SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing GFF2243 FitnessBrowser__WCS417:GFF2243 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 15 hits to proteins with known functional sites (download)

P78753 Probable asparagine synthetase [glutamine-hydrolyzing]; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
31% identity, 59% coverage: 1:377/634 of query aligns to 1:368/557 of P78753

query
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P78753

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Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
32% identity, 56% coverage: 25:379/634 of query aligns to 25:346/497 of 1ct9A

query
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1ct9A

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active site: L50 (= L52), N74 (= N76), G75 (= G77), T305 (≠ N340), R308 (vs. gap), E332 (= E365)
binding adenosine monophosphate: L232 (≠ C261), L233 (= L262), S234 (= S263), S239 (= S268), A255 (≠ H287), V256 (≠ L288), D263 (= D297), M316 (≠ L349), S330 (≠ T363), G331 (= G364), E332 (= E365)
binding glutamine: R49 (= R51), L50 (= L52), I52 (≠ L54), V53 (= V55), N74 (= N76), G75 (= G77), E76 (= E78), D98 (= D101)

Sites not aligning to the query:

active site: 1, 366
binding glutamine: 1

P22106 Asparagine synthetase B [glutamine-hydrolyzing]; AS-B; EC 6.3.5.4 from Escherichia coli (strain K12) (see 2 papers)
30% identity, 60% coverage: 1:379/634 of query aligns to 1:363/554 of P22106

query
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P22106

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M1 (= M1) modified: Initiator methionine, Removed
C2 (= C2) mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.
H30 (= H29) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D33) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ Y82) mutation to A: 5-fold decrease in glutamine affinity.
A105 (≠ H107) mutation to H: Little effect on the kinetic properties.
E349 (= E365) mutation E->A,Q: Loss of glutamine- and ammonia-dependent synthetase activity, but still exhibits glutaminase activity.; mutation to D: 5-fold increase in affinity for aspartate when assaying both the glutamine- and ammonia-dependent synthetase reactions, and 2-fold decrease in kcat for these reactions. Modifies the product glutamate/asparagine stoichiometry.

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
27% identity, 56% coverage: 27:379/634 of query aligns to 23:366/509 of 6gq3A

query
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6gq3A

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G

T

M

Q

Q

P

P

I

I

-

R

V

V

A

K

D

K

E

Y

G

P

D

Y

L

L

V

W

M

L

M

C

V
x
Y

N
|
N

G
|
G

E
|
E

F

I

Y

Y

D

N

Y

H

Q

K

R

K

I

M

R

Q

T

Q

E

H

L

F

E

E

G

-

Y

-

G

-

C

F

R

E

F

Y

K

Q

T

T

S

K

S
x
V

D
|
D

S

G

E

E

I

I

A

I

M

L

H

H

L

L

Y

Y

R

D

R

K

H

G

G

G

V

I

-

E

R

Q

G

T

L

I

K

C

Q

M

L

L

R

D

G

G

E

V

F

F

T

A

I

F

L

V

I

L

F

L

D

D

R

T

L

A

R

N

K

K

L

V

F

F

A

L

V

G

R

R

D

D

R

T

V

Y

G

G

V

V

K

R

P

P

L

L

Y

F

Y

K

T

A

E

M

H

T

E

E

-

D

G

G

A

F

W

L

Y

A

F

V

A

C

S

S

E

E

I

A

K

K

A

G

L

L

L

V

A

T

A

-

G

-

V

-

P

-

A

-

Q

-

W

L

D

K

H

H

E

S

A

A

Y

-

A

-

N

-

R

-

G

-

F

-

I

-

L

-

R

-

D

-

R

-

T

T

V

P

F

F

N

L

N

K

I

V

R

E

S

P

V

F

K

L

P

P

G

G

C

H

W

Y

I

E

I

V

A

L

D

D

-

L

-

K

-

P

-

N

-

G

-

K

E

V

S

A

G

S

L

V

Q

E

T

M

E

V

Q

K

Y

Y

W

H

D

H

W

C

D

R

-

D

-

V

F

F

P

P

D

G

A

F

E

E

A

I

T

E

E

T

Q

V

R

K

S

N

E

-

A

-

E

-

M

-

I

-

E

-

S

N

L

L

R

R

N

I

T

L

I

F

E

N

S

A

V

V

R

K

L

K

R

R

L

L

H

M

A

T

D

D

V

R

P

R

V

I

G

G

V

C

C

L

L

L

S

S

G

G

L

L

D

D

S

S

A

L

M

V

L

A

G

A

I

T

A

L

T

L

E

K

L

Q

T

L

G

K

Q

E

S

A

-

Q

-

V

-

Q

-

Y

-

P

L

L

Q

Q

A

T

F

F

H

A

L

I

S

G

F

M

E

E

G

D

E

S

Q

P

A

-

Y

-

D

D

E

L

R

L

Q

A

Y

A

A

R

E

K

V

V

A

A

A

D

R

H

H

I

N

G

R

S

A

E

H

H

L

Y

N

E

V

V

L

L

S

-

V

F

N

N

S

S

S

E

D

E

M

G

A

I

D

Q

N

A

F

L

E

D

N

E

A

V

L

I

W

F

H

S

A

L

E

E

M

T

P

Y

F

D

A

I

N
x
T

A

T

-

V

-
x
R

H

A

S

S

V

V

A

G

K

M

Y

Y

L

L

L

I

C

S

K

K

Y

Y

V

I

-

R

Q

K

N

N

Q

T

G

D

M

S

R

V

A

V

V

I

L

F

T

S

G

G

E

E

G

G

A

S

D

D

E

E

V

L

F

T

G

Q

G

G

Y

Y

P

I

H

Y

Y

F

R

H

R

K

active site: L49 (= L52), N74 (= N76), G75 (= G77), T324 (≠ N340), R327 (vs. gap)
binding 5-oxo-l-norleucine: R48 (= R51), V51 (≠ L54), V52 (= V55), Y73 (≠ V75), N74 (= N76), G75 (= G77), E76 (= E78), V95 (≠ S100), D96 (= D101)

