SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing AO356_26510 FitnessBrowser__pseudo5_N2C3_1:AO356_26510 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 13 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)
28% identity, 66% coverage: 1:418/631 of query aligns to 1:415/557 of P78753

query
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P78753

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S391 (≠ T394) modified: Phosphoserine

Sites not aligning to the query:

489 modified: Phosphoserine

1ct9A Crystal structure of asparagine synthetase b from escherichia coli (see paper)
28% identity, 56% coverage: 26:376/631 of query aligns to 27:343/497 of 1ct9A

query
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1ct9A

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active site: L50 (= L51), N74 (= N73), G75 (= G74), T305 (≠ N340), R308 (≠ G343), E332 (≠ D365)
binding adenosine monophosphate: L232 (≠ Y263), L233 (= L264), S234 (= S265), S239 (= S270), A255 (≠ T289), V256 (= V290), D263 (= D298), M316 (≠ L349), S330 (≠ A363), G331 (= G364), E332 (≠ D365)
binding glutamine: R49 (= R50), L50 (= L51), I52 (≠ M53), V53 (= V54), N74 (= N73), G75 (= G74), E76 (= E75), D98 (= D98)

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)
27% identity, 56% coverage: 26:376/631 of query aligns to 28:360/554 of P22106

query
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P22106

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H30 (= H28) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D32) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ Y79) mutation to A: 5-fold decrease in glutamine affinity.
A105 (≠ H104) mutation to H: Little effect on the kinetic properties.
E349 (≠ D365) 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.

Sites not aligning to the query:

1 modified: Initiator methionine, Removed
2 mutation C->A,S: Loss of glutamine-dependent activity but no effect on ammonia-dependent asparagine synthetase activity.

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, 55% coverage: 28:376/631 of query aligns to 26:376/561 of P08243

query
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P08243

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F

Q

G

T

M

Q

Q

P

P

F

I

H

R

T

V

D

K

-

Y

-

P

-

Y

V

L

H

W

V

L

V

C

V

Y

N

N

G

G

E

E

I

I

Y

Y

Q

N

Y

H

A

K

Q

M

R

Q

Q

Q

K

H

L

F

E

E

A

F

A

E

G

-

A

-

C

-

F

Y

A

Q

T

T

D

K

S

V

D

D

C

G

E

E

V

I

A

L

H

H

G

L

Y

Y

L

D

Q

K

L

G

G

G

I

I

D

E

-

Q

Y

T

V

I

R

C

E

M

L

L

N

D

G

G

E

V

F

F

A

A

G

F

V

V

I

L

W

L

D

D

A

T

R

A

R

N

R

K

K

K

L

V

F

F

A

L

I

G

R

R

D

D

R

T

W

Y

G

G

V

V

K

R

P

P

L

L

F

F

Y

K

R

A

L

M

S

T

D

E

Q

D

G

G

-

F

I

L

H

A

L

V

A

C

S

S

E

E

I

A

K

K

A

G

L

L

I

V

A

T

L

L

G

-

A

-

Q

-

P

-

R

-

W

-

D

K

H

H

A

S

A

A

L

-

F

-

Q

-

H

-

F

-

A

-

S

-

I

-

G

-

P

-

A

-

Q

-

T

T

L

P

F

F

E

L

G

K

I

V

H

E

Q

P

V

F

P

L

P

P

G

G

H

H

-

Y

-

E

V

V

L

L

E

D

W

L

S

K

T

P

Q

N

G

G

Y

K

G

V

V

A

T

S

P

V

L

E

L

M

S

V

A

K

V

Y

D

H

E

H

A

C

H

R

D

D

A
x
V

A

P

R

L

Q

H

H

A

L

L

A

Y

S

D

A

N

P

V

R

E

E

K

W

L

M

F

P

P

-

G

-

F

-

E

-

I

-

E

R

T

L

V

V

K

D

N

G

N

L

L

R

R

-

I

-

L

-

F

-

N

H

N

A

A

V

V

Q

K

D

K

R

R

F

L

Q

M

G

T

D

D

G

R

P

R

V

I

A

G

C

C

Y

L

L

L

S

S

G

G

V

L

D

D

S

S

A

S

T

L

V

V

A

A

L

T

A

L

R

K

H

Q

G

L

R

K

E

E

G

A

L

Q

S

V

A

Q

F

Y

T

P

V

L

D

Q

-

T

F

F

G

A

A

I

G

G

T

M

D

E

D

D

A

S

T

P

Q

D

-

L

-

A

A

A

A

R

G

K

I

V

A

A

A

D

S

H

L

I

G

G

L

S

R

E

H

H

E

Y

V

E

V

V

P

L

V

F

S

N

E

S

A

E

Q

E

L

G

V

I

D

Q

H

A

F

L

A

D

D

E

A

V

V

I

R

F

H

S

A

L

E

E

T

T

I

Y

G

D

F

I

N

T

T

T

I

V

G

R

A

A

A

S

-

V

-

G

R

M

W

Y

I

L

L

I

G

S

R

K

V

Y

L

I

-

R

A

K

S

N

S

T

G

D

Y

S

K

V

A

V

V

I

L
x
F

A

S

G

G

D

E

G

G

A

S

D

D

E

E

L

L

F

T

A

Q

G

G

Y

Y

S

I

F

Y

V210 (≠ A226) 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

6gq3A Human asparagine synthetase (asns) in complex with 6-diazo-5-oxo-l- norleucine (don) at 1.85 a resolution (see paper)
27% identity, 55% coverage: 28:376/631 of query aligns to 25:363/509 of 6gq3A

