SitesBLAST

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 (= H30) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D34) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ Y81) mutation to A: 5-fold decrease in glutamine affinity.
A105 (≠ H106) mutation to H: Little effect on the kinetic properties.
E349 (≠ D366) 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.

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
30% identity, 62% coverage: 2:395/636 of query aligns to 1:366/497 of 1ct9A

query
sites
1ct9A

C
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A

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M

active site: A1 (≠ C2), L50 (= L51), N74 (= N75), G75 (= G76), T305 (≠ P339), R308 (≠ D342), E332 (≠ D366), M366 (≠ L395)
binding adenosine monophosphate: L232 (≠ F265), L233 (= L266), S234 (= S267), S239 (= S272), A255 (≠ S291), V256 (≠ I292), D263 (≠ E301), M316 (≠ V351), S330 (= S364), G331 (= G365), E332 (≠ D366)
binding glutamine: A1 (≠ C2), R49 (= R50), L50 (= L51), I52 (≠ V53), V53 (≠ I54), N74 (= N75), G75 (= G76), E76 (= E77), D98 (= D100)

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)
29% identity, 59% coverage: 1:375/636 of query aligns to 1:365/557 of P78753

query
sites
P78753

M

M

C

C

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G

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Y

Sites not aligning to the query:

391 modified: Phosphoserine
489 modified: Phosphoserine

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, 59% coverage: 1:375/636 of query aligns to 1:374/561 of P08243

query
sites
P08243

M

M

C
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C

G

G

I

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G
x
A

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M

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x
F

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Y

Y

C2 (= C2) active site, For GATase activity; mutation to A: Loss of the glutamine-dependent asparagine synthetase activity, while the ammonia-dependent activity remained unaffected.
A6 (≠ G6) to E: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122975
V210 (≠ L209) to E: in dbSNP:rs1049674
F362 (≠ L363) to V: in ASNSD; dramatic reduction in protein abundance; dbSNP:rs398122973

Sites not aligning to the query:

550 R → C: in ASNSD; increases level of protein abundance; dbSNP:rs398122974

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
26% identity, 59% coverage: 2:375/636 of query aligns to 1:361/509 of 6gq3A

