ECMDB

Identification

Name:

Asparagine synthetase B [glutamine-hydrolyzing]

Synonyms:

Not Available

Gene Name:

asnB

Enzyme Class:

6.3.5.4

Biological Properties

General Function:

Involved in asparagine synthase (glutamine-hydrolyzing) activity

Specific Function:

ATP + L-aspartate + L-glutamine + H(2)O = AMP + diphosphate + L-asparagine + L-glutamate

Cellular Location:

Not Available

SMPDB Pathways:

Asparagine biosynthesis PW000813
Aspartate metabolism PW000787
Nitrogen metabolism PW000755

KEGG Pathways:

Alanine, aspartate and glutamate metabolism ec00250
Metabolic pathways eco01100
Nitrogen metabolism ec00910

KEGG Reactions:

1.0

→

1.0

1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water → 1.0Adenosine monophosphate + 1.0L-Asparagine + 1.0L-Glutamate + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard

1.0

↔

1.0

1.0Adenosine triphosphate + 1.0L-Aspartic acid + 1.0L-Glutamine + 1.0Water ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Asparagine + 1.0L-Glutamate
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1.0

↔

1.0

1.0Adenosine triphosphate + 1.0L-Aspartic acid + 1.0L-Glutamine + 1.0Water + 1.0Ammonia ↔ 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Asparagine + 1.0L-Glutamate
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SMPDB Reactions:

1.0

1.0L-Aspartic acid

1.0

→

1.0

1.0Pyrophosphate

1.0L-Asparagine

1.0L-Glutamic acid

1.0

1.0Adenosine triphosphate + 1.0L-Aspartic acid + 1.0L-Glutamine + 1.0Water + 1.0L-Aspartic acid → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Asparagine + 1.0L-Glutamic acid + 1.0L-Asparagine + 1.0L-Glutamate
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1.0L-Aspartic acid

1.0

→

1.0L-Asparagine

1.0

1.0L-Glutamic acid

1.0Pyrophosphate

1.0

1.0L-Aspartic acid + 1.0Water + 1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0L-Aspartic acid → 1.0L-Asparagine + 1.0Hydrogen ion + 1.0Adenosine monophosphate + 1.0L-Glutamic acid + 1.0Pyrophosphate + 1.0L-Asparagine + 1.0L-Glutamate
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1.0L-Aspartic acid

1.0

→

1.0L-Asparagine

1.0

1.0Pyrophosphate

1.0

1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0Ammonium + 1.0L-Aspartic acid → 1.0L-Asparagine + 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0Hydrogen ion + 1.0L-Asparagine
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EcoCyc Reactions:

1.0

→

1.0

1.0L-Aspartic acid + 1.0Adenosine triphosphate + 1.0L-Glutamine + 1.0Water → 1.0Adenosine monophosphate + 1.0L-Asparagine + 1.0L-Glutamate + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Adenosine triphosphate + 1.0L-Aspartic acid + 1.0L-Glutamine + 1.0Water → 1.0Adenosine monophosphate + 1.0Pyrophosphate + 1.0L-Asparagine + 1.0L-Glutamate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00045	Adenosine monophosphate	MetaboCard
ECMDB00538	Adenosine triphosphate	MetaboCard
ECMDB21186	Ammonium	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00168	L-Asparagine	MetaboCard
ECMDB00191	L-Aspartic acid	MetaboCard
ECMDB00148	L-Glutamate	MetaboCard
ECMDB00641	L-Glutamine	MetaboCard
ECMDB04142	Pyrophosphate	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Function
asparagine synthase (glutamine-hydrolyzing) activity
carbon-nitrogen ligase activity, with glutamine as amido-N-donor
catalytic activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
Process
asparagine biosynthetic process
asparagine metabolic process
aspartate family amino acid metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular metabolic process
metabolic process

Gene Properties

Blattner:

b0674

Gene Orientation

Counterclockwise

Centisome Percentage:

15.02

Left Sequence End

696736

Right Sequence End

698400

Gene Sequence:

>1665 bp
ATGGCAATACAACACCCTGACATCCAGCCTGCTGTTAACCATAGCGTTCAGGTGGCGATC
GCTGGTGCCGGCCCGGTTGGGCTGATGATGGCGAACTATCTCGGCCAGATGGGCATTGAC
GTGCTGGTGGTGGAGAAACTCGATAAGTTGATCGACTACCCGCGTGCGATTGGTATTGAT
GACGAGGCGCTGCGCACCATGCAGTCGGTCGGCCTGGTCGATGATGTTCTGCCGCACACT
ACGCCGTGGCACGCGATGCGTTTTCTCACCCCGAAAGGCCGCTGTTTTGCTGATATTCAG
CCAATGACCGATGAATTTGGCTGGCCGCGCCGTAACGCCTTTATTCAGCCGCAGGTCGAT
GCGGTGATGCTGGAAGGGGTGTCGCGTTTTCCGAATGTGCGCTGCTTGTTTTCCCGCGAG
CTGGAGGCCTTCAGTCAGCAAGATGACGAAGTGACCTTGCACCTGAAAACGGCAGAAGGG
CAGCGGGAAATAGTCAAAGCCCAGTGGCTGGTAGCCTGTGACGGTGGAGCAAGTTTTGTC
CGTCGCACTCTGAATGTGCCGTTTGAAGGTAAAACTGCGCCAAATCAGTGGATTGTGGTA
GATATCGCCAACGATCCGTTAAGTACGCCGCATATCTATTTGTGTTGCGATCCGGTGCGC
CCGTATGTTTCTGCCGCGCTGCCTCATGCGGTACGTCGCTTTGAATTTATGGTGATGCCG
GGAGAAACCGAAGAGCAGCTGCGTGAGCCGCAAAATATGCGCAAGCTGTTAAGCAAAGTG
CTGCCTAATCCGGACAATGTTGAATTGATTCGCCAGCGTGTCTACACCCACAACGCGCGA
CTGGCGCAACGTTTCCGTATTGATCGCGTACTGCTGGCGGGCGATGCCGCGCACATCATG
CCGGTATGGCAGGGGCAGGGCTATAACAGTGGTATGCGCGACGCCTTTAACCTCGCATGG
AAACTGGCGTTGGTTATCCAGGGGAAAGCCCGCGATGCGCTGCTCGATACCTATCAACAA
GAACGTCGCGATCACGCCAAAGCGATGATTGACCTGTCCGTGACGGCGGGCAACGTGCTG
GCTCCGCCGAAACGCTGGCAGGGTACGTTACGTGACGGCGTTTCCTGGCTGTTGAATTAT
CTGCCGCCAGTAAAACGCTACTTCCTCGAAATGCGCTTCAAGCCGATGCCGCAATATTAC
GGCGGTGCGCTGATGCGTGAGGGCGAAGCGAAGCACTCTCCGGTCGGCAAGATGTTTATT
CAGCCGAAAGTCACGCTGGAAAACGGCGACGTGACGCTGCTCGATAACGCGATCGGCGCG
AACTTCGCGGTAATTGGCTGGGGATGCAATCCACTGTGGGGGATGAGCGACGAGCAAATC
CAGCAGTGGCGCGCGTTGGGCACACGCTTCATTCAGGTGGTGCCGGAAGTGCAAATTCAT
ACCGCACAGGATAACCACGACGGCGTACTACGCGTGGGCGATACGCAAGGTCGCCTGCGT
AGCTGGTTCGCGCAACACAATGCTTCGCTGGTGGTGATGCGCCCGGATCGCTTTGTTGCC
GCCACCGCCATTCCGCAAACCCTGGGCAAGACCCTGAATAAACTGGCGTCGGTGATGACG
CTGACCCGCCCTGATGCCGACGTTTCTGTCGAAAAGGTAGCCTGA

Protein Properties

Pfam Domain Function:

Asn_synthase (PF00733 )

Protein Residues:

554

Protein Molecular Weight:

62659

Protein Theoretical pI:

PDB File:

1CT9

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Asparagine synthetase B [glutamine-hydrolyzing]
MCSIFGVFDIKTDAVELRKKALELSRLMRHRGPDWSGIYASDNAILAHERLSIVDVNAGA
QPLYNQQKTHVLAVNGEIYNHQALRAEYGDRYQFQTGSDCEVILALYQEKGPEFLDDLQG
MFAFALYDSEKDAYLIGRDHLGIIPLYMGYDEHGQLYVASEMKALVPVCRTIKEFPAGSY
LWSQDGEIRSYYHRDWFDYDAVKDNVTDKNELRQALEDSVKSHLMSDVPYGVLLSGGLDS
SIISAITKKYAARRVEDQERSEAWWPQLHSFAVGLPGSPDLKAAQEVANHLGTVHHEIHF
TVQEGLDAIRDVIYHIETYDVTTIRASTPMYLMSRKIKAMGIKMVLSGEGSDEVFGGYLY
FHKAPNAKELHEETVRKLLALHMYDCARANKAMSAWGVEARVPFLDKKFLDVAMRINPQD
KMCGNGKMEKHILRECFEAYLPASVAWRQKEQFSDGVGYSWIDTLKEVAAQQVSDQQLET
ARFRFPYNTPTSKEAYLYREIFEELFPLPSAAECVPGGPSVACSSAKAIEWDEAFKKMDD
PSGRAVGVHQSAYK

References

External Links:

Resource	Link
Uniprot ID:	P22106
Uniprot Name:	ASNB_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85674489
PDB ID:	1CT9
Ecogene ID:	EG10092
Ecocyc:	EG10092
ColiBase:	b0674
Kegg Gene:	b0674
EchoBASE ID:	EB0090
CCDB:	ASNB_ECOLI
BacMap:	16128650

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Larsen, T. M., Boehlein, S. K., Schuster, S. M., Richards, N. G., Thoden, J. B., Holden, H. M., Rayment, I. (1999). "Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product." Biochemistry 38:16146-16157. Pubmed: 10587437
Larsen, T. M., Boehlein, S. K., Schuster, S. M., Richards, N. G., Thoden, J. B., Holden, H. M., Rayment, I. I (2000). "Three-dimensional structure of escherichia coli asparagine synthetase B: A short journey from substrate to product" Biochemistry 39:7330. Pubmed: 10852734
Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
Scofield, M. A., Lewis, W. S., Schuster, S. M. (1990). "Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B." J Biol Chem 265:12895-12902. Pubmed: 1973930

Asparagine synthetase B [glutamine-hydrolyzing] (P22106)