Sites not aligning to the query:

active site: 4
binding 5-oxo-l-norleucine: 1

P08243 Asparagine synthetase [glutamine-hydrolyzing]; Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase; EC 6.3.5.4 from Homo sapiens (Human) (see 7 papers)
27% identity, 56% coverage: 27:379/634 of query aligns to 24:379/561 of P08243

query
sites
P08243

I

I

H

A

H

H

R

R

G

G

P

P

D

D

S

A

S

F

S

R

-

F

Q

E

W

N

F

V

D

N

P

G

K

Y

G

T

Q

N

A

C

F

F

G

G

Y

F

V

H

R

R

L

L

G

A

L

V

V

V

G

D

L

P

G

L

N

F

G

G

T

M

Q

Q

P

P

I

I

-

R

V

V

A

K

D

K

E

Y

G

P

D

Y

L

L

V

W

M

L

M

C

V

Y

N

N

G

G

E

E

F

I

Y

Y

D

N

Y

H

Q

K

R

K

I

M

R

Q

T

Q

E

H

L

F

E

E

G

-

Y

-

G

-

C

F

R

E

F

Y

K

Q

T

T

S

K

S

V

D

D

S

G

E

E

I

I

A

I

M

L

H

H

L

L

Y

Y

R

D

R

K

H

G

G

G

V

I

-

E

R

Q

G

T

L

I

K

C

Q

M

L

L

R

D

G

G

E

V

F

F

T

A

I

F

L

V

I

L

F

L

D

D

R

T

L

A

R

N

K

K

L

V

F

F

A

L

V

G

R

R

D

D

R

T

V

Y

G

G

V

V

K

R

P

P

L

L

Y

F

Y

K

T

A

E

M

H

T

E

E

-

D

G

G

A

F

W

L

Y

A

F

V

A

C

S

S

E

E

I

A

K

K

A

G

L

L

L

V

A

T

A

L

G

-

V

-

P

-

A

-

Q

-

W

-

D

K

H

H

E

S

A

A

Y

-

A

-

N

-

R

-

G

-

F

-

I

-

L

-

R

-

D

-

R

-

T

T

V

P

F

F

N

L

N

K

I

V

R

E

S

P

V

F

K

L

P

P

G

G

C

H

W

Y

I

E

I

V

A

L

D

D

-

L

-

K

-

P

-

N

-

G

-

K

E

V

S

A

G

S

L

V

Q

E

T

M

E

V

Q

K

Y

Y

W

H

D

H

W

C

-

R

D

D

F
x
V

P

P

-

L

-

H

-

A

-

L

-

Y

-

D

D

N

A

V

E

E

A

K

T

L

E

F

Q

P

R

G

S

F

E

E

A

I

E

E

M

T

I

V

E

K

-

N

S

N

L

L

R

R

N

I

T

L

I

F

E

N

S

A

V

V

R

K

L

K

R

R

L

L

H

M

A

T

D

D

V

R

P

R

V

I

G

G

V

C

C

L

L

L

S

S

G

G

L

L

D

D

S

S

A

L

M

V

L

A

G

A

I

T

A

L

T

L

E

K

L

Q

T

L

G

K

Q

E

S

A

-

Q

-

V

-

Q

-

Y

-

P

L

L

Q

Q

A

T

F

F

H

A

L

I

S

G

F

M

E

E

G

D

E

S

Q

P

A

-

Y

-

D

D

E

L

R

L

Q

A

Y

A

A

R

E

K

V

V

A

A

A

D

R

H

H

I

N

G

R

S

A

E

H

H

L

Y

N

E

V

V

L

L

S

-

V

F

N

N

S

S

S

E

D

E

M

G

A

I

D

Q

N

A

F

L

E

D

N

E

A

V

L

I

W

F

H

S

A

L

E

E

M

T

P

Y

F

D

A

I

N

T

A

T

-

V

-

R

H

A

S

S

V

V

A

G

K

M

Y

Y

L

L

L

I

C

S

K

K

Y

Y

V

I

-

R

Q

K

N

N

Q

T

G

D

M

S

R

V

A

V

V

I

L
x
F

T

S

G

G

E

E

G

G

A

S

D

D

E

E

V

L

F

T

G

Q

G

G

Y

Y

P

I

H

Y

Y

F

R

H

R

K

V210 (≠ F222) to E: in dbSNP:rs1049674
F362 (≠ L362) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973

Sites not aligning to the query:

2 active site, For GATase activity; C→A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
6 A → E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974

