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P54420 (ASNB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine synthetase [glutamine-hydrolyzing] 1

EC=6.3.5.4
Gene names
Name:asnB
Synonyms:asn
Ordered Locus Names:BSU30540
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length632 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Main asparagine synthetase in vegetative cells.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 632631Asparagine synthetase [glutamine-hydrolyzing] 1
PRO_0000056932

Regions

Domain2 – 214213Glutamine amidotransferase type-2
Nucleotide binding361 – 3622ATP By similarity
Region52 – 565Glutamine binding By similarity
Region77 – 793Glutamine binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site1021Glutamine By similarity
Binding site2881ATP; via amide nitrogen and carbonyl oxygen By similarity
Site3631Important for beta-aspartyl-AMP intermediate formation By similarity

Experimental info

Sequence conflict79 – 813EIY → VNL in AAB17067. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P54420 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 155F11E6988901EA

FASTA63272,666
        10         20         30         40         50         60 
MCGFVGVFNK HPLAQTADQE ELIKQMNQMI VHRGPDSDGY FHDEHVGFGF RRLSIIDVEN 

        70         80         90        100        110        120 
GGQPLSYEDE TYWIIFNGEI YNYIELREEL EAKGYTFNTD SDTEVLLATY RHYKEEAASK 

       130        140        150        160        170        180 
LRGMFAFLIW NKNDHVLYGA RDPFGIKPLY YTTINDQVYF ASERKSLMVA QNDIEIDKEA 

       190        200        210        220        230        240 
LQQYMSFQFV PEPSTLDAHV KKVEPGSQFT IRPDGDITFK TYFKANFKPV QTEEDKLVKE 

       250        260        270        280        290        300 
VRDAIYDSVN VHMRSDVPVG SFLSGGIDSS FIVSVAKEFH PSLKTFSVGF EQQGFSEVDV 

       310        320        330        340        350        360 
AKETAAALGI ENISKVISPE EYMNELPKIV WHFDDPLADP AAIPLYFVAK EAKKHVTVAL 

       370        380        390        400        410        420 
SGEGADELFG GYNIYREPLS LKPFERIPSG LKKMLLHVAA VMPEGMRGKS LLERGCTPLQ 

       430        440        450        460        470        480 
DRYIGNAKIF EESVKKQLLK HYNPNLSYRD VTKTYFTESS SYSDINKMQY VDIHTWMRGD 

       490        500        510        520        530        540 
ILLKADKMTM ANSLELRVPF LDKVVFDVAS KIPDELKTKN GTTKYLLRKA AEGIVPEHVL 

       550        560        570        580        590        600 
NRKKLGFPVP IRHWLKNEMN EWVRNIIQES QTDAYIHKDY VLQLLEDHCA DKADNSRKIW 

       610        620        630 
TVLIFMIWHS INIEKRYMPE ELSHQPKEVI FV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF008220 Genomic DNA. Translation: AAC00243.1.
AL009126 Genomic DNA. Translation: CAB15032.1.
U52812 Genomic DNA. Translation: AAB17067.1.
PIRH69590.
RefSeqNP_390932.1. NC_000964.3.

3D structure databases

ProteinModelPortalP54420.
SMRP54420. Positions 2-570.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP54420. 3 interactions.
MINTMINT-8366280.
STRING224308.BSU30540.

Proteomic databases

PaxDbP54420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15032; CAB15032; BSU30540.
GeneID937236.
KEGGbsu:BSU30540.
PATRIC18978012. VBIBacSub10457_3194.

Organism-specific databases

GenoListBSU30540. [Micado]

Phylogenomic databases

eggNOGCOG0367.
HOGENOMHOG000027495.
KOK01953.
OMAYFASERK.
OrthoDBEOG6P8TM1.
PhylomeDBP54420.

Enzyme and pathway databases

BioCycBSUB:BSU30540-MONOMER.
UniPathwayUPA00134; UER00195.

Family and domain databases

Gene3D3.40.50.620. 2 hits.
3.60.20.10. 1 hit.
InterProIPR006426. 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]
PfamPF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view]
PIRSFPIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
TIGRFAMsTIGR01536. asn_synth_AEB. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASNB_BACSU
AccessionPrimary (citable) accession number: P54420
Secondary accession number(s): O34902
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList