SitesBLAST

4ea8A X-ray crystal structure of perb from caulobacter crescentus in complex with coenzyme a and gdp-n-acetylperosamine at 1 angstrom resolution (see paper)
33% identity, 55% coverage: 106:247/257 of query aligns to 66:206/207 of 4ea8A

query
sites
4ea8A

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binding coenzyme a: H145 (≠ S186), F163 (≠ Y204), G165 (= G206), V166 (≠ S207), A184 (= A225), K206 (≠ Q247)
binding GDP-N-acetylperosamine: I68 (= I108), G69 (= G109)

Sites not aligning to the query:

binding GDP-N-acetylperosamine: 14, 15, 16, 35, 36, 37, 50

3bsyA Pgld from campylobacter jejuni, nctc 11168, in complex with acetyl coenzyme a (see paper)
30% identity, 54% coverage: 106:245/257 of query aligns to 51:191/193 of 3bsyA

query
sites
3bsyA

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binding acetyl coenzyme *a: H132 (≠ S186), S134 (≠ M188), V135 (≠ T189), A140 (≠ S194), F150 (≠ Y204), G152 (= G206), I153 (≠ S207), L158 (= L212), G170 (= G224), G171 (≠ A225), V176 (≠ T230), V186 (= V240), P189 (= P243)

5tyhA Pgld from campylobacter jejuni nctc 11168 in complex with 5-(2- furanyl)-1h-pyrazole-3-carboxylic acid (see paper)
30% identity, 54% coverage: 106:245/257 of query aligns to 43:183/185 of 5tyhA

query
sites
5tyhA

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binding 3-(furan-2-yl)-1H-pyrazole-5-carboxylic acid: I75 (= I133), S76 (≠ D134), N96 (≠ T158), N108 (= N170), S126 (≠ M188), V127 (≠ T189), F142 (≠ Y204), G144 (= G206), I145 (≠ S207), G163 (≠ A225)

3bssA Pgld from campylobacter jejuni, nctc 11168, with native substrate (see paper)
30% identity, 54% coverage: 106:245/257 of query aligns to 52:192/194 of 3bssA

query
sites
3bssA

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binding UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose: I54 (= I108), G55 (= G109), I59 (≠ A113)

Sites not aligning to the query:

binding UDP-2-acetamido-4-amino-2,4,6-trideoxy-alpha-D-glucopyranose: 12, 14, 34, 35, 36

2vheA Pgld-coa complex: an acetyl transferase from campylobacter jejuni (see paper)
30% identity, 54% coverage: 106:245/257 of query aligns to 52:192/194 of 2vheA

query
sites
2vheA

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binding coenzyme a: S135 (≠ M188), V136 (≠ T189), F151 (≠ Y204), G153 (= G206), I154 (≠ S207), G171 (= G224), G172 (≠ A225), V187 (= V240)

Sites not aligning to the query:

binding coenzyme a: 194

Q0P9D1 UDP-N-acetylbacillosamine N-acetyltransferase; Protein glycosylation D; UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase; EC 2.3.1.203 from Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (see 2 papers)
30% identity, 54% coverage: 106:245/257 of query aligns to 53:193/195 of Q0P9D1

query
sites
Q0P9D1

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N118 (= N170) mutation to A: Reduction in catalytic activity.
E124 (≠ S176) mutation to A: Reduction in catalytic activity.
H125 (= H177) active site, Proton acceptor; mutation to A: Strong reduction in catalytic activity.
H134 (≠ S186) binding acetyl-CoA; mutation to A: Slight reduction in catalytic activity.
I155 (≠ S207) binding acetyl-CoA
G173 (≠ A225) binding acetyl-CoA

Sites not aligning to the query:

15 H→A: Induces a higher KM and approximate 3-fold decrease in the turnover number.

4eaaA X-ray crystal structure of the h141n mutant of perosamine n- acetyltransferase from caulobacter crescentus in complex with coa and gdp-perosamine (see paper)
31% identity, 66% coverage: 79:247/257 of query aligns to 43:208/210 of 4eaaA

query
sites
4eaaA

L

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K

binding coenzyme a: P150 (≠ T189), F165 (≠ Y204), V168 (≠ S207), A186 (= A225), I201 (≠ V240), K208 (≠ Q247)
binding GDP-perosamine: D52 (≠ R89), I70 (= I108), G71 (= G109)

