Asparagine synthetase B [glutamine-hydrolyzing] - Escherichia coli (strain K12)

Names and origin

Protein names

Recommended name:
Asparagine synthetase B [glutamine-hydrolyzing]
EC=6.3.5.4

Gene names

Name:	asnB
Ordered Locus Names:	b0674, JW0660

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + L-aspartate + L-glutamine + H₂O = AMP + diphosphate + L-asparagine + L-glutamate.
Pathway	Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
Subunit structure	Homodimer.
Miscellaneous	This enzyme can use either ammonia or glutamine as a substrate with glutamine being the preferred nitrogen source.
Sequence similarities	Belongs to the asparagine synthetase family. Contains 1 glutamine amidotransferase type-2 domain.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 554

553

Asparagine synthetase B [glutamine-hydrolyzing]

PRO_0000056931

Regions

Domain

2 – 186

185

Glutamine amidotransferase type-2

Sites

Active site

2

1

For GATase activity

Secondary structure

1

.

554

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P22106-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 9091B269112C9F5C
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FASTA

554

62,659

        10         20         30         40         50         60 
MCSIFGVFDI KTDAVELRKK ALELSRLMRH RGPDWSGIYA SDNAILAHER LSIVDVNAGA 

        70         80         90        100        110        120 
QPLYNQQKTH VLAVNGEIYN HQALRAEYGD RYQFQTGSDC EVILALYQEK GPEFLDDLQG 

       130        140        150        160        170        180 
MFAFALYDSE KDAYLIGRDH LGIIPLYMGY DEHGQLYVAS EMKALVPVCR TIKEFPAGSY 

       190        200        210        220        230        240 
LWSQDGEIRS YYHRDWFDYD AVKDNVTDKN ELRQALEDSV KSHLMSDVPY GVLLSGGLDS 

       250        260        270        280        290        300 
SIISAITKKY AARRVEDQER SEAWWPQLHS FAVGLPGSPD LKAAQEVANH LGTVHHEIHF 

       310        320        330        340        350        360 
TVQEGLDAIR DVIYHIETYD VTTIRASTPM YLMSRKIKAM GIKMVLSGEG SDEVFGGYLY 

       370        380        390        400        410        420 
FHKAPNAKEL HEETVRKLLA LHMYDCARAN KAMSAWGVEA RVPFLDKKFL DVAMRINPQD 

       430        440        450        460        470        480 
KMCGNGKMEK HILRECFEAY LPASVAWRQK EQFSDGVGYS WIDTLKEVAA QQVSDQQLET 

       490        500        510        520        530        540 
ARFRFPYNTP TSKEAYLYRE IFEELFPLPS AAECVPGGPS VACSSAKAIE WDEAFKKMDD 

       550 
PSGRAVGVHQ SAYK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B." Scofield M.A., Lewis W.S., Schuster S.M. J. Biol. Chem. 265:12895-12902(1990) [PubMed: 1973930] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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." 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. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, 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. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product." Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G.J., Thoden J.B., Holden H.M., Rayment I. Biochemistry 38:16146-16157(1999) [PubMed: 10587437] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[6]	Erratum Larsen T.M., Boehlein S.K., Schuster S.M., Richards N.G.J., Thoden J.B., Holden H.M., Rayment I. Biochemistry 39:7330-7330(2000) [PubMed: 10852734] [Abstract]

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Cross-references

Sequence databases

J05554 Genomic DNA. Translation: AAA23498.1.
U00096 Genomic DNA. Translation: AAC73768.1.
AP009048 Genomic DNA. Translation: BAA35317.1.

PIR

AJECN. A36616.

RefSeq

AP_001312.1.
NP_415200.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CT9	X-ray	2.00	A/B/C/D	3-554	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9177N.

STRING

P22106.

Genome annotation databases

GeneID

945281.

GenomeReviews

Gene locus JW0660 in contig AP009048_GR.
Gene locus b0674 in contig U00096_GR.

KEGG

ecj:JW0660.
eco:b0674.

Organism-specific databases

EchoBASE

EB0090.

EcoGene

EG10092. asnB.

CMR

Search...

Phylogenomic databases

HOGENOM

P22106.

OMA

NKSLAAW.

Enzyme and pathway databases

BioCyc

EcoCyc:ASNSYNB-MON.
MetaCyc:ASNSYNB-MON.

Gene expression databases

Genevestigator

P22106.

Family and domain databases

InterPro

IPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR000583. GATase_2.
IPR017932. GATase_II.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

Pfam

PF00733. Asn_synthase. 1 hit.
PF00310. GATase_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01536. asn_synth_AEB. 1 hit.

PROSITE

PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

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Entry information

Entry name

ASNB_ECOLI

Accession

Primary (citable) accession number: P22106

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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