Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Asparagine synthetase [glutamine-hydrolyzing] 1

Gene

asnB

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

Functioni

Main asparagine synthetase in vegetative cells.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei2 – 21For GATase activityBy similarity
Binding sitei102 – 1021GlutamineBy similarity
Binding sitei288 – 2881ATP; via amide nitrogen and carbonyl oxygenBy similarity
Sitei363 – 3631Important for beta-aspartyl-AMP intermediate formationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi361 – 3622ATPBy similarity

GO - Molecular functioni

  1. asparagine synthase (glutamine-hydrolyzing) activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. glutamine metabolic process Source: UniProtKB-KW
  2. L-asparagine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Asparagine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU30540-MONOMER.
UniPathwayiUPA00134; UER00195.

Protein family/group databases

MEROPSiC44.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase [glutamine-hydrolyzing] 1 (EC:6.3.5.4)
Gene namesi
Name:asnB
Synonyms:asn
Ordered Locus Names:BSU30540
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU30540. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 632631Asparagine synthetase [glutamine-hydrolyzing] 1PRO_0000056932Add
BLAST

Proteomic databases

PaxDbiP54420.

Interactioni

Protein-protein interaction databases

IntActiP54420. 3 interactions.
MINTiMINT-8366280.
STRINGi224308.BSU30540.

Structurei

3D structure databases

ProteinModelPortaliP54420.
SMRiP54420. Positions 2-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 214213Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 565Glutamine 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.
HOGENOMiHOG000027495.
InParanoidiP54420.
KOiK01953.
OMAiHWLKNEM.
OrthoDBiEOG6P8TM1.
PhylomeDBiP54420.

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.

P54420-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCGFVGVFNK HPLAQTADQE ELIKQMNQMI VHRGPDSDGY FHDEHVGFGF
60 70 80 90 100
RRLSIIDVEN GGQPLSYEDE TYWIIFNGEI YNYIELREEL EAKGYTFNTD
110 120 130 140 150
SDTEVLLATY RHYKEEAASK LRGMFAFLIW NKNDHVLYGA RDPFGIKPLY
160 170 180 190 200
YTTINDQVYF ASERKSLMVA QNDIEIDKEA LQQYMSFQFV PEPSTLDAHV
210 220 230 240 250
KKVEPGSQFT IRPDGDITFK TYFKANFKPV QTEEDKLVKE VRDAIYDSVN
260 270 280 290 300
VHMRSDVPVG SFLSGGIDSS FIVSVAKEFH PSLKTFSVGF EQQGFSEVDV
310 320 330 340 350
AKETAAALGI ENISKVISPE EYMNELPKIV WHFDDPLADP AAIPLYFVAK
360 370 380 390 400
EAKKHVTVAL SGEGADELFG GYNIYREPLS LKPFERIPSG LKKMLLHVAA
410 420 430 440 450
VMPEGMRGKS LLERGCTPLQ DRYIGNAKIF EESVKKQLLK HYNPNLSYRD
460 470 480 490 500
VTKTYFTESS SYSDINKMQY VDIHTWMRGD ILLKADKMTM ANSLELRVPF
510 520 530 540 550
LDKVVFDVAS KIPDELKTKN GTTKYLLRKA AEGIVPEHVL NRKKLGFPVP
560 570 580 590 600
IRHWLKNEMN EWVRNIIQES QTDAYIHKDY VLQLLEDHCA DKADNSRKIW
610 620 630
TVLIFMIWHS INIEKRYMPE ELSHQPKEVI FV
Length:632
Mass (Da):72,666
Last modified:May 30, 2000 - v2
Checksum:i155F11E6988901EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 813EIY → VNL in AAB17067 (PubMed:9384377).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00243.1.
AL009126 Genomic DNA. Translation: CAB15032.1.
U52812 Genomic DNA. Translation: AAB17067.1.
PIRiH69590.
RefSeqiNP_390932.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15032; CAB15032; BSU30540.
GeneIDi937236.
KEGGibsu:BSU30540.
PATRICi18978012. VBIBacSub10457_3194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008220 Genomic DNA. Translation: AAC00243.1.
AL009126 Genomic DNA. Translation: CAB15032.1.
U52812 Genomic DNA. Translation: AAB17067.1.
PIRiH69590.
RefSeqiNP_390932.1. NC_000964.3.

3D structure databases

ProteinModelPortaliP54420.
SMRiP54420. Positions 2-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP54420. 3 interactions.
MINTiMINT-8366280.
STRINGi224308.BSU30540.

Protein family/group databases

MEROPSiC44.976.

Proteomic databases

PaxDbiP54420.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15032; CAB15032; BSU30540.
GeneIDi937236.
KEGGibsu:BSU30540.
PATRICi18978012. VBIBacSub10457_3194.

Organism-specific databases

GenoListiBSU30540. [Micado]

Phylogenomic databases

eggNOGiCOG0367.
HOGENOMiHOG000027495.
InParanoidiP54420.
KOiK01953.
OMAiHWLKNEM.
OrthoDBiEOG6P8TM1.
PhylomeDBiP54420.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
BioCyciBSUB:BSU30540-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. "Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region."
    Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
    Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168.
  2. "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.
  3. "Cloning and characterization of the metE gene encoding S-adenosylmethionine synthetase from Bacillus subtilis."
    Yocum R., Perkins J.B., Howitt C.L., Pero J.
    J. Bacteriol. 178:4604-4610(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
    Strain: 168 / PY79.
  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 nameiASNB_BACSU
AccessioniPrimary (citable) accession number: P54420
Secondary accession number(s): O34902
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: April 1, 2015
This is version 111 of the entry and version 2 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.