Reviewed, UniProtKB/Swiss-Prot O05272 (ASNO_BACSU)

Names and origin

Protein names

Recommended name:
    Asparagine synthetase [glutamine-hydrolyzing] 3
    EC=6.3.5.4

Gene names

Name:	asnO
Synonyms:	yisO, yucB
Ordered Locus Names:	BSU10790

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	614 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Asparagine synthetase involved in sporulation.
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 Sporulation
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 sporulation resulting in formation of a cellular spore 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 – 614	614	Asparagine synthetase [glutamine-hydrolyzing] 3		PRO_0000056934
Regions
	Domain	2 – 216	215	Glutamine amidotransferase type-2
Sites
	Active site	2	1	For GATase activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	O05272-1 [UniParc]. Last modified May 30, 2000. Version 3. Checksum: D621D9A4557A8AC1	FASTA	614	70,714
	10 20 30 40 50 60 MCGITGWVDF KKQLVQEKQT MDRMTDTLSK RGPDDSNVWG EHHVLFGHKR LAVVDIEGGR 70 80 90 100 110 120 QPMACTYKGD TYTIIYNGEL YNTEDLRKEL RARGHQFERT SDTEVLLHSY IEWQEDCVDH 130 140 150 160 170 180 LNGIFAFAVW DEKRNLLFAA RDRLGVKPFF YTKEGSSFLF GSEIKAILAH PDIKARVDRT 190 200 210 220 230 240 GLSEIFGLGP SRTPGTGIFK GIKEIRPAHA LTFSKDGLNI WRYWNVESEK HTDSFDDTVA 250 260 270 280 290 300 NVRSLFQDAV TRQLVSDVPV CTFLSGGLDS SAITAIAAGH FEKEGKAPLH TYSIDYEEND 310 320 330 340 350 360 KYFQASAFQP NDDGPWIEKM TEAFGTTHHK CVISQKDLVD HLEEAVLVKD LPGMADVDSS 370 380 390 400 410 420 LLWFCREIKK DFVVSLSGEC ADEIFGGYPW FHTADVESGF PWMRSTEERI KLLSDSWQKK 430 440 450 460 470 480 LNLKEYVNAK YEETLAETPL LDGETGVDKA RRQLFYLNML WFMTNLLDRK DRMSMGASLE 490 500 510 520 530 540 VRVPFADHRL VEYVWNIPWE MKMHDNREKG ILRKALEGIL PDDILYRKKS PYPKTHHPEY 550 560 570 580 590 600 TKGVSEWLKT IRSQKDSVLH TLLDRKQLDQ LLETEGSSFK VPWFGQLMKG PQLIAHLAQI 610 HTWFEAYRID IDER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacillus subtilis genome project, DNA sequence from yucA to yucH." Oudega B., Koningstein G., Duesterhoeft A. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis." Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J. Microbiology 143:3305-3308(1997) [PubMed: 9353931] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Three asparagine synthetase genes of Bacillus subtilis." Yoshida K., Fujita Y., Ehrlich S.D. J. Bacteriol. 181:6081-6091(1999) [PubMed: 10498721] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z93940 Genomic DNA. Translation: CAB07965.1. Y09476 Genomic DNA. Translation: CAA70643.1. Different initiation. AL009126 Genomic DNA. Translation: CAB12919.2.
PIR	F69837.
RefSeq	NP_388960.2.
3D structure databases
HSSP	HSSP built from PDB template 1CT9 based on UniProtKB P22106.
ModBase	Search...
Genome annotation databases
GeneID	939783.
GenomeReviews	Gene locus BSU10790 in contig AL009126_GR.
KEGG	bsu:BSU10790.
NMPDR	fig|224308.1.peg.1079.
Organism-specific databases
SubtiList	BG12240. asnO. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	O05272.
OMA	APLHTYS.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU1079-MON.
BRENDA	6.3.5.4. 150.
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

ASNO_BACSU

Accession

Primary (citable) accession number: O05272

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	November 3, 2009
This is version 71 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)