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Protein

Asparagine synthetase [glutamine-hydrolyzing] 3

Gene

asnO

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Asparagine synthetase involved in sporulation.

Catalytic activityi

ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate.

Pathway:iL-asparagine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route).
Proteins known to be involved in this subpathway in this organism are:
  1. Asparagine synthetase [glutamine-hydrolyzing] 2 (asnH), Asparagine synthetase [glutamine-hydrolyzing] 1 (asnB), Asparagine synthetase [glutamine-hydrolyzing] 3 (asnO)
This subpathway is part of the pathway L-asparagine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-asparagine from L-aspartate (L-Gln route), the pathway L-asparagine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei102 – 1021GlutamineBy similarity
Sitei379 – 3791Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi377 – 3782ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis, Sporulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU10790-MONOMER.
UniPathwayiUPA00134; UER00195.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase [glutamine-hydrolyzing] 3 (EC:6.3.5.4)
Gene namesi
Name:asnO
Synonyms:yisO, yucB
Ordered Locus Names:BSU10790
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU10790. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 614613Asparagine synthetase [glutamine-hydrolyzing] 3PRO_0000056934Add
BLAST

Proteomic databases

PaxDbiO05272.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005966.

Structurei

3D structure databases

ProteinModelPortaliO05272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 216215Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 545Glutamine bindingBy similarity
Regioni77 – 793Glutamine bindingBy similarity

Sequence similaritiesi

Belongs to the asparagine synthetase family.Curated
Contains 1 glutamine amidotransferase type-2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0367.
HOGENOMiHOG000027494.
InParanoidiO05272.
KOiK01953.
OMAiFGQLMSG.
OrthoDBiEOG6Q5NPQ.
PhylomeDBiO05272.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O05272-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGITGWVDF KKQLVQEKQT MDRMTDTLSK RGPDDSNVWG EHHVLFGHKR
60 70 80 90 100
LAVVDIEGGR QPMACTYKGD TYTIIYNGEL YNTEDLRKEL RARGHQFERT
110 120 130 140 150
SDTEVLLHSY IEWQEDCVDH LNGIFAFAVW DEKRNLLFAA RDRLGVKPFF
160 170 180 190 200
YTKEGSSFLF GSEIKAILAH PDIKARVDRT GLSEIFGLGP SRTPGTGIFK
210 220 230 240 250
GIKEIRPAHA LTFSKDGLNI WRYWNVESEK HTDSFDDTVA NVRSLFQDAV
260 270 280 290 300
TRQLVSDVPV CTFLSGGLDS SAITAIAAGH FEKEGKAPLH TYSIDYEEND
310 320 330 340 350
KYFQASAFQP NDDGPWIEKM TEAFGTTHHK CVISQKDLVD HLEEAVLVKD
360 370 380 390 400
LPGMADVDSS LLWFCREIKK DFVVSLSGEC ADEIFGGYPW FHTADVESGF
410 420 430 440 450
PWMRSTEERI KLLSDSWQKK LNLKEYVNAK YEETLAETPL LDGETGVDKA
460 470 480 490 500
RRQLFYLNML WFMTNLLDRK DRMSMGASLE VRVPFADHRL VEYVWNIPWE
510 520 530 540 550
MKMHDNREKG ILRKALEGIL PDDILYRKKS PYPKTHHPEY TKGVSEWLKT
560 570 580 590 600
IRSQKDSVLH TLLDRKQLDQ LLETEGSSFK VPWFGQLMKG PQLIAHLAQI
610
HTWFEAYRID IDER
Length:614
Mass (Da):70,714
Last modified:May 30, 2000 - v3
Checksum:iD621D9A4557A8AC1
GO

Sequence cautioni

The sequence CAA70643.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z93940 Genomic DNA. Translation: CAB07965.1.
Y09476 Genomic DNA. Translation: CAA70643.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12919.2.
PIRiF69837.
RefSeqiNP_388960.2. NC_000964.3.
WP_003233080.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB12919; CAB12919; BSU10790.
GeneIDi939783.
KEGGibsu:BSU10790.
PATRICi18973862. VBIBacSub10457_1125.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z93940 Genomic DNA. Translation: CAB07965.1.
Y09476 Genomic DNA. Translation: CAA70643.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12919.2.
PIRiF69837.
RefSeqiNP_388960.2. NC_000964.3.
WP_003233080.1. NZ_JNCM01000035.1.

3D structure databases

ProteinModelPortaliO05272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100005966.

Proteomic databases

PaxDbiO05272.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12919; CAB12919; BSU10790.
GeneIDi939783.
KEGGibsu:BSU10790.
PATRICi18973862. VBIBacSub10457_1125.

Organism-specific databases

GenoListiBSU10790. [Micado]

Phylogenomic databases

eggNOGiCOG0367.
HOGENOMiHOG000027494.
InParanoidiO05272.
KOiK01953.
OMAiFGQLMSG.
OrthoDBiEOG6Q5NPQ.
PhylomeDBiO05272.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
BioCyciBSUB:BSU10790-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
3.60.20.10. 1 hit.
InterProiIPR006426. Asn_synth_AEB.
IPR001962. Asn_synthase.
IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR029055. Ntn_hydrolases_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR01536. asn_synth_AEB. 1 hit.
PROSITEiPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiASNO_BACSU
AccessioniPrimary (citable) accession number: O05272
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 24, 2015
This is version 113 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.