query
sites
6gq3A

H

H

R

R

G

G

P

P

D

D

G

A

-

F

R

R

A

F

S

E

W

N

L

V

S

N

A

G

D

Y

G

T

L

N

C

C

G

C

I

F

G

G

F

F

H

H

R
|
R

L
|
L

A

A

M
x
V

V
|
V

G

D

A

P

R

L

E

F

Q

G

T

M

Q

Q

P

P

F

I

H

R

T

V

D

K

-

Y

-

P

-

Y

V

L

H

W

V

L

V

C

V
x
Y

N
|
N

G
|
G

E
|
E

I

I

Y

Y

Q

N

Y

H

A

K

Q

M

R

Q

Q

Q

K

H

L

F

E

E

A

F

A

E

G

-

A

-

C

-

F

Y

A

Q

T

T

D

K

S
x
V

D
|
D

C

G

E

E

V

I

A

L

H

H

G

L

Y

Y

L

D

Q

K

L

G

G

G

I

I

D

E

-

Q

Y

T

V

I

R

C

E

M

L

L

N

D

G

G

E

V

F

F

A

A

G

F

V

V

I

L

W

L

D

D

A

T

R

A

R

N

R

K

K

K

L

V

F

F

A

L

I

G

R

R

D

D

R

T

W

Y

G

G

V

V

K

R

P

P

L

L

F

F

Y

K

R

A

L

M

S

T

D

E

Q

D

G

G

-

F

I

L

H

A

L

V

A

C

S

S

E

E

I

A

K

K

A

G

L

L

I

V

A

T

L

L

G

-

A

-

Q

-

P

-

R

-

W

-

D

K

H

H

A

S

A

A

L

-

F

-

Q

-

H

-

F

-

A

-

S

-

I

-

G

-

P

-

A

-

Q

-

T

T

L

P

F

F

E

L

G

K

I

V

H

E

Q

P

V

F

P

L

P

P

G

G

H

H

-

Y

-

E

V

V

L

L

E

D

W

L

S

K

T

P

Q

N

G

G

Y

K

G

V

V

A

T

S

P

V

L

E

L

M

S

V

A

K

V

Y

D

H

E

H

A

C

H

R

D

D

A

V

A

F

R

P

Q

G

H

F

L

E

A

I

S

E

A

T

P

V

R

K

E

N

W

N

M

L

P

R

R

I

L

L

V

F

D

N

G

-

L

-

R

-

H

N

A

A

V

V

Q

K

D

K

R

R

F

L

Q

M

G

T

D

D

G

R

P

R

V

I

A

G

C

C

Y

L

L

L

S

S

G

G

V

L

D

D

S

S

A

S

T

L

V

V

A

A

L

T

A

L

R

K

H

Q

G

L

R

K

E

E

G

A

L

Q

S

V

A

Q

F

Y

T

P

V

L

D

Q

-

T

F

F

G

A

A

I

G

G

T

M

D

E

D

D

A

S

T

P

Q

D

-

L

-

A

A

A

A

R

G

K

I

V

A

A

A

D

S

H

L

I

G

G

L

S

R

E

H

H

E

Y

V

E

V

V

P

L

V

F

S

N

E

S

A

E

Q

E

L

G

V

I

D

Q

H

A

F

L

A

D

D

E

A

V

V

I

R

F

H

S

A

L

E

E

T

T

I

Y

G

D

F

I

N
x
T

T

T

I

V

G
x
R

A

A

A

S

-

V

-

G

R

M

W

Y

I

L

L

I

G

S

R

K

V

Y

L

I

-

R

A

K

S

N

S

T

G

D

Y

S

K

V

A

V

V

I

L

F

A

S

G

G

D

E

G

G

A

S

D

D

E

E

L

L

F

T

A

Q

G

G

Y

Y

S

I

F

Y

active site: L49 (= L51), N74 (= N73), G75 (= G74), T324 (≠ N340), R327 (≠ G343)
binding 5-oxo-l-norleucine: R48 (= R50), V51 (≠ M53), V52 (= V54), Y73 (≠ V72), N74 (= N73), G75 (= G74), E76 (= E75), V95 (≠ S97), D96 (= D98)

Sites not aligning to the query:

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

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)
24% identity, 44% coverage: 97:373/631 of query aligns to 80:353/503 of Q9XB61

query
sites
Q9XB61

S

N

D

D

C

A

E

E

V

L

A

A

H

L

G

L

Y

F

L

T

Q

R

L

L

G

G

I

A

D

N

Y

A

V

L

R

A

E

L

L

A

N

E

G

G

E

D

F

F

A

C

G

F

V

F

I

I

W

-

D

D

A

E

R

P

R

N

R

G

K

E

L

L

F

T

A

V

I

I

R

T

D

E

R

S

W

R

G

G

V

F

K

S

P

P

L

V

F

-

Y

H

R

V

L

V

S

Q

D

G

Q

K

G

K

I

A

H

W

L

M

A

T

S

N

E

S

I

L

K

K

A

L

L

V

I

T

A

A

L

A

-

E

G

G

A

E

Q

G

P

A

R

L

W

W

-

F

-

E

D

E

H

E

A

A

A

L

L

V

F

C

Q

Q

H

S

F

L

F

M

A

R

S

A

I

-

G

-

P

D

A

T

Q

Y

T

T

L

P

F

V

E

K

G

N

I

A

H

Q

Q

R

V

L

P

K

P

P

G

G

-

A

-

V

H

H

V

V

L

L

E

T

W

H

S

D

T

S

Q

E

G

G

Y

Y

G

S

V

F

T

V

P

E

L

S

L

R

S

T

A

L

V

T

D

T

E

P

A

A

H

S

D

N

A

-

R

-

Q

-

H

Q

L

L

A

L

S

A

A

L

P

P

R

R

E

E

W

P

M

L

P

L

R

A

L

L

V

I

D

D

G

R

L

Y

R

L

H

N

A

A

-

P

V

L

Q

E

D

D

R

L

F

A

Q

P

G

R

D

F

G

D

P

T

V

V

A

G

C

I

Y
x
P

L
|
L

S
|
S

G
|
G

V
x
L

D
|
D

S
|
S

A

S

T

L

V

V

A

T

A

A

L

L

A

A

A

S

R

R

H

H

G

F

R

K

E

K

G

-

L

L

S

N

A

T

F

Y

T

S

V
x
I

D

-

F

-

G

-

A

-

G

G

T

T

D

E

D

L

A

S

T

N

Q

E

-

F

-

E

-

F

A

S

A

Q

G

Q

I

V

A

A

A

D

S

A

L

L

G

G

L

T

R

H

H

H

E

Q

V

M

V

K

P

I

V

L

S

S

E

E

A

T

Q

E

L

V

V

I

D

N

H

G

F

I

A

I

D

E

A

S

V

I

R

Y

H

Y

A

N

E

E

T

I

-

F

-

D

-

G

-

L

-

S

-

A

-

E

I

I

G

Q

F

S

N

G

T

L

I

F

G

N

A

V

A

Y

R

R

W

Q

I

A

L

Q

G

G

R

Q

V

V

L

-

A

-

S

-

G

-

Y

-

K

S

A

C

V

M

L

L

A

T

G
|
G

D
x
Y

G
|
G

A
x
S

D
|
D

E

L

L

L

F

F

A

G

G

G

244:251 (vs. 263:270, 75% identical) binding
I270 (≠ V290) binding
GYGSD 344:348 (≠ GDGAD 364:368) binding
Y345 (≠ D365) mutation to A: Loss of activity.; mutation to F: Reduces catalytic efficiency.
G346 (= G366) binding

Sites not aligning to the query:

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

1q19A Carbapenam synthetase (see paper)
24% identity, 44% coverage: 97:373/631 of query aligns to 79:352/500 of 1q19A

