Reviewed, UniProtKB/Swiss-Prot P64247 (ASNH_MYCTU)

Names and origin

Protein names

Recommended name:
    Putative asparagine synthetase [glutamine-hydrolyzing]
    EC=6.3.5.4

Gene names

Name:	asnB
Ordered Locus Names:	Rv2201, MT2257
ORF Names:	MTCY190.12

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	652 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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.
Sequence similarities	Belongs to the asparagine synthetase family. Contains 1 glutamine amidotransferase type-2 domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Asparagine biosynthesis
Domain	Glutamine amidotransferase
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	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...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 652	652	Putative asparagine synthetase [glutamine-hydrolyzing]		PRO_0000056935
Regions
	Domain	2 – 231	230	Glutamine amidotransferase type-2
Sites
	Active site	2	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	P64247-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: C4624495A845F790	FASTA	652	72,150
	10 20 30 40 50 60 MCGLLAFVAA PAGAAGPEGA DAASAIARAS HLMRHRGPDE SGTWHAVDGA SGGVVFGFNR 70 80 90 100 110 120 LSIIDIAHSH QPLRWGPPEA PDRYVLVFNG EIYNYLELRD ELRTQHGAVF ATDGDGEAIL 130 140 150 160 170 180 AGYHHWGTEV LQRLRGMFAF ALWDTVTREL FCARDPFGIK PLFIATGAGG TAVASEKKCL 190 200 210 220 230 240 LDLVELVGFD TEIDHRALQH YTVLQYVPEP ETLHRGVRRL ESGCFARIRA DQLAPVITRY 250 260 270 280 290 300 FVPRFAASPI TNDNDQARYD EITAVLEDSV AKHMRADVTV GAFLSGGIDS TAIAALAIRH 310 320 330 340 350 360 NPRLITFTTG FEREGFSEID VAVASAEAIG ARHIAKVVSA DEFVAALPEI VWYLDEPVAD 370 380 390 400 410 420 PALVPLFFVA REARKHVKVV LSGEGADELF GGYTIYREPL SLRPFDYLPK PLRRSMGKVS 430 440 450 460 470 480 KPLPEGMRGK SLLHRGSLTL EERYYGNARS FSGAQLREVL PGFRPDWTHT DVTAPVYAES 490 500 510 520 530 540 AGWDPVARMQ HIDLFTWLRG DILVKADKIT MANSLELRVP FLDPEVFAVA SRLPAGAKIT 550 560 570 580 590 600 RTTTKYALRR ALEPIVPAHV LHRPKLGFPV PIRHWLRAGE LLEWAYATVG SSQAGHLVDI 610 620 630 640 650 AAVYRMLDEH RCGSSDHSRR LWTMLIFMLW HAIFVEHSVV PQISEPQYPV QL

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842579 Genomic DNA. Translation: CAA94270.1. AE000516 Genomic DNA. Translation: AAK46543.1.
PIR	B70785.
RefSeq	NP_216717.1. NP_336729.1.
3D structure databases
HSSP	HSSP built from PDB template 1CT9 based on UniProtKB P22106.
ModBase	Search...
Genome annotation databases
GeneID	888472. 924169.
GenomeReviews	Gene locus MT2257 in contig AE000516_GR. Gene locus Rv2201 in contig AL123456_GR.
KEGG	mtc:MT2257. mtu:Rv2201.
TIGR	MT2257.
Organism-specific databases
TubercuList	Rv2201.
Phylogenomic databases
HOGENOM	P64247.
OMA	KPFDYLP.
Enzyme and pathway databases
BRENDA	6.3.5.4. 809.
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...

Entry information

Entry name

ASNH_MYCTU

Accession

Primary (citable) accession number: P64247
Secondary accession number(s): Q10374

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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