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P54420

- ASNB_BACSU

UniProt

P54420 - ASNB_BACSU

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Protein

Asparagine synthetase [glutamine-hydrolyzing] 1

Gene

asnB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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: 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.
OMAiYFASERK.
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]
PIRSFiPIRSF001589. Asn_synthetase_glu-h. 1 hit.
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 [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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF008220 Genomic DNA. Translation: AAC00243.1 .
AL009126 Genomic DNA. Translation: CAB15032.1 .
U52812 Genomic DNA. Translation: AAB17067.1 .
PIRi H69590.
RefSeqi NP_390932.1. NC_000964.3.

3D structure databases

ProteinModelPortali P54420.
SMRi P54420. Positions 2-570.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P54420. 3 interactions.
MINTi MINT-8366280.
STRINGi 224308.BSU30540.

Protein family/group databases

MEROPSi C44.976.

Proteomic databases

PaxDbi P54420.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15032 ; CAB15032 ; BSU30540 .
GeneIDi 937236.
KEGGi bsu:BSU30540.
PATRICi 18978012. VBIBacSub10457_3194.

Organism-specific databases

GenoListi BSU30540. [Micado ]

Phylogenomic databases

eggNOGi COG0367.
HOGENOMi HOG000027495.
InParanoidi P54420.
KOi K01953.
OMAi YFASERK.
OrthoDBi EOG6P8TM1.
PhylomeDBi P54420.

Enzyme and pathway databases

UniPathwayi UPA00134 ; UER00195 .
BioCyci BSUB:BSU30540-MONOMER.

Family and domain databases

Gene3Di 3.40.50.620. 2 hits.
3.60.20.10. 1 hit.
InterProi IPR006426. 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 ]
Pfami PF00733. Asn_synthase. 1 hit.
PF13537. GATase_7. 1 hit.
[Graphical view ]
PIRSFi PIRSF001589. Asn_synthetase_glu-h. 1 hit.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR01536. asn_synth_AEB. 1 hit.
PROSITEi PS51278. GATASE_TYPE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 109 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