P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
26% identity, 28% coverage: 42:217/634 of query aligns to 74:238/476 of P00497

query
sites
P00497

K

K

G

G

Q

K

A

G

A

A

F

I

G

G

Y

H

V

V

R

R

L

Y

G

A

L

T

V

A

G

G

L

G

G

G

N

G

-

Y

-

E

G

N

T

V

Q

Q

P

P

I

L

V

L

-

F

-

R

-

S

A

Q

D

N

E

N

G

G

D

S

L

L

V

A

M

L

M

A

V

H

N

N

G

G

E

N

F

L

Y

V

D

N

Y

A

Q

T

R

Q

I

L

R

K

T

Q

E

Q

L

L

E

E

G

N

Y

Q

G

G

C

S

R

I

F

F

K

Q

T

T

S

S

D

D

S

T

E

E

I

V

A

L

M

A

H

H

L

L

Y

I

R

K

R

R

H

S

G

G

V

H

R

F

G

T

L

L

K

K

-

D

-

Q

-

I

-

K

-

N

-

S

-

L

-

S

Q

M

L

L

R

K

G

G

E

A

F

Y

T

A

I

F

L

L

I

I

F

M

D

T

R

-

L

-

R

E

K

T

K

E

L

M

F

I

A

V

V

A

R

L

D

D

R

P

V

N

G

G

V

L

K

R

P

P

L

L

Y

S

Y

I

T

G

E

M

H

M

E

G

G

D

A

A

W

Y

Y

V

F

V

A

A

S

S

E

E

I

T

K

C

A

A

L

F

L

D

A

V

G

G

V

A

P

-

A

-

Q

-

W

-

D

-

H

-

E

-

A

-

Y

-

A

-

N

-

R

-

G

-

F

-

I

-

L

-

R

-

D

-

R

-

T

-

V

-

F

-

N

T

N

Y

I

L

R

R

S

E

V

V

K

E

P

P

G

G

C

E

W

M

I

L

I

I

A

I

D

N

E

D

S

E

G

G

L

M

Q

K

T

S

E

E

Q

R

Y

F

Sites not aligning to the query:

1:11 modified: propeptide
12 active site, Nucleophile; C→F: Loss of enzyme activity and N-terminal processing.
247 binding [4Fe-4S] cluster
294 binding Mg(2+)
356 binding Mg(2+)
357 binding Mg(2+)
393 binding [4Fe-4S] cluster
394 F→V: Partial loss of activity.
442 D→S: Partial loss of activity.
448 binding [4Fe-4S] cluster; C→S: Loss of activity.
451 binding [4Fe-4S] cluster; C→S: Loss of activity.
452 F→C: Lethal.

1gph1 Structure of the allosteric regulatory enzyme of purine biosynthesis (see paper)
26% identity, 28% coverage: 42:217/634 of query aligns to 63:227/465 of 1gph1

query
sites
1gph1

K

K

G

G

Q

K

A

G

A

A

F

I

G

G

Y

H

V

V

R

R

L

Y

G

A

L

T

V

A

G

G

L

G

G

G

N

G

-

Y

-

E

G

N

T

V

Q

Q

P

P

I

L

V

L

-

F

-

R

-

S

A

Q

D

N

E

N

G

G

D

S

L

L

V

A

M

L

M

A

V

H

N

N

G

G

E

N

F

L

Y

V

D

N

Y

A

Q

T

R

Q

I

L

R

K

T

Q

E

Q

L

L

E

E

G

N

Y

Q

G

G

C

S

R

I

F

F

K

Q

T

T

S

S

D

D

S

T

E

E

I

V

A

L

M

A

H

H

L

L

Y

I

R

K

R

R

H

S

G

G

V

H

R

F

G

T

L

L

K

K

-

D

-

Q

-

I

-

K

-

N

-

S

-

L

-

S

Q

M

L

L

R

K

G

G

E

A

F

Y

T

A

I

F

L

L

I

I

F

M

D

T

R

-

L

-

R

E

K

T

K

E

L

M

F

I

A

V

V

A

R

L

D

D

R

P

V

N

G

G

V

L

K

R

P

P

L

L

Y

S

Y

I

T

G

E

M

H

M

E

G

G

D

A

A

W

Y

Y

V

F

V

A

A

S

S

E

E

I

T

K

C

A

A

L

F

L

D

A

V

G

G

V

A

P

-

A

-

Q

-

W

-

D

-

H

-

E

-

A

-

Y

-

A

-

N

-

R

-

G

-

F

-

I

-

L

-

R

-

D

-

R

-

T

-

V

-

F

-

N

T

N

Y

I

L

R

R

S

E

V

V

K

E

P

P

G

G

C

E

W

M

I

L

I

I

A

I

D

N

E

D

S

E

G

G

L

M

Q

K

T

S

E

E

Q

R

Y

F

Sites not aligning to the query:

active site: 300, 305, 315, 423
binding adenosine monophosphate: 242, 242, 244, 245, 246, 282, 283, 283, 304, 305, 307, 345, 346, 347, 349, 350, 353, 388
binding iron/sulfur cluster: 236, 237, 382, 384, 388, 437, 440

Q9STG9 Amidophosphoribosyltransferase 2, chloroplastic; AtATase2; AtPURF2; PRPP2; Glutamine phosphoribosylpyrophosphate amidotransferase 2; AtGPRAT2; Protein CHLOROPLAST IMPORT APPARATUS 1; Protein DIFFERENTIAL DEVELOPMENT OF VASCULAR ASSOCIATED CELLS; EC 2.4.2.14 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 29% coverage: 2:187/634 of query aligns to 87:304/561 of Q9STG9

