chemotaxis.; mutation to Q: Decrease in 4-HBA transport and strong decrease in chemotaxis.
R124 (= R136) mutation to A: Abolishes 4-HBA transport.
E144 (= E156) mutation to A: Strong decrease in 4-HBA transport.

Sites not aligning to the query:

183 H→A: Decrease in 4-HBA transport and chemotaxis.
323 D→N: Abolishes 4-HBA transport and chemotaxis.
328 H→A: Decrease in 4-HBA transport and chemotaxis.; H→R: Decrease in 4-HBA transport and loss of chemotaxis.
386 R→A: Strong decrease in 4-HBA transport.
398 R→A: Abolishes 4-HBA transport.
444 H→A: No change in 4-HBA transport and chemotaxis.

Query Sequence

>WP_009142420.1 NCBI__GCF_000188195.1:WP_009142420.1
MSENNIHTQAAEANFQTEEGKKDFWRATISCWLGTTMEYTDFALYGLAAGIIFGEVFFPE
STPVMALLQSFAAFSVGFIARPIGAIVFGMLGDKMGRKFVMVITISLMGLATTCIGLIPS
YEKIGAWSAALLVLMRFMQGLGAGAELSGGAVMLGEYAPVKRRGVVSSIIGLGSNSGTLL
ASAVWLLVLQLDHDDLMSWGWRIPFLGSILIAYIALLIRKHMRETPVFEKQKKQLEKMRK
EAFEKGVELQKKDKRSFFARTKAFWVMVGLRIGENGPSYLAQGFIIGYVVSFLSVDKSVA
TMSVFVASVLGFFIIPFSGWLSDKFGRRITYRWFCILLVLWAFPAFMLLDTKEPWIVGPV
IVIGMGLASLGIFGVQAAWGVELFGVTNRYTKMAFAKELGSIMSGGTAPMIASALLSYYG
HWWPIATYFAVCAFIGLVSTFIAPETRGRDLNLPEDAL

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