query
sites
1q19A

S

N

D

D

C

A

E

E

V

L

A

A

H

L

G

L

Y

F

L

T

Q

R

L

L

G

G

I

A

D

N

Y

A

V

L

R

A

E

L

L

A

N

E

G

G

E

D

F

F

A

C

G

F

V

F

I

I

W

-

D

D

A

E

R

P

R

N

R

G

K

E

L

L

F

T

A

V

I

I

R

T

D

E

R

S

W

R

G

G

V

F

K

S

P

P

L

V

F

-

Y

H

R

V

L

V

S

Q

D

G

Q

K

G

K

I

A

H

W

L

M

A

T

S

N

E

S

I

L

K

K

A

L

L

V

I

T

A

A

L

A

-

E

G

G

A

E

Q

G

P

A

R

L

W

W

-

F

-

E

D

E

H

E

A

A

A

L

L

V

F

C

Q

Q

H

S

F

L

F

M

A

R

S

A

I

-

G

-

P

D

A

T

Q

Y

T

T

L

P

F

V

E

K

G

N

I

A

H

Q

Q

R

V

L

P

K

P

P

G

G

-

A

-

V

H

H

V

V

L

L

E

T

W

H

S

D

T

S

Q

E

G

G

Y

Y

G

S

V

F

T

V

P

E

L

S

L

R

S

T

A

L

V

T

D

T

E

P

A

A

H

S

D

N

A

-

R

-

Q

-

H

Q

L

L

A

L

S

A

A

L

P

P

R

R

E

E

W

P

M

L

P

L

R

A

L

L

V

I

D

D

G

R

L

Y

R

L

H

N

A

A

-

P

V

L

Q

E

D

D

R

L

F

A

Q

P

G

R

D

F

G

D

P

T

V

V

A

G

C

I

Y
x
P

L
|
L

S
|
S

G

G

V

L

D
|
D

S
|
S

A

S

T

L

V

V

A

T

A

A

L

L

A

A

A

S

R

R

H

H

G

F

R

K

E

K

G

-

L

L

S

N

A

T

F

Y

T
x
S

V
x
I

D

-

F

-

G

-

A

-

G

G

T

T

D

E

D

L

A

S

T

N

Q

E

-

F

-

E

-

F

A

S

A

Q

G

Q

I

V

A

A

A

D

S

A

L

L

G

G

L

T

R

H

H

H

E

Q

V

M

V

K

P

I

V

L

S

S

E

E

A

T

Q

E

L

V

V

I

D

N

H

G

F

I

A

I

D

E

A

S

V

I

R

Y

H

Y

A

N

E

E

T

I

-

F

-

D

-

G

-
x
L

-

S

-

A

-
x
E

I

I

G

Q

F

S

N

G

T

L

I

F

G

N

A

V

A

Y

R

R

W

Q

I

A

L

Q

G

G

R

Q

V

V

L

-

A

-

S

-

G

-

Y

-

K

S

A

C

V

M

L

L

A
x
T

G
|
G

D
x
Y

G
|
G

A

S

D
|
D

E
x
L

L

L

F

F

A

G

G

G

active site: L318 (vs. gap), E321 (vs. gap), Y344 (≠ D365)
binding diphosphomethylphosphonic acid adenosyl ester: P243 (≠ Y263), L244 (= L264), S245 (= S265), D249 (= D269), S250 (= S270), S268 (≠ T289), I269 (≠ V290), T342 (≠ A363), G343 (= G364), D347 (= D368)
binding (2s,5s)-5-carboxymethylproline: Y344 (≠ D365), 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

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, 43% coverage: 12:281/631 of query aligns to 117:383/561 of Q9STG9

query
sites
Q9STG9

A

A

P

G

V

I

P

V

T

T

V

V

T

S

L

K

D

D

A

K

A

V

L

L

D

Q

T

T

L

I

R

T

H

G

R

V

G

G

-

L

-

V

-

S

-

E

-

V

-

F

P

S

D

E

G

S

R

K

A

L

S

D

W

Q

L

L

S

P

A

G

D

D

G

-

L

-

C

I

G

A

I

I

G

G

F

H

H

V

R

R

L

Y

A

S

M

T

V

A

G

G

A

S

R

S

-

M

-

L

E

K

Q

N

T

V

Q

Q

P

P

F

F

-

V

-

A

-

G

-

Y

H

R

T

F

D

G

D

S

V

V

H

G

V

V

V

A

V
x
H

N

N

G

G

E

N

I

L

Y

V

Q

N

Y

Y

A

T

A

K

Q

L

R

R

Q

A

K

D

L

L

E

E

A

E

A

N

G

G

A

S

C

I

F

F

A

N

T

T

D

S

S

S

D

D

C

T

E

E

V

V

A

L

H

H

-

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

G

P

Y

F

L

F

Q

M

L

R

G

I

I

V

D

D

Y

A

V

C

R

E

E

K

L

L

N

Q

G

G

E

A

F

Y

A

S

G

M

V

V

I

F

W

-

D

-

A

V

R

T

R

E

R

D

K

K

L

L

F

V

A

A

I

V

R

R

D

D

R

P

W

H

G

G

V

F

K
x
R

P
|
P

L

L

F

V

Y

M

-

G

R

R

L

R

S

S

D

N

Q

G

G

A

I

V

H

V

L

F

A

A

S

S

E

E

I

T

K

C

A

A

L

L

I

D

A

L

L

I

G

E

A

A

Q

T

P

-

R

-

W

-

D

-

H

-

A

-

L

-

F

-

Q

-

H

-

F

-

A

-

S

-

I

-

G

-

P

-

A

-

Q

-

T

-

L

-

F

Y

E

E

G

-

I

-

H

R

Q

E

V

V

P

Y

P

P

G

G

H

E

V

V

L

L

E

V

W

V

S

D

T

K

Q

D

G

G

Y

V

G

K

V

C

T

Q

P

C

L

L

L

M

S

P

A

H

V

P

D

E

E

P

A

K

H

Q

D

C

A

I

A

F

R

E

Q

H

H

I

L

Y

A

F

S

S

A

L

P

P

R

N

E

S

W

I

M

V

-

F

P

G

R

R

L

S

V

V

D

Y

G

E

L

S

R

R

H

H

A

V

V

F

Q

G

D

E

R

I

F

L

Q

A

G

T

D

E

G

S

P

P

V

V

A

D

C

C

Y

D

L

V

S

V

G

I

G

A

V

V

-

P

D

D

S

S

A
x
G

T

V

V

V

A

A

L

L

-

G

-

Y

A

A

R

K

H

A

G

G

H187 (≠ V72) mutation to T: In cia1-2; small plants with white leaves showing an irregular mosaic of green sectors.
R264 (≠ K143) mutation to K: Strong resistance to the bleaching herbicides DAS073 and DAS734.
P265 (= P144) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734; when associated with F-494.
G371 (≠ A271) mutation to S: Low resistance to the bleaching herbicides DAS073 and DAS734.