query
sites
6gq3A

C
|
C

G

G

I

I

S
x
W

G

A

I

L

F

F

D

G

T

S

R

D

G

D

T

C

G

L

T

S

I

V

P

Q

R

C

D

L

L

S

I

A

S

M

R

K

I

I

N

-

V

-

Q

-

S

A

H

H

R

R

G

G

P

P

D

D

E

A

-

F

-

R

-

F

N

E

E

N

V

V

H

N

L

G

E

Y

P

T

G

N

L

C

A

C

L

F

G

G

H

F

R

H

R
|
R

L
|
L

S

A

V
|
V

I
x
V

D

D

L

P

A

L

T

F

G

G

T

M

Q

Q

P

P

L

I

-

R

F

V

N

K

E

K

D

Y

G

P

T

Y

V

L

G

W

I

L

V

C

F
x
Y

N
|
N

G
|
G

E
|
E

I

I

Y

Y

N

N

Y

H

L

K

E

K

L

M

M

Q

Q

Q

E

H

L

F

N

E

D

-

L

-

G

-

Y

F

R

E

F

Y

R

Q

T

T

R

K

S
x
V

D
|
D

T

G

E

E

V

I

I

I

V

L

H

H

A

L

W

Y

Q

D

A

K

W

G

G

G

-

I

E

E

A

Q

C

T

V

I

H

C

R

M

L

L

R

D

G

G

M

V

F

F

A

A

F

F

A

V

L

L

W

L

D

D

R

T

K

A

H

N

Q

K

T

K

L

V

F

F

L

L

A

G

R

R

D

D

R

T

M

Y

G

G

V

V

K

R

P

P

M

L

H

F

Y

K

A

A

W

M

L

T

P

E

D

D

G

G

S

F

F

L

I

A

F

V

G

C

S

S

E

E

L

A

K

K

V

-

L

-

T

-

A

-

H

-

P

-

G

-

F

-

V

-

R

-

D

-

I

-

D

-

P

-

L

-

A

-

V

-

E

-

G

G

Y

L

F

V

S

T

F

L

G

K

Y

H

V

S

P

A

D

T

P

P

R

-

C

-

I

-

Y

F

Q

L

N

K

A

V

H

E

K

P

L

F

P

L

A

P

A

G

H

H

T

Y

L

E

T

V

L

L

R

D

R

L

G

K

D

P

A

N

G

G

R

K

P

V

A

A

P

S

R

V

P

E

Y

M

W

V

D

K

V

Y

R

H

F

H

T

C

N

R

D

D

-

V

-

F

N

P

P

G

I

F

K

E

L

I

Q

E

D

T

A

V

Q

K

A

N

E

N

L

L

R

R

E

I

R

L

V

F

R

N

E

N

S

A

V

V

R

K

L

K

R

R

M

L

I

M

A

T

D

D

V

R

P

R

L

I

G

G

A

C

F

L

L

L

S

S

G

G

V

L

D

D

S

S

A

L

V

V

V

A

A

A

T

T

M

L

-

L

-

K

-

Q

-

L

-

K

A

E

G

A

L

Q

S

V

S

Q

T

Y

P

P

V

L

H

Q

T

T

C

F

S

A

I

I

G

G

F

M

D

E

D

D

P

S

R

-

F

-

D

P

E

D

S

L

F

A

A

A

Q

R

Q

K

V

V

A

A

D

D

H

H

Y

I

R

G

T

S

D

E

H

H

R

Y

L

E

D

V

I

L

V

F

S

N

S

S

D

E

-

G

F

I

D

Q

L

A

I

L

D

D

T

E

L

V

A

I

W

F

-

S

-

L

-

E

L

T

Y

Y

D

D

E

I

P
x
T

F

T

A

V

D
x
R

S

A

S

S

A

-

I

V

P

G

T

M

Y

Y

R

L

V

I

C

S

Q

K

M

Y

A

I

R

R

K

K

H

N

V

T

-

D

-

S

T

V

V

V

A

I

L

F

S

S

G

G

D

E

G

G

G

S

D

D

E

E

S

L

M

T

G

Q

G

G

Y

Y

active site: W4 (≠ S5), L49 (= L51), N74 (= N75), G75 (= G76), T324 (≠ P339), R327 (≠ D342)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (= R50), V51 (= V53), V52 (≠ I54), Y73 (≠ F74), N74 (= N75), G75 (= G76), E76 (= E77), V95 (≠ S99), D96 (= D100)

6lbpA Structure of the glutamine phosphoribosylpyrophosphate amidotransferase from arabidopsis thaliana (see paper)
27% identity, 26% coverage: 35:201/636 of query aligns to 57:243/460 of 6lbpA

query
sites
6lbpA

E

E

N

S

E

K

V

L

H

D

L

Q

E

L

P

P

G

G

-

D

L

I

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

S

V

T

I

A

-

G

-

S

D

S

L

M

A

L

T

K

G

N

T

V

Q

Q

P

P

L

F

F

V

N

A

-

G

-

Y

E

R

D

F

G

G

T

S

V

V

G

G

I

V

V

A

F

H

N
|
N

G
|
G

E

N

I

L

Y

V

N

N

Y

Y

L

T

E

K

L

L

M

R

Q

A

E

D

L

L

N

E

D

E

L

N

G

G

Y

S

R

I

F

F

R

N

T

T

R

S

S

S

D

D

T

T

E

E

V

V

I

V

V

L

H

H

A

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

-

P

-

F

W

F

Q

M

A

R

W

I

G

V

E

D

A

A

C

C

V

-

H

E

R

K

L

L

R

Q

G

G

M

-

F

-

A

A

F

Y

A

S

L

M

W

V

D

F

R

V

K

T

H

E

Q

D

T

K

L

L

F

V

L

A

A

V

R

R

D

D

R

P

M

H

G

G

V

F

K

R

P

P

M

L

H

V

Y

M

A

G

W

R

L

R

P

S

D

N

G

G

S

A

F

V

I

V

F

F

G

A

S

S

E

E

L

T

K

C

V

A

L

L

-

D

-

L

-

I

-

E

-

A

-

T

-

Y

-

E

-

R

T

E

A

V

H

Y

P

P

G

G

F

E

V

V

R

L

D

V

I

V

D

D

P

K

L

D

A

G

V

V

E

K

G

C

Y

Q

F

C

S

L

F

M

G

P

Y

H

V

-

P

P

D

E

P

P

R

K

-

Q

C
|
C

I

I

Y
x
F

Q

E

N

H

A

I

H
x
Y

active site: N102 (= N75), G103 (= G76), Y243 (≠ H201)
binding iron/sulfur cluster: C237 (= C195), F239 (≠ Y197)

