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Protein

Asparagine synthetase [glutamine-hydrolyzing] 2

Gene

asnH

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 sitei100 – 1001GlutamineBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi395 – 3962ATPBy 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:BSU39920-MONOMER.
UniPathwayiUPA00134; UER00195.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine synthetase [glutamine-hydrolyzing] 2 (EC:6.3.5.4)
Gene namesi
Name:asnH
Synonyms:yxaN
Ordered Locus Names:BSU39920
ORF Names:S14NR, VE7AR
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU39920. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 747746Asparagine synthetase [glutamine-hydrolyzing] 2PRO_0000056933Add
BLAST

Proteomic databases

PaxDbiP42113.
PRIDEiP42113.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU39920.

Structurei

3D structure databases

ProteinModelPortaliP42113.
SMRiP42113. Positions 2-542.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 218217Glutamine 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.
HOGENOMiHOG000155832.
InParanoidiP42113.
KOiK01953.
OMAiNCWHEDR.
OrthoDBiEOG6P8TM1.
PhylomeDBiP42113.

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.

P42113-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MCGLAGIINL AAPRSQECTF HILKGMADAI SYRGPDDEQY HIDSKVGFAF
60 70 80 90 100
RRLSILDLVN GQQPFLNEDG SIVVMVNGEI YNYKELKASL HNHMFKTTSD
110 120 130 140 150
CEVIVHLYEE KGIGFVDDII GMFSIAIWDK NKNKVFLVRD RFGIKPLFYT
160 170 180 190 200
ELKHELIFAS EIKSLFSHPH CPRQFNWKEA LSDIWLSGEA ASNHKETTSF
210 220 230 240 250
FVNIQNLDAG HYLEINLTTN ERKTASYWSL QDILLRQGYR ENLHPDDLIE
260 270 280 290 300
GYRELLADSV HRCLQSDVEV GLFLSGGIDS AAVAHFAAEK QDLHTFTVLS
310 320 330 340 350
QSTFTNEDAK YAHWLAKDLH LPNHQVLYQL GNDELLQPES YKHLLWICET
360 370 380 390 400
PFCGPEQLYK FHLHKYAKAI RPNLKVMLTG QGSDEFNGGY STTLSPAENP
410 420 430 440 450
SWEGFIESVN TMEMNRLHRL QGNIFRVWEE HFGLSPINLS YLKSNDSSQA
460 470 480 490 500
DPWQSYVLTK YRDLQMYNCW HEDRIAAANH IENRVPFLDH RLVEWVCGIP
510 520 530 540 550
DGLRKDLLWD KSVLRKSLTN ELHTSYTHRP KVPFFYGKDV RYTHKMMFHL
560 570 580 590 600
LKKNNYQLIE EAFSHSDASS IIQVEHIHAI MTYLEDDPEF TNFEFLLRLV
610 620 630 640 650
NMGLLSKMTK ETPSVQLDIT SHLESITIKD WHSQEGDIAS RLNISANKCE
660 670 680 690 700
GQDILALNPG VTLLRPESDS EHCIYIAEEG FIQFIVSEED VGAWLHILCD
710 720 730 740
INGKDTLHTI LDRHGVSLEE VAKYIQEAIE HNIILIKQKN LPEGAYR
Length:747
Mass (Da):85,932
Last modified:July 28, 2009 - v2
Checksum:iE1447AC0B72922CE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851W → C in BAA21593. (PubMed:7584049)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005554 Genomic DNA. Translation: BAA21593.1.
AL009126 Genomic DNA. Translation: CAB16028.2.
PIRiA69591.
RefSeqiNP_391871.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB16028; CAB16028; BSU39920.
GeneIDi937677.
KEGGibsu:BSU39920.
PATRICi18980052. VBIBacSub10457_4188.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB005554 Genomic DNA. Translation: BAA21593.1.
AL009126 Genomic DNA. Translation: CAB16028.2.
PIRiA69591.
RefSeqiNP_391871.2. NC_000964.3.

3D structure databases

ProteinModelPortaliP42113.
SMRiP42113. Positions 2-542.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU39920.

Proteomic databases

PaxDbiP42113.
PRIDEiP42113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB16028; CAB16028; BSU39920.
GeneIDi937677.
KEGGibsu:BSU39920.
PATRICi18980052. VBIBacSub10457_4188.

Organism-specific databases

GenoListiBSU39920. [Micado]

Phylogenomic databases

eggNOGiCOG0367.
HOGENOMiHOG000155832.
InParanoidiP42113.
KOiK01953.
OMAiNCWHEDR.
OrthoDBiEOG6P8TM1.
PhylomeDBiP42113.

Enzyme and pathway databases

UniPathwayiUPA00134; UER00195.
BioCyciBSUB:BSU39920-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]
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons."
    Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.
    DNA Res. 2:61-69(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / BGSC1A1.
  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. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 185.
  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 nameiASNH_BACSU
AccessioniPrimary (citable) accession number: P42113
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 28, 2009
Last modified: January 7, 2015
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

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.