Sites not aligning to the query:

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, 43% coverage: 12:281/631 of query aligns to 31:297/460 of 6lbpA

query
sites
6lbpA

A

A

P

G

V

I

P

V

T

T

V

V

T

S

L

K

D

D

A

K

A

V

L

L

D

Q

T

T

L

I

R

T

H

G

R

V

G

G

-

L

-

V

-

S

-

E

-

V

-

F

P

S

D

E

G

S

R

K

A

L

S

D

W

Q

L

L

S

P

A

G

D

D

G

-

L

-

C

I

G

A

I

I

G

G

F

H

H

V

R

R

L

Y

A

S

M

T

V

A

G

G

A

S

R

S

-

M

-

L

E

K

Q

N

T

V

Q

Q

P

P

F

F

-

V

-

A

-

G

-

Y

H

R

T

F

D

G

D

S

V

V

H

G

V

V

V

A

V

H

N
|
N

G
|
G

E

N

I

L

Y

V

Q

N

Y

Y

A

T

A

K

Q

L

R

R

Q

A

K

D

L

L

E

E

A

E

A

N

G

G

A

S

C

I

F

F

A

N

T

T

D

S

S

S

D

D

C

T

E

E

V

V

A

L

H

H

-

L

-

I

-

A

-

I

-

S

-

K

-

A

-

R

G

P

Y

F

L

F

Q

M

L

R

G

I

I

V

D

D

Y

A

V

C

R

E

E

K

L

L

N

Q

G

G

E

A

F

Y

A

S

G

M

V

V

I

F

W

-

D

-

A

V

R

T

R

E

R

D

K

K

L

L

F

V

A

A

I

V

R

R

D

D

R

P

W

H

G

G

V

F

K

R

P

P

L

L

F

V

Y

M

-

G

R

R

L

R

S

S

D

N

Q

G

G

A

I

V

H

V

L

F

A

A

S

S

E

E

I

T

K

C

A

A

L

L

I

D

A

L

L

I

G

E

A

A

Q

T

P

-

R

-

W

-

D

-

H

-

A

-

L

-

F

-

Q

-

H

-

F

-

A

-

S

-

I

-

G

-

P

-

A

-

Q

-

T

-

L

-

F

Y

E

E

G

-

I

-

H

R

Q

E

V

V

P

Y

P

P

G

G

H

E

V

V

L

L

E

V

W

V

S

D

T

K

Q

D

G

G

Y

V

G

K

V

C

T

Q

P

C

L

L

L

M

S

P

A

H

V

P

D

E

E

P

A

K

H

Q

D
x
C

A

I

A
x
F

R

E

Q

H

H

I

L
x
Y

A

F

S

S

A

L

P

P

R

N

E

S

W

I

M

V

-

F

P

G

R

R

L

S

V

V

D

Y

G

E

L

S

R

R

H

H

A

V

V

F

Q

G

D

E

R

I

F

L

Q

A

G

T

D

E

G

S

P

P

V

V

A

D

C

C

Y

D

L

V

S

V

G

I

G

A

V

V

-

P

D

D

S

S

A

G

T

V

V

V

A

A

L

L

-

G

-

Y

A

A

R

K

H

A

G

G

active site: N102 (= N73), G103 (= G74), Y243 (≠ L231)
binding iron/sulfur cluster: C237 (≠ D225), F239 (≠ A227)

Sites not aligning to the query:

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

1mbzA Beta-lactam synthetase with trapped intermediate (see paper)
26% identity, 48% coverage: 71:373/631 of query aligns to 67:345/496 of 1mbzA