Sites not aligning to the query:

binding GDP-perosamine: 14, 15, 16, 35, 36, 37

P07464 Galactoside O-acetyltransferase; GAT; Acetyl-CoA:galactoside 6-O-acetyltransferase; Thiogalactoside acetyltransferase; Thiogalactoside transacetylase; EC 2.3.1.18 from Escherichia coli (strain K12) (see 3 papers)
31% identity, 48% coverage: 127:250/257 of query aligns to 80:185/203 of P07464

query
sites
P07464

R

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S

H

H

H

E

E

S

L

K

R

L

-

G

-

D

-

F

-

S

-

V

-

M

K

T

N

G

G

V

E

R

M

I

Y

S

S

G

F

N

P

C

I

R

T

I

I

G

G

H

N

G

N

A

V

Y

W

I

I

G

G

S
|
S

G

H

A

V

V

V

V

I

L

N

Q

P

G

G

R

V

A

T

V

I

G

G

E

D

A

N

A

S

V

V

V

I

G

G

A
|
A

G

G

A

S

V

I

V

V

T
|
T

R
x
K

D

D

V

I

E

P

P

P

R

N

V

V

S

A

V

A

G

G

I

V

P

P

A

C

R
|
R

I

V

Q

I

R
|
R

W

E

I

I

N85 (≠ L132) binding in other chain; binding in other chain
D93 (≠ H140) binding substrate
H115 (≠ S173) mutation to A: Results in an 1800-fold decrease in catalytic activity.
S142 (= S207) binding in other chain
A160 (= A225) binding in other chain
TK 165:166 (≠ TR 230:231) binding acetyl-CoA
R180 (= R245) binding acetyl-CoA
R183 (= R248) binding in other chain

Sites not aligning to the query:

1 modified: Initiator methionine, Removed; Partial
17 binding substrate
71 binding substrate

1krrA Galactoside acetyltransferase in complex with acetyl-coenzyme a (see paper)
31% identity, 48% coverage: 127:250/257 of query aligns to 79:184/200 of 1krrA

query
sites
1krrA

R

R

S

N

F

F

P

Y

A

A

L
x
N

I

F

D

N

P

L

D

T

I

I

D

V

V

D

H

D

R

Y

S

T

V

V

N

T

I

I

G

G

E

D

G

N

S

V

I

L

I
|
I

C
x
A

P
|
P

G

N

V

V

I

T

L

L

T

S

V

V

N

-

V

-

I

-

G

-

K

-

F

-

V

-

I

-

V

-

N

-

V
x
T

A

G

S
x
H

S

P

I

V

S

H

H

H

E

E

S

L

K

R

L

-

G

-

D

-

F

-

S

-

V

-

M

K

T

N

G

G

V

E

R

M

I

Y

S

S

G

F

N

P

C

I

R

T

I

I

G

G

H

N

G

N

A

V

Y

W

I

I

G
|
G

S
|
S

G

H

A

V

V

V

V

I

L
x
N

Q

P

G

G

R

V

A

T

V

I

G

G

E

D

A

N

A

S

V

V

V

I

G
|
G

A
|
A

G

G

A

S

V

I

V

V

T

T

R

K

D

D

V

I

E

P

P

P

R

N

V

V

S

A

V
x
A

G

G

I

V

P
|
P

A

C

R

R

I

V

Q

I

R
|
R

W

E

I

I

binding acetyl coenzyme *a: N84 (≠ L132), I103 (= I151), A104 (≠ C152), P105 (= P153), T112 (≠ V171), H114 (≠ S173), G140 (= G206), S141 (= S207), N146 (≠ L212), G158 (= G224), A159 (= A225), A174 (≠ V240), P177 (= P243), R182 (= R248)

Query Sequence

>WP_083780027.1 NCBI__GCF_000092905.1:WP_083780027.1
MACTPTRKNSCWAGKVWWRGVNIGEVEGAEEKGIRPLVIVGAGGMGRETAWLVERINARK
PTWNILGFVDDRRPDESLLLGYPYLGPVRSSLNKIIHEGIRPAVSVAIGDSKARFGVVSG
LFNMGIRSFPALIDPDIDVHRSVNIGEGSIICPGVILTVNVVIGKFVIVNVASSISHESK
LGDFSSVMTGVRISGNCRIGHGAYIGSGAVVLQGRAVGEAAVVGAGAVVTRDVEPRVVSV
GIPARIQRWIEVKPDDR

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