Sites not aligning to the query:

active site: 1, 27, 301, 306, 316, 424
binding iron/sulfur cluster: 383, 385, 434, 436, 437

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, 26% coverage: 35:201/636 of query aligns to 143:329/561 of Q9STG9

query
sites
Q9STG9

E

E

N

S

E

K

V

L

H

D

L

Q

E

L

P

P

G

G

-

D

L

I

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

S

V

T

I

A

-

G

-

S

D

S

L

M

A

L

T

K

G

N

T

V

Q

Q

P

P

L

F

F

V

N

A

-

G

-

Y

E

R

D

F

G

G

T

S

V

V

G

G

I

V

V

A

F
x
H

N

N

G

G

E

N

I

L

Y

V

N

N

Y

Y

L

T

E

K

L

L

M

R

Q

A

E

D

L

L

N

E

D

E

L

N

G

G

Y

S

R

I

F

F

R

N

T

T

R

S

S

S

D

D

T

T

E

E

V

V

I

V

V

L

H

H

A

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

-

P

-

F

W

F

Q

M

A

R

W

I

G

V

E

D

A

A

C

C

V

-

H

E

R

K

L

L

R

Q

G

G

M

-

F

-

A

A

F

Y

A

S

L

M

W

V

D

F

R

V

K

T

H

E

Q

D

T

K

L

L

F

V

L

A

A

V

R

R

D

D

R

P

M

H

G

G

V

F

K
x
R

P
|
P

M

L

H

V

Y

M

A

G

W

R

L

R

P

S

D

N

G

G

S

A

F

V

I

V

F

F

G

A

S

S

E

E

L

T

K

C

V

A

L

L

-

D

-

L

-

I

-

E

-

A

-

T

-

Y

-

E

-

R

T

E

A

V

H

Y

P

P

G

G

F

E

V

V

R

L

D

V

I

V

D

D

P

K

L

D

A

G

V

V

E

K

G

C

Y

Q

F

C

S

L

F

M

G

P

Y

H

V

-

P

P

D

E

P

P

R

K

-

Q

C

C

I

I

Y

F

Q

E

N

H

A

I

H

Y

H187 (≠ F74) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K145) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P146) 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.

1ao0A Glutamine phosphoribosylpyrophosphate (prpp) amidotransferase from b. Subtilis complexed with adp and gmp (see paper)
26% identity, 21% coverage: 45:178/636 of query aligns to 67:207/455 of 1ao0A

query
sites
1ao0A

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

-

V

-

I

-

D

-

L

-

A

A

T

T

G

G

-

Y

-

E

-

N

T

V

Q

Q

P

P

L

L

F

L

-

F

-

R

-

S

N

Q

E

N

D

N

G

G

T

S

V

L

G

A

I

L

V

A

F

H

N
|
N

G
|
G

E

N

I

L

Y

V

N

N

Y

A

L

T

E

Q

L

L

M

K

Q

Q

E

Q

L

L

N

E

D

N

L

Q

G

G

Y

S

R

I

F

F

R

Q

T

T

R

S

S

S

D

D

T

T

E

E

V

V

I

L

V

A

H

H

A

L

W

I

Q

K

A

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

-

I

E

K

A

N

C

S

V

L

H

S

R

M

L

L

R

K

G

G

M

A

F

Y

A

A

F

F

A

L

L

I

W

M

D

T

R

E

K

T

H

E

Q

-

T

-

L

M

F

I

L

V

A

A

R

L

D

D

R

P

M

N

G

G

V

L

K

R

P

P

M

L

H

S

Y

I

A

G

W

M

L

M

P

G

D

D

G

A

S

Y

F

V

I

V

F

A

G

S

S

E

E

T

L

C

K

A

V

F

L

D

T

V

A

V

H

G

P

A

G

T

F

Y

V

L

R

R

D

E

I

V

D

E

P

P

active site: N98 (= N75), G99 (= G76)