query
sites
1mbzA

V

V

V

L

N
x
A

G
|
G

E

E

I

I

Y

Y

Q

N

Y

-

A

-

Q

R

R

D

Q

E

K

L

L

L

E

S

A

V

A

L

G

P

A

A

C

G

F

P

A

A

T

P

D

E

S

G

D

D

C

A

E

E

V

L

V

V

A

L

H

R

G

L

Y

L

L

E

Q

R

L

Y

G

D

I

L

D

H

Y

A

V

F

R

R

E

L

L

V

N

N

G

G

E

R

F

F

A

A

G

T

V

V

I

V

W

R

D

T

A

G

R

D

R

R

R

-

K

-

L

V

F

L

A

L

I

A

R

T

D

D

R

H

W

A

G

G

V

S

K

V

P

P

L

L

F

Y

Y

T

R

C

L

V

S

A

D

P

Q

G

G

E

I

V

H

R

L

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

I

A

A

A

L

H

G

G

A

-

Q

-

P

-

R

-

W

-

D

-

H

-

A

-

L

-

F

-

Q

-

H

-

F

F

F

P

A

L

S

A

I

D

G

A

P

R

A

R

Q

V

T

A

L

G

F

L

E

T

G

G

I

V

H

Y

Q

Q

V

V

P

P

P

A

G

G

H

A

V

V

L

M

E

D

W

-

S

-

T

-

Q

-

G

-

Y

-

G

-

V

-

T

-

P

-

L

-

S

-

A

-

V

I

D

D

E

L

A

G

H

S

D

G

A

T

A

A

R

V

Q

T

H

H

L

-

A

-

S

-

A

-

P

-

R

R

E

T

W

W

M

T

P

P

R

G

L

L

V

S

D

R

-

R

-

I

-

L

-

P

-

E

-

G

-

E

-

A

-

V

-

A

-

V

-

R

-

A

G

A

L

L

R

E

H

K

A

A

V

V

Q

A

D

Q

R

R

F

V

Q

T

-

P

G

G

D

D

G

T

P

P

V

L

A

-

C

V

Y
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

A

S

T

G

V

V

A

A

L

C

A

A

A

H

R

R

H

A

G

A

R

G

E

E

G

-

L

-

S

-

A

L

F

D

T

T

V

V

D
x
S

F
x
M

G

G

A

T

G

D

T

T

D

S

D

N

A

E

-

F

T

R

Q

E

A

A

A

R

G

A

I

V

A

V

A

D

S

H

L

L

G

R

L

T

R

R

H

H

E

R

V

E

V

I

P

T

V

I

S

P

E

T

A

T

Q

E

L

L

V

L

D

A

H

Q

F

L

A

P

D

Y

A

A

V

V

R

W

H

A

A

S

E

E

T

S

I

V

G

D

F

P

N
x
D

T

I

I

I

G

E

A
x
Y

A

L

R

L

W

P

I
x
L

L

T

G

A

R

L

V

Y

L

R

A

A

S

L

S

D

G

G

-

P

Y

E

K

R

A

R

V

I

L

L

A

T

G
|
G

D
x
Y

G
|
G

A

A

D
|
D

E
x
I

L

P

F

L

A

G

G

G

active site: A69 (≠ N73), G70 (= G74), D311 (≠ N340), Y337 (≠ D365)
binding arginine-n-methylcarbonyl phosphoric acid 5'-adenosine ester: V236 (≠ Y263), L237 (= L264), S238 (= S265), S243 (= S270), S261 (≠ D291), M262 (≠ F292), Y315 (≠ A344), L319 (≠ I348), G336 (= G364), Y337 (≠ D365), G338 (= G366), D340 (= D368), I341 (≠ E369)
binding magnesium ion: D242 (= D269), D340 (= D368)
binding pyrophosphate 2-: S238 (= S265), G240 (= G267), D242 (= D269), S243 (= S270), 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

1mb9A Beta-lactam synthetase complexed with atp (see paper)
26% identity, 48% coverage: 71:373/631 of query aligns to 68:344/485 of 1mb9A

query
sites
1mb9A

V

V

V

L

N
x
A

G
|
G

E

E

I

I

Y

Y

Q

N

Y

-

A

-

Q

R

R

D

Q

E

K

L

L

L

E

S

A

V

A

L

G

P

A

A

C

G

F

P

A

A

T

P

D

E

S

G

D

D

C

A

E

E

V

L

V

V

A

L

H

R

G

L

Y

L

L

E

Q

R

L

Y

G

D

I

L

D

H

Y

A

V

F

R

R

E

L

L

V

N

N

G

G

E

R

F

F

A

A

G

T

V

V

I

V

W

R

D

T

A

G

R

D

R

R

R

-

K

-

L

V

F

L

A

L

I

A

R

T

D

D

R

H

W

A

G

G

V

S

K

V

P

P

L

L

F

Y

Y

T

R

C

L

V

S

A

D

P

Q

G

G

E

I

V

H

R

L

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

I

A

A

A

L

F

G

P

A

L

Q

A

P

D

R

A

W

R

D

R

H

V

A

A

A

G

L

L

F

-

Q

-

H

-

F

-

A

-

S

-

I

-

G

-

P

-

A

-

Q

-

T

-

L

-

F

-

E

T

G

G

I

V

H

Y

Q

Q

V

V

P

P

P

A

G

G

H

A

V

V

L

M

E

D

W

-

S

-

T

-

Q

-

G

-

Y

-

G

-

V

-

T

-

P

-

L

-

S

-

A

-

V

I

D

D

E

L

A

G

H

S

D

G

A

T

A

A

R

V

Q

T

H

H

L

-

A

-

S

-

A

-

P

-

R

R

E

T

W

W

M

T

P

P

R

G

L

L

V

S

D

R

-

R

-

I

-

L

-

P

-

E

-

G

-

E

-

A

-

V

-

A

-

V

-

R

-

A

G

A

L

L

R

E

H

K

A

A

V

V

Q

A

D

Q

R

R

F

V

Q

T

-

P

G

G

D

D

G

T

P

P

V

L

A

-

C

V

Y
x
V

L
|
L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

A

S

T

G

V

V

A

A

L

C

A

A

A

H

R

R

H

A

G

A

R

G

E

E

G

-

L

-

S

-

A

L

F

D

T

T

V

V

D
x
S

F
x
M

G

G

A

T

G

D

T

T

D

S

D

N

A

E

-

F

T

R

Q

E

A

A

A

R

G

A

I

V

A

V

A

D

S

H

L

L

G

R

L

T

R

R

H

H

E

R

V

E

V

I

P

T

V

I

S

P

E

T

A

T

Q

E

L

L

V

L

D

A

H

Q

F

L

A

P

D

Y

A

A

V

V

R

W

H

A

A

S

E

E

T

S

I

V

G

D

F

P

N
x
D

T

I

I

I

G

E

A
x
Y

A

L

R

L

W

P

I
x
L

L

T

G

A

R

L

V

Y

L

R

A

A

S

L

S

D

G

G

-

P

Y

E

K

R

A

R

V

I

L

L

A

T

G
|
G

D
x
Y

G

G

A

A

D
|
D

E

I

L

P

F

L

A

G

G

G

active site: A70 (≠ N73), G71 (= G74), D310 (≠ N340), Y336 (≠ D365)
binding adenosine monophosphate: V235 (≠ Y263), L236 (= L264), S242 (= S270), S260 (≠ D291), M261 (≠ F292), Y314 (≠ A344), L318 (≠ I348), G335 (= G364), Y336 (≠ D365)
binding adenosine-5'-triphosphate: V235 (≠ Y263), L236 (= L264), S237 (= S265), G239 (= G267), D241 (= D269), S242 (= S270), S260 (≠ D291), M261 (≠ F292), L318 (≠ I348), G335 (= G364), D339 (= D368)
binding magnesium ion: D241 (= D269), D339 (= D368)
binding pyrophosphate 2-: S237 (= S265), G239 (= G267), D241 (= D269), S242 (= S270), D339 (= D368)