query
sites
Q9STG9

C

C

G

G

Y

V

I

V

G

G

V

I

F

Y

A

G

K

D

Q

S

P

E

R

A

A

S

F

-

N

-

P

-

N

R

M

L

F

C

D

Y

A

L

A

A

L

L

R

H

A

A

I

L

H

Q

H

H

R

R

G

G

P

Q

D

E

-

G

-

A

-

G

-

I

-

V

-

T

-

V

-

S

-

K

-

D

-

K

-

V

-

L

-

Q

-

T

-

I

-

T

-

G

-

V

-

G

-

L

-

V

-

S

-

E

-

V

-

F

S

S

S

E

S

S

Q

K

W

L

F

D

D

Q

P

L

K

P

G

G

Q

D

A

I

A

A

F

I

G

G

Y

H

V

V

R

R

L

Y

G

S

L

T

V

A

G

G

-

S

L

M

G

L

N

K

G

N

T

V

Q

Q

P

P

I

F

V

V

A

A

D

G

E

Y

-

R

-

F

G

G

D

S

L

V

V

G

M

V

M

A

V
x
H

N

N

G

G

E

N

F

L

Y

V

D

N

Y

Y

Q

T

R

K

I

L

R

R

T

A

E

D

L

L

E

E

G

E

Y

N

G

G

C

S

R

I

F

F

K

N

T

T

S

S

D

D

S

T

E

E

I

V

A

V

M

L

H

H

L

L

Y

I

R

A

R

I

H

S

G

K

V

A

R

R

-

P

-

F

-

M

-

R

-

I

-

V

-

D

G

A

L

C

K

E

Q

K

L

L

R

Q

G

G

E

A

F

Y

T

S

I

M

L

V

I

F

F

V

D

T

R

-

L

-

R

E

K

D

K

K

L

L

F

V

A

A

V

V

R

R

D

D

R

P

V

H

G

G

V

F

K
x
R

P
|
P

L

L

Y

V

Y

M

T

G

E

R

H

R

E

S

-

N

G

G

A

A

W

V

Y

V

F

F

A

A

S

S

E

E

I

T

K

C

A

A

L

L

L

D

A

L

A

-

G

-

V

I

P

E

A

A

Q

T

W

Y

D

E

H

R

E

E

A

V

Y

Y

A

P

N

G

R

E

G

V

F

L

I

V

L

V

H187 (≠ V75) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K146) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P147) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.

Sites not aligning to the query:

371 G→S: Low resistance to the bleaching herbicides DAS073 and DAS734.
476 P→S: Resistance to the bleaching herbicides DAS073 and DAS734.
494 Y→F: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with S-265.

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
27% identity, 29% coverage: 2:187/634 of query aligns to 1:218/460 of 6lbpA

query
sites
6lbpA

C
|
C

G

G

Y

V

I

V

G

G

V

I

F

Y

A

G

K

D

Q

S

P

E

R

A

A

S

F

-

N

-

P

-

N

R

M

L

F

C

D

Y

A

L

A

A

L

L

R

H

A

A

I

L

H

Q

H

H

R

R

G
|
G

P

Q

D

E

-

G

-

A

-

G

-

I

-

V

-

T

-

V

-

S

-

K

-

D

-

K

-

V

-

L

-

Q

-

T

-

I

-

T

-

G

-

V

-

G

-

L

-

V

-

S

-

E

-

V

-

F

S

S

S

E

S

S

Q

K

W

L

F

D

D

Q

P

L

K

P

G

G

Q

D

A

I

A

A

F

I

G

G

Y

H

V

V

R

R

L

Y

G

S

L

T

V

A

G

G

-

S

L

M

G

L

N

K

G

N

T

V

Q

Q

P

P

I

F

V

V

A

A

D

G

E

Y

-

R

-

F

G

G

D

S

L

V

V

G

M

V

M

A

V

H

N
|
N

G
|
G

E

N

F

L

Y

V

D

N

Y

Y

Q

T

R

K

I

L

R

R

T

A

E

D

L

L

E

E

G

E

Y

N

G

G

C

S

R

I

F

F

K

N

T

T

S

S

D

D

S

T

E

E

I

V

A

V

M

L

H

H

L

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

-

P

Y

F

R

F

R

M

H

R

G

I

V

V

R

D

G

A

L

C

K

E

Q

K

L

L

R

Q

G

G

E

A

F

Y

T

S

I

M

L

V

I

F

F

V

D

T

R

-

L

-

R

E

K

D

K

K

L

L

F

V

A

A

V

V

R

R

D

D

R

P

V

H

G

G

V

F

K

R

P

P

L

L

Y

V

Y

M

T

G

E

R

H

R

E

S

-

N

G

G

A

A

W

V

Y

V

F

F

A

A

S

S

E

E

I

T

K

C

A

A

L

L

L

D

A

L

A

-

G

-

V

I

P

E

A

A

Q

T

W

Y

D

E

H

R

E

E

A

V

Y

Y

A

P

N

G

R

E

G

V

F

L

I

V

L

V

active site: C1 (= C2), G27 (= G31), N102 (= N76), G103 (= G77)

Sites not aligning to the query:

active site: 243, 301, 306, 316, 424
binding iron/sulfur cluster: 237, 239, 383, 385, 434, 436, 437

1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
27% identity, 28% coverage: 42:217/634 of query aligns to 63:223/455 of 1ao0A