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

P00497 Amidophosphoribosyltransferase; ATase; Glutamine phosphoribosylpyrophosphate amidotransferase; GPATase; EC 2.4.2.14 from Bacillus subtilis (strain 168) (see 5 papers)
24% identity, 21% coverage: 45:178/636 of query aligns to 78:222/476 of P00497

query
sites
P00497

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

A

V

T

I

A

D

G

L

G

A

G

-

G

-

Y

T

E

G

N

T

V

Q

Q

P

P

L

L

F

L

-

F

-

R

-

S

N

Q

E

N

D

N

G

G

T

S

V

L

G

A

I

L

V

A

F

H

N

N

G

G

E

N

I

L

Y

V

N

N

Y

A

L

T

E

Q

L

L

M

K

Q

Q

E

Q

L

L

N

E

D

N

L

Q

G

G

Y

S

R

I

F

F

R

Q

T

T

R

S

S

S

D

D

T

T

E

E

V

V

I

L

V

A

H

H

A

L

W

I

Q

K

A

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

-

I

E

K

A

N

C

S

V

L

H

S

R

M

L

L

R

K

G

G

M

A

F

Y

A

A

F

F

A

L

L

I

W

M

D

T

R

E

K

T

H

E

Q

-

T

-

L

M

F

I

L

V

A

A

R

L

D

D

R

P

M

N

G

G

V

L

K

R

P

P

M

L

H

S

Y

I

A

G

W

M

L

M

P

G

D

D

G

A

S

Y

F

V

I

V

F

A

G

S

S

E

E

T

L

C

K

A

V

F

L

D

T

V

A

V

H

G

P

A

G

T

F

Y

V

L

R

R

D

E

I

V

D

E

P

P

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)
24% identity, 21% coverage: 45:178/636 of query aligns to 67:211/465 of 1gph1

query
sites
1gph1

A

A

L

I

G

G

H

H

R

V

R

R

L

Y

S

A

V

T

I

A

D

G

L

G

A

G

-

G

-

Y

T

E

G

N

T

V

Q

Q

P

P

L

L

F

L

-

F

-

R

-

S

N

Q

E

N

D

N

G

G

T

S

V

L

G

A

I

L

V

A

F

H

N

N

G

G

E

N

I

L

Y

V

N

N

Y

A

L

T

E

Q

L

L

M

K

Q

Q

E

Q

L

L

N

E

D

N

L

Q

G

G

Y

S

R

I

F

F

R

Q

T

T

R

S

S

S

D

D

T

T

E

E

V

V

I

L

V

A

H

H

A

L

W

I

Q

K

A

R

W

S

G

G

-

H

-

F

-

T

-

L

-

K

-

D

-

Q

-

I

E

K

A

N

C

S

V

L

H

S

R

M

L

L

R

K

G

G

M

A

F

Y

A

A

F

F

A

L

L

I

W

M

D

T

R

E

K

T

H

E

Q

-

T

-

L

M

F

I

L

V

A

A

R

L

D

D

R

P

M

N

G

G

V

L

K

R

P

P

M

L

H

S

Y

I

A

G

W

M

L

M

P

G

D

D

G

A

S

Y

F

V

I

V

F

A

G

S

S

E

E

T

L

C

K

A

V

F

L

D

T

V

A

V

H

G

P

A

G

T

F

Y

V

L

R

R

D

E

I

V

D

E

P

P

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

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
27% identity, 48% coverage: 73:377/636 of query aligns to 67:348/496 of 1mbzA

