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 (= H25) mutation to A: 4,5-fold decrease in glutamine affinity.
D34 (= D29) mutation D->N,E: Little effect on the kinetic properties.
H81 (≠ Y75) mutation to A: 5-fold decrease in glutamine affinity.
A105 (= A99) mutation to H: Little effect on the kinetic properties.
E349 (= E354) 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)
34% identity, 58% coverage: 14:363/601 of query aligns to 18:341/497 of 1ct9A

query
sites
1ct9A

K

K

A

A

K

L

D

E

A

L

L

S

A

R

L

L

L

M

S

R

H

H

R

R

G

G

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P

D

D

F

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C

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G

G

I

I

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Y

Q

A

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S

Q

D

N

N

L

A

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F

L

A

A

H

H

H

E

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x
R

L
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I

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x
V

G

D

T

V

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N

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A

D

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Q

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P

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Y

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E

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K

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N
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Y

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A

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M

F

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D

D

D

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E

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-

D

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S

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A

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Y

Y

active site: L50 (= L46), N74 (= N69), G75 (= G70), T305 (≠ L327), R308 (≠ P330), E332 (= E354)
binding adenosine monophosphate: L232 (= L251), L233 (= L252), S234 (= S253), S239 (= S258), A255 (≠ T276), V256 (≠ L277), D263 (≠ E287), M316 (≠ L338), S330 (= S352), G331 (= G353), E332 (= E354)
binding glutamine: R49 (≠ K45), L50 (= L46), I52 (= I48), V53 (≠ T49), N74 (= N69), G75 (= G70), E76 (= E71), D98 (≠ E93)

Sites not aligning to the query:

active site: 1, 366
binding glutamine: 1

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, 63% coverage: 1:378/601 of query aligns to 1:388/557 of P78753

query
sites
P78753

M

M

C

C

A

G

I

I

F

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G

A

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H

L

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A

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A

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D

D

F

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D

G

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A

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Q

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P

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Y

S

E

D

-

D

-

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K

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N

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G

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Y

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L

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)
28% identity, 60% coverage: 1:363/601 of query aligns to 1:374/561 of P08243

query
sites
P08243

M

M

C
|
C

A

G

I

I

F

W

G
x
A

I

L

L

F

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G

E

S

H

D

D

D

E

C

K

L

K

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A

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D

C

A

L

L

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A

A

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M

-

K

L

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A

H

H

R

R

G

G

G

P

D

D

-

A

-

F

-

R

F

F

C

E

G

N

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N

Q

G

G

Y

Q

T

N

N

L

C

F

C

F

F

A

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H

F

H

H

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R

L

L

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A

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D

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S

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M

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Q

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P

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-

K

S

K

Y

Y

E

P

K

Y

I

L

L

W

L

L

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C

F

Y

N

N

G

G

E

E

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I

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Y

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N

Y

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S

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C

-

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D

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F

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C

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D

D

T
x
V

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P

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F

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P

-

G

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F

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E

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I

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V

Q

K

N

N

A

N

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A

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A

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L

M

Y

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F

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Y

I

I

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K

D

N

G

T

Y

D

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S

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x
F

S

S

G

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D

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L

F

T

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Q

G

G

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 (≠ T215) to E: in dbSNP:rs1049674
F362 (vs. gap) 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)
29% identity, 60% coverage: 2:363/601 of query aligns to 1:361/509 of 6gq3A

query
sites
6gq3A

C
|
C

A

G

I

I

F
x
W

G

A

I

L

L

F

G

G

E

S

H

D

D

D

E

C

K

L

K

S

A

V

K

Q

D

C

A

L

L

S

A

A

L

M

-

K

L

I

S

A

H

H

R

R

G

G

G

P

D

D

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|
L

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Y

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W

L

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Y

N
|
N

G
|
G

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|
E

I

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T

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D

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x
R

A

A

A

S

V

V

P

G

L

M

Y

Y

L

L

L

I

F

S

G

K

H

Y

I

I

K

R

K

K

D

N

G

T

Y

D

K

S

V

V

L

I

-

F

S

S

G

G

E

E

G

G

S

S

D

D

E

E

L

L

F

T

L

Q

G

G

Y

Y

active site: W4 (≠ F5), L49 (= L46), N74 (= N69), G75 (= G70), T324 (≠ L327), R327 (≠ P330)
binding 5-oxo-l-norleucine: C1 (= C2), R48 (≠ K45), V51 (≠ I48), V52 (≠ T49), Y73 (≠ F68), N74 (= N69), G75 (= G70), E76 (= E71), V95 (≠ S92), D96 (≠ E93)

Query Sequence

>WP_011371799.1 NCBI__GCF_000012965.1:WP_011371799.1
MCAIFGILGEHDEKKAKDALALLSHRGGDFCGITQGQNLFFAHHKLSITGTNSDSNQPFS
YEKILLSFNGEIYNYKELRADLSCEFNFKTQSEAEVIAASYLKWGVNFVLHLRGMFAIAL
LDDEILYLFRDRLGKKPLFYLHVNAFIFASEIKALVPFLHSIEMDEDALLSYLSFLAPTP
PFTFFKNIKKLAAGEYLIFKDSKVEIKRYFDLLDTTPSLITNRDEAVFLVQNALEEAINI
RLATDVPMASLLSGGIDSAAINAYAKKASMDIQTYTLGYKEFAKYDERQNASLSASLLGV
KNRAVEISQREFDESCDIVLDALDEPLNDPAAVPLYLLFGHIKKDGYKVVLSGEGSDELF
LGYRQYFEFLDIEKLTNLKNKNWLSGYFHSNFSMNREWERYKRVFDGSLLFRTTGENFTD
LQKNVSMKRNVRDNESLKYIQNYRETFLASSHSDESIWYSYIDLHLFQAEHYLTKLDRLS
MAHSIESRTPFLDHKLASLVFSIDPKIRYMDGVTKSLLKSALKPMLDEKILSRRKKGFSN
PFMEYLIESKKISLIKEVNEKTGIFKKEILDEHIKKAANGGFKQHIWGLYVLSVWLKKYL
L

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