query
sites
1ao0A

K

K

G

G

Q

K

A

G

A

A

F

I

G

G

Y

H

V

V

R

R

L

Y

G

A

L

-

V

T

G

G

L

Y

G

E

N

N

G

-

T

V

Q

Q

P

P

I

L

V

L

-

F

-

R

-

S

A

Q

D

N

E

N

G

G

D

S

L

L

V

A

M

L

M

A

V

H

N
|
N

G
|
G

E

N

F

L

Y

V

D

N

Y

A

Q

T

R

Q

I

L

R

K

T

Q

E

Q

L

L

E

E

G

N

Y

Q

G

G

C

S

R

I

F

F

K

Q

T

T

S

S

D

D

S

T

E

E

I

V

A

L

M

A

H

H

L

L

Y

I

R

K

R

R

H

S

G

G

V

H

R

F

G

T

L

L

K

K

-

D

-

Q

-

I

-

K

-

N

-

S

-

L

-

S

Q

M

L

L

R

K

G

G

E

A

F

Y

T

A

I

F

L

L

I

I

F

M

D

T

R

-

L

-

R

E

K

T

K

E

L

M

F

I

A

V

V

A

R

L

D

D

R

P

V

N

G

G

V

L

K

R

P

P

L

L

Y

S

Y

I

T

G

E

M

H

M

E

G

G

D

A

A

W

Y

Y

V

F

V

A

A

S

S

E

E

I

T

K

C

A

A

L

F

L

D

A

V

G

G

V

A

P

-

A

-

Q

-

W

-

D

-

H

-

E

-

A

-

Y

-

A

-

N

-

R

-

G

-

F

-

I

-

L

-

R

-

D

-

R

-

T

-

V

-

F

-

N

T

N

Y

I

L

R

R

S

E

V

V

K

E

P

P

G

G

C

E

W

M

I

L

I

I

A

I

D

N

E

D

S

E

G

G

L

M

Q

K

T

S

E

E

Q

R

Y

F

active site: N98 (= N76), G99 (= G77)

Sites not aligning to the query:

active site: 1, 27, 238, 296, 301, 311, 419
binding guanosine-5'-monophosphate: 234, 238, 279, 341, 342, 343, 345, 346, 347, 348, 349
binding adenosine-5'-diphosphate: 25, 238, 240, 241, 242, 277, 278, 279, 300, 301, 301, 303
binding magnesium ion: 279, 341, 342
binding iron/sulfur cluster: 232, 233, 234, 378, 380, 433, 436

Q9XB61 Carbapenam-3-carboxylate synthase; Carbapenam-3-carboxylate ligase; EC 6.3.3.6 from Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp. carotovora) (see 3 papers)
23% identity, 43% coverage: 99:373/634 of query aligns to 79:353/503 of Q9XB61

query
sites
Q9XB61

S

A

S

N

D

D

S

A

E

E

I

L

A

L

M

A

H

L

L

L

Y

F

R

T

R

R

H

L

G

G

V

A

R

N

G

A

L

L

K

A

Q

L

L

A

R

E

G

G

E

D

F

F

T

C

I

F

L

F

I

I

F

-

D

D

R

E

L

P

R

N

K

G

K

E

L

L

F

T

A

V

V

I

R

T

D

E

R

S

V

R

G

G

V

F

K

S

P

P

L

V

Y

H

Y

V

T

V

E

Q

H

G

E

K

G

K

A

A

W

W

Y

M

F

T

A

N

S

S

E

L

I

K

K

L

A

V

L

T

L

A

A

A

A

E

G

G

V

E

P

G

A

A

Q

L

W

W

-

F

D

E

H

E

E

E

A

A

Y

L

A

V

N

C

R

Q

G

S

F

L

I

M

L

R

R

A

D

D

R

T

-

Y

T

T

V

P

F

V

N

K

N

N

I

A

R

Q

S

R

V

L

K

K

P

P

G

G

C

A

W

V

I

H

I

V

A

L

D

-

E

-

S

-

G

-

L

-

Q

-

T

T

E

H

Q

D

Y

S

W

E

D

G

W

Y

D

S

F

F

P

V

D

E

A

S

E

R

A

T

T

L

E

T

Q

T

R

P

S

A

E

S

A

N

E

Q

M

L

I

L

-

A

-

L

-

P

-

R

E

E

S

P

L

L

R

L

N

A

T

L

I

I

E

D

E

R

S

Y

V

L

R

N

L

A

R

P

L

L

H

E

A

D

D

L

V

A

P

P

-

R

-

F

-

D

-

T

V

V

G

G

V

I

C
x
P

L
|
L

S
|
S

G
|
G

L
|
L

D
|
D

S
|
S

S

S

A

-

M

-

L

-

G

-

I

L

A

V

T

T

E

A

L

L

T

A

G

S

Q

R

S

H

L

F

Q

K

A

K

F

L

H

N

L

T

S

Y

F

S

E
x
I

G

G

E

T

Q

E

A

L

Y

S

D

N

E

E

R

F

Q

E

Y

F

A

S

E

Q

V

Q

A

V

A

A

R

D

H

A

N

L

R

G

A

T

H

H

L

H

N

Q

V

M

L

K

S

I

V

L

N

S

S

E

S

T

D

E

M

V

A

I

D

N

N

G

F

I

E

I

N

E

A

S

L

I

W

Y

H

Y

A

N

E

E

M

I

P

F

F

D

A

G

N

L

A

S

H

A

S

E

V

I

A

Q

K

S

Y

G

L

L

L

F

C

N

K

V

Y

Y

V

R

Q

Q

N

A

Q

Q

G

G

-

Q

M

V

R

S

A

C

V

M

L

L

T

T

G
|
G

E
x
Y

G
|
G

A
x
S

D
|
D

E

L

V

L

F

F

G

G

244:251 (vs. 261:268, 88% identical) binding ATP
I270 (≠ E291) binding ATP
GYGSD 344:348 (≠ GEGAD 364:368) binding ATP
Y345 (≠ E365) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G366) binding substrate

Sites not aligning to the query:

371 binding substrate
374 binding substrate
380 E→A: Loss of activity.; E→D: Reduces catalytic efficiency.; E→Q: Reduces catalytic efficiency.
421 binding ATP
443 mutation K->A,M: Loss of activity.
444:446 binding ATP