Sites not aligning to the query:

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

1jgtB Crystal structure of beta-lactam synthetase (see paper)
26% identity, 48% coverage: 71:373/631 of query aligns to 71:353/500 of 1jgtB

query
sites
1jgtB

V

V

V

L

N
x
A

G
|
G

E

E

I

I

Y

Y

Q

N

Y

-

A

-

Q

R

R

D

Q

E

K

L

L

L

E

S

A

V

A

L

G

P

A

A

C

G

F

P

A

A

T

P

D

E

S

G

D

D

C

A

E

E

V

L

V

V

A

L

H

R

G

L

Y

L

L

E

Q

R

L

Y

G

D

I

L

D

H

Y

A

V

F

R

R

E

L

L

V

N

N

G

G

E

R

F

F

A

A

G

T

V

V

I

V

W

R

D

T

A

G

R

D

R

R

R

-

K

-

L

V

F

L

A

L

I

A

R

T

D

D

R

H

W

A

G

G

V

S

K

V

P

P

L

L

F

Y

Y

T

R

C

L

V

S

A

D

P

Q

G

G

E

I

V

H

R

L

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

I

A

A

A

L

-

G

H

A

R

Q

D

P

P

R

K

W

G

D

F

H

P

A

L

A

A

L

D

F

A

Q

R

H

R

F

V

F

A

A

G

S

-

I

-

G

-

P

-

A

-

Q

-

T

-

L

-

F

L

E

T

G

G

I

V

H

Y

Q

Q

V

V

P

P

P

A

G

G

H

A

V

V

L

M

E

D

W

-

S

-

T

-

Q

-

G

-

Y

-

G

-

V

-

T

-

P

-

L

-

S

-

A

-

V

I

D

D

E

L

A

G

H

S

D

G

A

T

A

A

R

V

Q

T

H

H

L

-

A

-

S

-

A

-

P

-

R

R

E

T

W

W

M

T

P

P

R

G

L

L

V

S

D

R

-

R

-

I

-

L

-

P

-

E

-

G

-

E

-

A

-

V

-

A

-

V

-

R

-

A

G

A

L

L

R

E

H

K

A

A

V

V

Q

A

D

Q

R

R

F

V

Q

T

-

P

G

G

D

D

G

T

P

P

V

L

A

-

C

V

Y
x
V

L
|
L

S
|
S

G

G

G
|
G

V
x
I

D
|
D

S
|
S

A

S

T

G

V

V

A

A

L

C

A

A

A

H

R

R

H

A

G

A

R

G

E

E

G

-

L

-

S

-

A

L

F

D

T

T

V

V

D
x
S

F
x
M

G

G

A

T

G

D

T

T

D

S

D

N

A

E

-

F

T

R

Q

E

A

A

A

R

G

A

I

V

A

V

A

D

S

H

L

L

G

R

L

T

R

R

H

H

E

R

V

E

V

I

P

T

V

I

S

P

E

T

A

T

Q

E

L

L

V

L

D

A

H

Q

F

L

A

P

D

Y

A

A

V

V

R

W

H

A

A

S

E

E

T

S

I

V

G

D

F

P

N
x
D

T

I

I

I

G

E

A
x
Y

A

L

R

L

W

P

I
x
L

L

T

G

A

R

L

V

Y

L

R

A

A

S

L

S

D

G

G

-

P

Y

E

K

R

A

R

V

I

L

L

A

T

G
|
G

D
x
Y

G
|
G

A

A

D
|
D

E
x
I

L

P

F

L

A

G

G

G

active site: A73 (≠ N73), G74 (= G74), D319 (≠ N340), Y345 (≠ D365)
binding diphosphomethylphosphonic acid adenosyl ester: V244 (≠ Y263), L245 (= L264), S246 (= S265), G248 (= G267), I249 (≠ V268), D250 (= D269), S251 (= S270), S269 (≠ D291), M270 (≠ F292), L327 (≠ I348), G344 (= G364), Y345 (≠ D365), D348 (= D368)
binding n2-(carboxyethyl)-l-arginine: Y323 (≠ A344), Y345 (≠ D365), G346 (= G366), D348 (= D368), I349 (≠ E369)
binding magnesium ion: D250 (= D269), 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