query
sites
1mbzA

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

Y

R

L

D

E

E

L

L

M

-

Q

-

E

-

L

L

N

S

D

V

L

L

G

P

Y

A

R

G

F

P

R

A

T

P

R

E

S

G

D

D

T

A

E

E

V

L

I

V

V

L

H

R

A

L

W

L

Q

E

A

R

W

Y

G

D

E

L

A

H

C

A

V

F

H

R

R

L

L

V

R

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

-

D

-

R

R

K

T

H

G

Q

D

T

R

L

V

F

L

L

L

A

A

R

T

D

D

R

H

M

A

G

G

V

S

K

V

P

P

M

L

H

Y

Y

T

A

C

W

V

L

A

P

P

D

-

G

G

S

E

F

V

I

R

F

A

G

S

S

T

E

E

L

A

K

K

V

A

L

L

T

A

A

A

H

H

P

-

G

G

F

F

V

-

R

-

D

-

I

-

D

-

P

P

L

L

A

A

V

-

E

-

G

-

Y

-

F

-

S

-

F

-

G

-

Y

-

V

-

P

-

D

D

P

A

R

R

C

R

I

V

-

A

-

G

Y

L

Q

T

N

G

A

V

H

Y

K

Q

L

V

P

P

A

A

A

G

H

A

T

V

L

M

T

D

L

I

R

D

R

L

G

G

D

-

A

S

G

G

R

T

P

A

A

V

P

T

R

H

P

R

Y

T

W

W

D

T

V

P

R

G

F

L

T

S

N

R

D

-

N

R

P

I

I

L

K

P

L

E

Q

G

D

E

A

A

Q

V

A

A

E

A

L

V

R

R

E

A

R

A

V

L

R

E

E

K

S

A

V

V

R

A

L

Q

R

R

M

V

I

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

T

-

M

C

A

A

G

H

L

R

S

A

T

G

P

E

V

L

H

D

T

T

C

V

S
|
S

I
x
M

G

G

F

T

D

D

D

T

P

S

R

-

F

-

D

N

E

E

S

F

S

R

F

E

A

A

Q

R

Q

A

V

V

A

V

D

D

H

H

Y

L

R

R

T

T

D

R

H

H

R

R

L

E

D

I

I

T

V

I

S

P

S

T

D

T

D

E

F

L

D

-

L

-

I

-

D

-

T

-

L

L

A

A

W

Q

L

L

Y

P

D

Y

E

A

P

V

F

W

A

A

D

S

S

E

S

S

A

V

I

D

P

P

T
x
D

-

I

-

E

-
x
Y

-

L

-

P

-
x
L

-

T

-

A

-

L

Y

Y

R

R

V

A

C

L

Q

D

M

G

A

P

R

E

K

R

H

R

V

I

T

-

V

-

A

-

L

L

S

T

G
|
G

D
x
Y

G
|
G

G

A

D
|
D

E
x
I

S

P

M

L

G

G

Y

M

R

H

R

R

active site: A69 (≠ N75), G70 (= G76), D311 (≠ T348), Y337 (≠ D366)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ F265), L237 (= L266), S238 (= S267), S243 (= S272), S261 (= S291), M262 (≠ I292), Y315 (vs. gap), L319 (vs. gap), G336 (= G365), Y337 (≠ D366), G338 (= G367), D340 (= D369), I341 (≠ E370)
binding magnesium ion: D242 (= D271), D340 (= D369)
binding pyrophosphate 2-: S238 (= S267), G240 (= G269), D242 (= D271), S243 (= S272), D340 (= D369)

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

1jgtB Crystal structure of beta-lactam synthetase (see paper)
27% identity, 48% coverage: 73:377/636 of query aligns to 71:356/500 of 1jgtB