1q19A Carbapenam synthetase (see paper)
23% identity, 43% coverage: 99:373/634 of query aligns to 78:352/500 of 1q19A

query
sites
1q19A

S

A

S

N

D

D

S

A

E

E

I

L

A

L

M

A

H

L

L

L

Y

F

R

T

R

R

H

L

G

G

V

A

R

N

G

A

L

L

K

A

Q

L

L

A

R

E

G

G

E

D

F

F

T

C

I

F

L

F

I

I

F

-

D

D

R

E

L

P

R

N

K

G

K

E

L

L

F

T

A

V

V

I

R

T

D

E

R

S

V

R

G

G

V

F

K

S

P

P

L

V

Y

H

Y

V

T

V

E

Q

H

G

E

K

G

K

A

A

W

W

Y

M

F

T

A

N

S

S

E

L

I

K

K

L

A

V

L

T

L

A

A

A

A

E

G

G

V

E

P

G

A

A

Q

L

W

W

-

F

D

E

H

E

E

E

A

A

Y

L

A

V

N

C

R

Q

G

S

F

L

I

M

L

R

R

A

D

D

R

T

-

Y

T

T

V

P

F

V

N

K

N

N

I

A

R

Q

S

R

V

L

K

K

P

P

G

G

C

A

W

V

I

H

I

V

A

L

D

-

E

-

S

-

G

-

L

-

Q

-

T

T

E

H

Q

D

Y

S

W

E

D

G

W

Y

D

S

F

F

P

V

D

E

A

S

E

R

A

T

T

L

E

T

Q

T

R

P

S

A

E

S

A

N

E

Q

M

L

I

L

-

A

-

L

-

P

-

R

E

E

S

P

L

L

R

L

N

A

T

L

I

I

E

D

E

R

S

Y

V

L

R

N

L

A

R

P

L

L

H

E

A

D

D

L

V

A

P

P

-

R

-

F

-

D

-

T

V

V

G

G

V

I

C
x
P

L
|
L

S
|
S

G

G

L

L

D
|
D

S
|
S

S

S

A

-

M

-

L

-

G

-

I

L

A

V

T

T

E

A

L

L

T

A

G

S

Q

R

S

H

L

F

Q

K

A

K

F

L

H

N

L

T

S

Y

F
x
S

E
x
I

G

G

E

T

Q

E

A

L

Y

S

D

N

E

E

R

F

Q

E

Y

F

A

S

E

Q

V

Q

A

V

A

A

R

D

H

A

N

L

R

G

A

T

H

H

L

H

N

Q

V

M

L

K

S

I

V

L

N

S

S

E

S

T

D

E

M

V

A

I

D

N

N

G

F

I

E

I

N

E

A

S

L

I

W

Y

H

Y

A

N

E

E

M

I

P

F

F

D

A

G

N
x
L

A

S

H

A

S
x
E

V

I

A

Q

K

S

Y

G

L

L

L

F

C

N

K

V

Y

Y

V

R

Q

Q

N

A

Q

Q

G

G

-

Q

M

V

R

S

A

C

V

M

L

L

T
|
T

G
|
G

E
x
Y

G
|
G

A

S

D
|
D

E
x
L

V

L

F

F

G

G

active site: L318 (≠ N340), E321 (≠ S343), Y344 (≠ E365)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ C261), L244 (= L262), S245 (= S263), D249 (= D267), S250 (= S268), S268 (≠ F290), I269 (≠ E291), T342 (= T363), G343 (= G364), D347 (= D368)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ E365), G345 (= G366), L348 (≠ E369)

Sites not aligning to the query:

active site: 56, 379, 442
binding diphosphomethylphosphonic acid adenosyl ester: 442, 443, 444, 445
binding (2s,5s)-5-carboxymethylproline: 373, 379

1jgtB Crystal structure of beta-lactam synthetase (see paper)
24% identity, 47% coverage: 74:373/634 of query aligns to 71:353/500 of 1jgtB

