ASNO_BACSU
ID ASNO_BACSU Reviewed; 614 AA.
AC O05272;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 3;
DE EC=6.3.5.4;
GN Name=asnO; Synonyms=yisO, yucB; OrderedLocusNames=BSU10790;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Oudega B., Koningstein G., Duesterhoeft A.;
RT "Bacillus subtilis genome project, DNA sequence from yucA to yucH.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10498721; DOI=10.1128/jb.181.19.6081-6091.1999;
RA Yoshida K., Fujita Y., Ehrlich S.D.;
RT "Three asparagine synthetase genes of Bacillus subtilis.";
RL J. Bacteriol. 181:6081-6091(1999).
CC -!- FUNCTION: Asparagine synthetase involved in sporulation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartate + L-glutamine = AMP + diphosphate +
CC H(+) + L-asparagine + L-glutamate; Xref=Rhea:RHEA:12228,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58048, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.4;
CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC asparagine from L-aspartate (L-Gln route): step 1/1.
CC -!- SIMILARITY: Belongs to the asparagine synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA70643.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z93940; CAB07965.1; -; Genomic_DNA.
DR EMBL; Y09476; CAA70643.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12919.2; -; Genomic_DNA.
DR PIR; F69837; F69837.
DR RefSeq; NP_388960.2; NC_000964.3.
DR RefSeq; WP_003233080.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O05272; -.
DR SMR; O05272; -.
DR STRING; 224308.BSU10790; -.
DR PaxDb; O05272; -.
DR PRIDE; O05272; -.
DR EnsemblBacteria; CAB12919; CAB12919; BSU_10790.
DR GeneID; 939783; -.
DR KEGG; bsu:BSU10790; -.
DR PATRIC; fig|224308.179.peg.1160; -.
DR eggNOG; COG0367; Bacteria.
DR InParanoid; O05272; -.
DR OMA; DWSGIYS; -.
DR PhylomeDB; O05272; -.
DR BioCyc; BSUB:BSU10790-MON; -.
DR UniPathway; UPA00134; UER00195.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd01991; Asn_Synthase_B_C; 1.
DR CDD; cd00712; AsnB; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR006426; Asn_synth_AEB.
DR InterPro; IPR001962; Asn_synthase.
DR InterPro; IPR033738; AsnB_N.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF00733; Asn_synthase; 1.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome;
KW Sporulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..614
FT /note="Asparagine synthetase [glutamine-hydrolyzing] 3"
FT /id="PRO_0000056934"
FT DOMAIN 2..216
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250"
FT BINDING 50..54
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 77..79
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 377..378
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 379
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000250"
SQ SEQUENCE 614 AA; 70714 MW; D621D9A4557A8AC1 CRC64;
MCGITGWVDF KKQLVQEKQT MDRMTDTLSK RGPDDSNVWG EHHVLFGHKR LAVVDIEGGR
QPMACTYKGD TYTIIYNGEL YNTEDLRKEL RARGHQFERT SDTEVLLHSY IEWQEDCVDH
LNGIFAFAVW DEKRNLLFAA RDRLGVKPFF YTKEGSSFLF GSEIKAILAH PDIKARVDRT
GLSEIFGLGP SRTPGTGIFK GIKEIRPAHA LTFSKDGLNI WRYWNVESEK HTDSFDDTVA
NVRSLFQDAV TRQLVSDVPV CTFLSGGLDS SAITAIAAGH FEKEGKAPLH TYSIDYEEND
KYFQASAFQP NDDGPWIEKM TEAFGTTHHK CVISQKDLVD HLEEAVLVKD LPGMADVDSS
LLWFCREIKK DFVVSLSGEC ADEIFGGYPW FHTADVESGF PWMRSTEERI KLLSDSWQKK
LNLKEYVNAK YEETLAETPL LDGETGVDKA RRQLFYLNML WFMTNLLDRK DRMSMGASLE
VRVPFADHRL VEYVWNIPWE MKMHDNREKG ILRKALEGIL PDDILYRKKS PYPKTHHPEY
TKGVSEWLKT IRSQKDSVLH TLLDRKQLDQ LLETEGSSFK VPWFGQLMKG PQLIAHLAQI
HTWFEAYRID IDER