query
sites
1jgtB

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

Y

R

L

D

E

E

L

L

M

-

Q

-

E

-

L

L

N

S

D

V

L

L

G

P

Y

A

R

G

F

P

R

A

T

P

R

E

S

G

D

D

T

A

E

E

V

L

I

V

V

L

H

R

A

L

W

L

Q

E

A

R

W

Y

G

D

E

L

A

H

C

A

V

F

H

R

R

L

L

V

R

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

-

D

-

R

R

K

T

H

G

Q

D

T

R

L

V

F

L

L

L

A

A

R

T

D

D

R

H

M

A

G

G

V

S

K

V

P

P

M

L

H

Y

Y

T

A

C

W

V

L

A

P

P

D

-

G

G

S

E

F

V

I

R

F

A

G

S

S

T

E

E

L

A

K

K

V

A

L

L

T

A

A

A

H

H

-

R

-

D

-

P

P

K

G

G

F

F

V

-

R

-

D

-

I

-

D

-

P

P

L

L

A

A

V

-

E

-

G

-

Y

-

F

-

S

-

F

-

G

-

Y

-

V

-

P

-

D

D

P

A

R

R

C

R

I

V

-

A

-

G

Y

L

Q

T

N

G

A

V

H

Y

K

Q

L

V

P

P

A

A

A

G

H

A

T

V

L

M

T

D

L

I

R

D

R

L

G

G

D

-

A

S

G

G

R

T

P

A

A

V

P

T

R

H

P

R

Y

T

W

W

D

T

V

P

R

G

F

L

T

S

N

R

D

-

N

R

P

I

I

L

K

P

L

E

Q

G

D

E

A

A

Q

V

A

A

E

A

L

V

R

R

E

A

R

A

V

L

R

E

E

K

S

A

V

V

R

A

L

Q

R

R

M

V

I

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L
|
L

S
|
S

G

G

G
|
G

V
x
I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

T

-

M

C

A

A

G

H

L

R

S

A

T

G

P

E

V

L

H

D

T

T

C

V

S
|
S

I
x
M

G

G

F

T

D

D

D

T

P

-

R

-

F

S

D

N

E

E

S

F

S

R

F

E

A

A

Q

R

Q

A

V

V

A

V

D

D

H

H

Y

L

R

R

T

T

D

R

H

H

R

R

L

E

D

I

I

T

V

I

S

P

S

T

D

T

D

E

F

L

D

-

L

-

I

-

D

-

T

-

L

L

A

A

W

Q

L

L

Y

P

D

Y

E

A

P

V

F

W

A

A

D

S

S

E

S

S

A

V

I

D

P

P

T
x
D

-

I

-

E

-
x
Y

-

L

-

P

-
x
L

-

T

-

A

-

L

Y

Y

R

R

V

A

C

L

Q

D

M

G

A

P

R

E

K

R

H

R

V

I

T

-

V

-

A

-

L

L

S

T

G
|
G

D
x
Y

G
|
G

G

A

D
|
D

E
x
I

S

P

M

L

G

G

Y
x
M

R

H

R

R

active site: A73 (≠ N75), G74 (= G76), D319 (≠ T348), Y345 (≠ D366)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ F265), L245 (= L266), S246 (= S267), G248 (= G269), I249 (≠ V270), D250 (= D271), S251 (= S272), S269 (= S291), M270 (≠ I292), L327 (vs. gap), G344 (= G365), Y345 (≠ D366), D348 (= D369)
binding n2-(carboxyethyl)-l-arginine: Y323 (vs. gap), Y345 (≠ D366), G346 (= G367), D348 (= D369), I349 (≠ E370), M354 (≠ Y375)
binding magnesium ion: D250 (= D271), D348 (= D369)

Sites not aligning to the query:

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

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
27% identity, 48% coverage: 73:377/636 of query aligns to 63:343/491 of 1mc1A