1mc1A Beta-lactam synthetase with product (dgpc), amp and ppi (see paper)
25% identity, 48% coverage: 71:373/631 of query aligns to 63:340/491 of 1mc1A

query
sites
1mc1A

V

V

V

L

N
x
A

G
|
G

E

E

I

I

Y

Y

Q

N

Y

-

A

-

Q

R

R

D

Q

E

K

L

L

L

E

S

A

V

A

L

G

P

A

A

C

G

F

P

A

A

T

P

D

E

S

G

D

D

C

A

E

E

V

L

V

V

A

L

H

R

G

L

Y

L

L

E

Q

R

L

Y

G

D

I

L

D

H

Y

A

V

F

R

R

E

L

L

V

N

N

G

G

E

R

F

F

A

A

G

T

V

V

I

V

W

R

D

T

A

G

R

D

R

R

R

-

K

-

L

V

F

L

A

L

I

A

R

T

D

D

R

H

W

A

G

G

V

S

K

V

P

P

L

L

F

Y

Y

T

R

C

L

V

S

A

D

P

Q

G

G

E

I

V

H

R

L

A

A

S

S

T

E

E

I

A

K

K

A

A

L

L

I

A

A

A

L

-

G

-

A

-

Q

-

P

-

R

-

W

-

D

-

H

-

A

-

L

-

F

-

Q

-

H

G

F

F

F

P

A

L

S

A

I

D

G

A

P

R

A

R

Q

V

T

A

L

G

F

L

E

T

G

G

I

V

H

Y

Q

Q

V

V

P

P

P

A

G

G

H

A

V

V

L

M

E

D

W

-

S

-

T

-

Q

-

G

-

Y

-

G

-

V

-

T

-

P

-

L

-

S

-

A

-

V

I

D

D

E

L

A

G

H

S

D

G

A

T

A

A

R

V

Q

T

H

H

L

-

A

-

S

-

A

-

P

-

R

R

E

T

W

W

M

T

P

P

R

G

L

L

V

S

D

R

-

R

-

I

-

L

-

P

-

E

-

G

-

E

-

A

-

V

-

A

-

V

-

R

-

A

G

A

L

L

R

E

H

K

A

A

V

V

Q

A

D

Q

R

R

F

V

Q

T

-

P

G

G

D

D

G

T

P

P

V

L

A

-

C

V

Y
x
V

L

L

S
|
S

G

G

G
|
G

V

I

D
|
D

S
|
S

A

S

T

G

V

V

A

A

L

C

A

A

A

H

R

R

H

A

G

A

R

G

E

E

G

-

L

-

S

-

A

L

F

D

T

T

V

V

D
x
S

F
x
M

G

G

A

T

G

D

T

T

D

S

D

N

A

E

-

F

T

R

Q

E

A

A

A

R

G

A

I

V

A

V

A

D

S

H

L

L

G

R

L

T

R

R

H

H

E

R

V

E

V

I

P

T

V

I

S

P

E

T

A

T

Q

E

L

L

V

L

D

A

H

Q

F

L

A

P

D

Y

A

A

V

V

R

W

H

A

A

S

E

E

T

S

I

V

G

D

F

P

N
x
D

T

I

I

I

G

E

A
x
Y

A

L

R

L

W

P

I

L

L

T

G

A

R

L

V

Y

L

R

A

A

S

L

S

D

G

G

-

P

Y

E

K

R

A

R

V

I

L

L

A

T

G
|
G

D
x
Y

G
|
G

A

A

D
|
D

E
x
I

L

P

F

L

A

G

G

G

active site: A65 (≠ N73), G66 (= G74), D306 (≠ N340), Y332 (≠ D365)
binding adenosine monophosphate: V231 (≠ Y263), S233 (= S265), S238 (= S270), S256 (≠ D291), M257 (≠ F292), G331 (= G364)
binding magnesium ion: D237 (= D269), D335 (= D368)
binding deoxyguanidinoproclavaminic acid: Y310 (≠ A344), Y332 (≠ D365), G333 (= G366), I336 (≠ E369)
binding pyrophosphate 2-: S233 (= S265), G235 (= G267), D237 (= D269), S238 (= S270), 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

>AO356_26510 FitnessBrowser__pseudo5_N2C3_1:AO356_26510
MCGFVVACHHQAPVPTVTLDAALDTLRHRGPDGRASWLSADGLCGIGFHRLAMVGAREQT
QPFHTDDVHVVVNGEIYQYAAQRQKLEAAGACFATDSDCEVVAHGYLQLGIDYVRELNGE
FAGVIWDARRRKLFAIRDRWGVKPLFYRLSDQGIHLASEIKALIALGAQPRWDHAALFQH
FFASIGPAQTLFEGIHQVPPGHVLEWSTQGYGVTPLLSAVDEAHDAARQHLASAPREWMP
RLVDGLRHAVQDRFQGDGPVACYLSGGVDSATVAALAARHGREGLSAFTVDFGAGTDDAT
QAAGIAASLGLRHEVVPVSEAQLVDHFADAVRHAETIGFNTIGAARWILGRVLASSGYKA
VLAGDGADELFAGYSFSSVERLCARSHNHARLMTQVLEGGRQGLAAELGQPLPLFDMDPD
RFGGQVPYLLASWNYQRSGLRPLLRTQFLEAFRHFNPYEVLMQQTGASAASGLRRSLHLW
QKSMFANHILVSERFDMAHGIETRYPFLDNRVTAVAAMLPDEWLVEGAENKRFLREAVAA
LTPEAARCAAKRPFEAPAVFAQPGDGPFRRYLREVLHDSSVKHSGIFDVQELLRLEARLP
SLSGKMAQRVDSLLTMALSFFVLQQCFAVTE

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