query
sites
1jgtB

M

V

V

L

N
x
A

G
|
G

E

E

F

I

Y

Y

D

N

Y

R

Q

D

R

E

I

L

R

L

T

S

E

V

L

L

E

P

G

A

Y

G

G

P

C

A

R

-

F

-

K

-

T

P

S

E

S

G

D

D

S

A

E

E

I

L

A

V

M

L

H

R

L

L

Y

L

R

E

R

R

H

Y

G

D

V

L

R

H

G

A

L

F

K

R

Q

L

L

V

R

N

G

G

E

R

F

F

T

A

I

T

L

V

I

V

F

-

D

-

R

R

L

T

R

G

K

D

K

R

L

V

F

L

A

L

V

A

R

T

D

D

R

H

V

A

G

G

V

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

E

V

H

A

E

P

G

G

A

E

W

V

Y

R

F

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

L

A

A

A

A

H

G

R

V

D

P

P

A

-

Q

-

W

-

D

-

H

-

E

-

A

-

Y

-

A

-

N

-

R

K

G

G

F

F

I

P

L

L

R

A

D

D

-

A

R

R

T

R

V

V

-

A

-

G

F

L

N

T

N

G

I

V

R

Y

S

Q

V

V

K

P

P

A

G

G

C

A

W

V

I

M

I

D

A

I

D

D

E

L

S

G

G

S

L

G

Q

T

T

A

E

V

Q

T

Y

H

W

R

D

T

W

W

D

-

F

-

P

-

D

-

A

T

E

P

A

G

T

L

E

S

Q

R

R

R

-

I

-

L

S

P

E

E

A

G

E

E

M

A

I

V

E

A

S

A

L

V

R

R

N

A

T

A

I

L

E

E

E

K

S

A

V

V

R

A

L

Q

R

R

L

V

H

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

C
x
V

L
|
L

S
|
S

G

G

G
|
G

L
x
I

D
|
D

S
|
S

S

S

A

G

M

V

L

A

G

A

I

C

A

A

T

H

E

R

L

A

T

A

G

G

Q

E

S

-

L

L

Q

D

A

T

F

V

H
x
S

L
x
M

S

-

F

-

E

-

G

G

E

T

Q

D

A

T

Y

S

D

N

E

E

R

F

Q

R

Y

E

A

A

E

R

V

A

A

V

R

D

H

H

N

L

R

R

A

T

H

R

L

H

N

R

V

E

L

I

S

T

V

I

N

P

S

T

D

E

M

L

A

L

D

A

N

Q

F

L

E

P

N

Y

A

A

L

V

W

W

H

A

A

S

E

E

M

-

P

-

F

-

A

S

N

V

A

D

H

P

S
x
D

V

I

A

I

K

E

Y
|
Y

L

L

C

P

K
x
L

Y

T

V

A

Q

L

N

Y

Q

R

G

A

M

L

-

D

-

G

-

P

-

E

R

R

A

R

V

I

L

L

T

T

G
|
G

E
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

G

G

active site: A73 (≠ N76), G74 (= G77), D319 (≠ S343), Y345 (≠ E365)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ C261), L245 (= L262), S246 (= S263), G248 (= G265), I249 (≠ L266), D250 (= D267), S251 (= S268), S269 (≠ H287), M270 (≠ L288), L327 (≠ K351), G344 (= G364), Y345 (≠ E365), D348 (= D368)
binding n2-(carboxyethyl)-l-arginine: Y323 (= Y347), Y345 (≠ E365), G346 (= G366), D348 (= D368), I349 (≠ E369)
binding magnesium ion: D250 (= D267), D348 (= D368)

Sites not aligning to the query:

active site: 379, 440
binding diphosphomethylphosphonic acid adenosyl ester: 420, 440
binding n2-(carboxyethyl)-l-arginine: 354, 370, 379

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
23% identity, 47% coverage: 74:373/634 of query aligns to 67:345/496 of 1mbzA

query
sites
1mbzA

M

V

V

L

N
x
A

G
|
G

E

E

F

I

Y

Y

D

N

Y

R

Q

D

R

E

I

L

R

L

T

S

E

V

L

L

E

P

G

A

Y

G

G

P

C

A

R

-

F

-

K

-

T

P

S

E

S

G

D

D

S

A

E

E

I

L

A

V

M

L

H

R

L

L

Y

L

R

E

R

R

H

Y

G

D

V

L

R

H

G

A

L

F

K

R

Q

L

L

V

R

N

G

G

E

R

F

F

T

A

I

T

L

V

I

V

F

-

D

-

R

R

L

T

R

G

K

D

K

R

L

V

F

L

A

L

V

A

R

T

D

D

R

H

V

A

G

G

V

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

E

V

H

A

E

P

G

G

A

E

W

V

Y

R

F

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

L

A

A

A

A

H

G

G

V

F

P

P

A

L

Q

A

W

-

D

D

H

A

E

R

A

R

Y

V

A

A

N

G

R

-

G

-

F

-

I

-

L

-

R

-

D

-

R

-

T

-

V

-

F

L

N

T

N

G

I

V

R

Y

S

Q

V

V

K

P

P

A

G

G

C

A

W

V

I

M

I

D

A

I

D

D

E

L

S

G

G

S

L

G

Q

T

T

A

E

V

Q

T

Y

H

W

R

D

T

W

W

D

-

F

-

P

-

D

-

A

T

E

P

A

G

T

L

E

S

Q

R

R

R

-

I

-

L

S

P

E

E

A

G

E

E

M

A

I

V

E

A

S

A

L

V

R

R

N

A

T

A

I

L

E

E

E

K

S

A

V

V

R

A

L

Q

R

R

L

V

H

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

C
x
V

L
|
L

S
|
S

G

G

G
|
G

L

I

D
|
D

S
|
S

S

S

A

G

M

V

L

A

G

A

I

C

A

A

T

H

E

R

L

A

T

A

G

G

Q

E

S

-

L

L

Q

D

A

T

F

V

H
x
S

L
x
M

S

-

F

-

E

-

G

G

E

T

Q

D

A

T

Y

S

D

N

E

E

R

F

Q

R

Y

E

A

A

E

R

V

A

A

V

R

D

H

H

N

L

R

R

A

T

H

R

L

H

N

R

V

E

L

I

S

T

V

I

N

P

S

T

D

E

M

L

A

L

D

A

N

Q

F

L

E

P

N

Y

A

A

L

V

W

W

H

A

A

S

E

E

M

S

P

V

F

D

A

P

N
x
D

A

-

H

-

S

-

V

I

A

I

K

E

Y
|
Y

L

L

C

P

K
x
L

Y

T

V

A

Q

L

N

Y

Q

R

G

A

M

L

-

D

-

G

-

P

-

E

R

R

A

R

V

I

L

L

T

T

G
|
G

E
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

G

G

active site: A69 (≠ N76), G70 (= G77), D311 (≠ N340), Y337 (≠ E365)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ C261), L237 (= L262), S238 (= S263), S243 (= S268), S261 (≠ H287), M262 (≠ L288), Y315 (= Y347), L319 (≠ K351), G336 (= G364), Y337 (≠ E365), G338 (= G366), D340 (= D368), I341 (≠ E369)
binding magnesium ion: D242 (= D267), D340 (= D368)
binding pyrophosphate 2-: S238 (= S263), G240 (= G265), D242 (= D267), S243 (= S268), D340 (= D368)

Sites not aligning to the query:

active site: 371, 432
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: 362, 371, 432, 434, 435
binding pyrophosphate 2-: 412, 432, 433