query
sites
1mc1A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

Y

R

L

D

E

E

L

L

M

-

Q

-

E

-

L

L

N

S

D

V

L

L

G

P

Y

A

R

G

F

P

R

A

T

P

R

E

S

G

D

D

T

A

E

E

V

L

I

V

V

L

H

R

A

L

W

L

Q

E

A

R

W

Y

G

D

E

L

A

H

C

A

V

F

H

R

R

L

L

V

R

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

-

D

-

R

R

K

T

H

G

Q

D

T

R

L

V

F

L

L

L

A

A

R

T

D

D

R

H

M

A

G

G

V

S

K

V

P

P

M

L

H

Y

Y

T

A

C

W

V

L

A

P

P

D

-

G

G

S

E

F

V

I

R

F

A

G

S

S

T

E

E

L

A

K

K

V

A

L

L

T

A

A

A

H

-

P

-

G

G

F

F

V

-

R

-

D

-

I

-

D

-

P

P

L

L

A

A

V

-

E

-

G

-

Y

-

F

-

S

-

F

-

G

-

Y

-

V

-

P

-

D

D

P

A

R

R

C

R

I

V

-

A

-

G

Y

L

Q

T

N

G

A

V

H

Y

K

Q

L

V

P

P

A

A

A

G

H

A

T

V

L

M

T

D

L

I

R

D

R

L

G

G

D

-

A

S

G

G

R

T

P

A

A

V

P

T

R

H

P

R

Y

T

W

W

D

T

V

P

R

G

F

L

T

S

N

R

D

-

N

R

P

I

I

L

K

P

L

E

Q

G

D

E

A

A

Q

V

A

A

E

A

L

V

R

R

E

A

R

A

V

L

R

E

E

K

S

A

V

V

R

A

L

Q

R

R

M

V

I

T

-

P

A

G

D

D

V

T

P

P

L

L

G

-

A

V

F
x
V

L

L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

S

S

A

G

V

V

V

A

A

A

T

-

M

C

A

A

G

H

L

R

S

A

T

G

P

E

V

L

H

D

T

T

C

V

S
|
S

I
x
M

G

G

F

T

D

D

D

T

P

S

R

-

F

-

D

N

E

E

S

F

S

R

F

E

A

A

Q

R

Q

A

V

V

A

V

D

D

H

H

Y

L

R

R

T

T

D

R

H

H

R

R

L

E

D

I

I

T

V

I

S

P

S

T

D

T

D

E

F

L

D

-

L

-

I

-

D

-

T

-

L

L

A

A

W

Q

L

L

Y

P

D

Y

E

A

P

V

F

W

A

A

D

S

S

E

S

S

A

V

I

D

P

P

T
x
D

-

I

-

E

-
x
Y

-

L

-

P

-

L

-

T

-

A

-

L

Y

Y

R

R

V

A

C

L

Q

D

M

G

A

P

R

E

K

R

H

R

V

I

T

-

V

-

A

-

L

L

S

T

G
|
G

D
x
Y

G
|
G

G

A

D
|
D

E
x
I

S

P

M

L

G

G

Y

M

R

H

R

R

active site: A65 (≠ N75), G66 (= G76), D306 (≠ T348), Y332 (≠ D366)
binding adenosine monophosphate: V231 (≠ F265), S233 (= S267), S238 (= S272), S256 (= S291), M257 (≠ I292), G331 (= G365)
binding magnesium ion: D237 (= D271), D335 (= D369)
binding deoxyguanidinoproclavaminic acid: Y310 (vs. gap), Y332 (≠ D366), G333 (= G367), I336 (≠ E370)
binding pyrophosphate 2-: S233 (= S267), G235 (= G269), D237 (= D271), S238 (= S272), D335 (= D369)

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

1mb9A Beta-lactam synthetase complexed with atp (see paper)
25% identity, 48% coverage: 73:377/636 of query aligns to 68:347/485 of 1mb9A

query
sites
1mb9A

V

V

F

L

N
x
A

G
|
G

E

E

I

I

Y

Y

N

N

Y

R

L

D

E

E

L

L

M

-

Q

-

E

-

L

L

N

S

D

V

L

L

G

P

Y

A

R

G

F

P

R

A

T

P

R

E

S

G

D

D

T

A

E

E

V

L

I

V

V

L

H

R

A

L

W

L

Q

E

A

R

W

Y

G

D

E

L

A

H

C

A

V

F

H

R

R

L

L

V

R

N

G

G

M

R

F

F

A

A

F

T

A

V

L

V

W

-

D

-

R

R

K

T

H

G

Q

D

T

R

L

V

F

L

L

L

A

A

R

T

D

D

R

H

M

A

G

G

V

S

K

V

P

P

M

L

H

Y

Y

T

A

C

W

V

L

A

P

P

D

-

G

G

S

E

F

V

I

R

F

A

G

S

S

T

E

E

L

A

K

K

V

A

L

L

T

A

A

A

H

F

P

P

G

-

F

-

V

-

R

-

D

-

I

-

D

-

P

-

L

-

A

-

V

-

E

-

G

-

Y

-

F

-

S

-

F

-

G

-

Y

-

V

L

P

A

D

D

P

A

R

R

C

R

I

V

-

A

-

G

Y

L

Q

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N

G

A

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K

Q

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A

A

A

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A

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M

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L

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D

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-

A

S

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G

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A

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T

W

W

D

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F

L

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N

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-

N

R

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E

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A

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D

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x
V

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L

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S

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S

S

S

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G

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V

V

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M

C

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x
M

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G

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D

D

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R

-

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N

E

E

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A

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V

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D

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T

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F

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D

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L

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L

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Q

L

L

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D

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Y

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x
L

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active site: A70 (≠ N75), G71 (= G76), D310 (≠ T348), Y336 (≠ D366)
binding adenosine monophosphate: V235 (≠ F265), L236 (= L266), S242 (= S272), S260 (= S291), M261 (≠ I292), Y314 (vs. gap), L318 (vs. gap), G335 (= G365), Y336 (≠ D366)
binding adenosine-5'-triphosphate: V235 (≠ F265), L236 (= L266), S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), S260 (= S291), M261 (≠ I292), L318 (vs. gap), G335 (= G365), D339 (= D369)
binding magnesium ion: D241 (= D271), D339 (= D369)
binding pyrophosphate 2-: S237 (= S267), G239 (= G269), D241 (= D271), S242 (= S272), D339 (= D369)

Sites not aligning to the query:

active site: 370, 431
binding adenosine-5'-triphosphate: 411, 431
binding pyrophosphate 2-: 411, 431

1q19A Carbapenam synthetase (see paper)
35% identity, 18% coverage: 262:374/636 of query aligns to 240:352/500 of 1q19A

query
sites
1q19A

L

V

G

G

A

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x
P

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L

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S

G

G

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L

D
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D

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S

S

S

A

L

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V

V

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A

A

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M

L

A

A

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I

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F

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N

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D

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L

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x
L

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x
E

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L

Y

F

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A

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L

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G

active site: L318 (≠ S343), E321 (vs. gap), Y344 (≠ D366)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ F265), L244 (= L266), S245 (= S267), D249 (= D271), S250 (= S272), S268 (= S291), I269 (= I292), T342 (≠ S364), G343 (= G365), D347 (= D369)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D366), G345 (= G367), L348 (≠ E370)

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

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)
35% identity, 18% coverage: 262:374/636 of query aligns to 241:353/503 of Q9XB61

query
sites
Q9XB61

L

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M

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F

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D

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D

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F

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I

-

N

D

G

L

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I

I

D

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I

A

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W

-

L

Y

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Y

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E

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F

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D

D

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A

-

E

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G

244:251 (vs. 265:272, 75% identical) binding ATP
I270 (= I292) binding ATP
GYGSD 344:348 (≠ GDGGD 365:369) binding ATP
Y345 (≠ D366) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G367) 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

Query Sequence

>WP_013721407.1 NCBI__GCF_000204645.1:WP_013721407.1
MCGISGIFDTRGTGTIPRDLISRINNVQSHRGPDENEVHLEPGLALGHRRLSVIDLATGT
QPLFNEDGTVGIVFNGEIYNYLELMQELNDLGYRFRTRSDTEVIVHAWQAWGEACVHRLR
GMFAFALWDRKHQTLFLARDRMGVKPMHYAWLPDGSFIFGSELKVLTAHPGFVRDIDPLA
VEGYFSFGYVPDPRCIYQNAHKLPAAHTLTLRRGDAGRPAPRPYWDVRFTNDNPIKLQDA
QAELRERVRESVRLRMIADVPLGAFLSGGVDSSAVVATMAGLSSTPVHTCSIGFDDPRFD
ESSFAQQVADHYRTDHRLDIVSSDDFDLIDTLAWLYDEPFADSSAIPTYRVCQMARKHVT
VALSGDGGDESMGGYRRYRMHLGEEAVRGRLPLALRRGMFGPLGRWYPKADWAPRSLRAK
TTFQALAMDSVQAYCHSMSQLRGDERRALFSPAFQRSLGGYGALEVFRLHAEQAQTEDPL
ALIQYLDYKTWLVGDINTKVDRASMAHSLEVREPLMDHLLVEWLATLPSDFKIRAGQGKV
IFKQAYEPLLPRDVLYRPKMGFSVPLAAWLRGPLKDRVRLALLGERMRDCGYFNPVTLRR
LVDEHNSGLRDHATALWMLLMFEAFLRLNEGAAPHG

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