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
23% identity, 47% coverage: 74:373/634 of query aligns to 63:340/491 of 1mc1A

query
sites
1mc1A

M

V

V

L

N
x
A

G
|
G

E

E

F

I

Y

Y

D

N

Y

R

Q

D

R

E

I

L

R

L

T

S

E

V

L

L

E

P

G

A

Y

G

G

P

C

A

R

-

F

-

K

-

T

P

S

E

S

G

D

D

S

A

E

E

I

L

A

V

M

L

H

R

L

L

Y

L

R

E

R

R

H

Y

G

D

V

L

R

H

G

A

L

F

K

R

Q

L

L

V

R

N

G

G

E

R

F

F

T

A

I

T

L

V

I

V

F

-

D

-

R

R

L

T

R

G

K

D

K

R

L

V

F

L

A

L

V

A

R

T

D

D

R

H

V

A

G

G

V

S

K

V

P

P

L

L

Y

Y

Y

T

T

C

E

V

H

A

E

P

G

G

A

E

W

V

Y

R

F

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

L

A

A

A

A

-

G

-

V

-

P

-

A

-

Q

-

W

-

D

-

H

-

E

-

A

-

Y

-

A

-

N

-

R

-

G

G

F

F

I

P

L

L

R

A

D

D

-

A

R

R

T

R

V

V

-

A

-

G

F

L

N

T

N

G

I

V

R

Y

S

Q

V

V

K

P

P

A

G

G

C

A

W

V

I

M

I

D

A

I

D

D

E

L

S

G

G

S

L

G

Q

T

T

A

E

V

Q

T

Y

H

W

R

D

T

W

W

D

-

F

-

P

-

D

-

A

T

E

P

A

G

T

L

E

S

Q

R

R

R

-

I

-

L

S

P

E

E

A

G

E

E

M

A

I

V

E

A

S

A

L

V

R

R

N

A

T

A

I

L

E

E

E

K

S

A

V

V

R

A

L

Q

R

R

L

V

H

T

-

P

A

G

D

D

V

T

P

P

V

L

G

-

V

V

C
x
V

L

L

S
|
S

G

G

G
|
G

L

I

D
|
D

S
|
S

S

S

A

G

M

V

L

A

G

A

I

C

A

A

T

H

E

R

L

A

T

A

G

G

Q

E

S

-

L

L

Q

D

A

T

F

V

H
x
S

L
x
M

S

-

F

-

E

-

G

G

E

T

Q

D

A

T

Y

S

D

N

E

E

R

F

Q

R

Y

E

A

A

E

R

V

A

A

V

R

D

H

H

N

L

R

R

A

T

H

R

L

H

N

R

V

E

L

I

S

T

V

I

N

P

S

T

D

E

M

L

A

L

D

A

N

Q

F

L

E

P

N

Y

A

A

L

V

W

W

H

A

A

S

E

E

M

S

P

V

F

D

A

P

N
x
D

A

-

H

-

S

-

V

I

A

I

K

E

Y
|
Y

L

L

C

P

K

L

Y

T

V

A

Q

L

N

Y

Q

R

G

A

M

L

-

D

-

G

-

P

-

E

R

R

A

R

V

I

L

L

T

T

G
|
G

E
x
Y

G
|
G

A

A

D
|
D

E
x
I

V

P

F

L

G

G

active site: A65 (≠ N76), G66 (= G77), D306 (≠ N340), Y332 (≠ E365)
binding adenosine monophosphate: V231 (≠ C261), S233 (= S263), S238 (= S268), S256 (≠ H287), M257 (≠ L288), G331 (= G364)
binding magnesium ion: D237 (= D267), D335 (= D368)
binding deoxyguanidinoproclavaminic acid: Y310 (= Y347), Y332 (≠ E365), G333 (= G366), I336 (≠ E369)
binding pyrophosphate 2-: S233 (= S263), G235 (= G265), D237 (= D267), S238 (= S268), D335 (= D368)

Sites not aligning to the query:

active site: 366, 427
binding adenosine monophosphate: 427, 430
binding deoxyguanidinoproclavaminic acid: 357, 366, 427
binding pyrophosphate 2-: 407, 427, 428

Query Sequence

>GFF2243 FitnessBrowser__WCS417:GFF2243
MCGYIGVFAKQPRAFNPNMFDAALRAIHHRGPDSSSQWFDPKGQAAFGYVRLGLVGLGNG
TQPIVADEGDLVMMVNGEFYDYQRIRTELEGYGCRFKTSSDSEIAMHLYRRHGVRGLKQL
RGEFTILIFDRLRKKLFAVRDRVGVKPLYYTEHEGAWYFASEIKALLAAGVPAQWDHEAY
ANRGFILRDRTVFNNIRSVKPGCWIIADESGLQTEQYWDWDFPDAEATEQRSEAEMIESL
RNTIEESVRLRLHADVPVGVCLSGGLDSSAMLGIATELTGQSLQAFHLSFEGEQAYDERQ
YAEVAARHNRAHLNVLSVNSSDMADNFENALWHAEMPFANAHSVAKYLLCKYVQNQGMRA
VLTGEGADEVFGGYPHYRRDMVLYNHENQDPSAIAELSRRLHASEDRYLPGGKNDVKWVQ
DELGHGVSWLQTQSALFGPLAQLYSDDFHERFSHTDAYREFYDRLSPRALNGWEPVNRSL
YMVAKSSLPNVVLTSLGDRMEMAGSLEGRPPLLDHQVIEAACRLPVNMKVRGATEKYALR
EAMRPYVPQAVLDRKKQYFRAPPASESPQSKLYEMINDVLSGPTLNNVPFFDPRKVRALL
ATLPSLSTAQRASADNLLMEIAGLCLMQKRFALN

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