ID   ASNB_BACSU              Reviewed;         632 AA.
AC   P54420; O34902;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 1;
DE            EC=6.3.5.4;
GN   Name=asnB; Synonyms=asn; OrderedLocusNames=BSU30540;
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;
RX   PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA   Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT   "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT   200 kb rrnB-dnaB region.";
RL   Microbiology 143:3431-3441(1997).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
RC   STRAIN=168 / PY79;
RX   PubMed=8755891; DOI=10.1128/jb.178.15.4604-4610.1996;
RA   Yocum R., Perkins J.B., Howitt C.L., Pero J.;
RT   "Cloning and characterization of the metE gene encoding S-
RT   adenosylmethionine synthetase from Bacillus subtilis.";
RL   J. Bacteriol. 178:4604-4610(1996).
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: Main asparagine synthetase in vegetative cells.
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}.
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DR   EMBL; AF008220; AAC00243.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15032.1; -; Genomic_DNA.
DR   EMBL; U52812; AAB17067.1; -; Genomic_DNA.
DR   PIR; H69590; H69590.
DR   RefSeq; NP_390932.1; NC_000964.3.
DR   RefSeq; WP_004398625.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P54420; -.
DR   SMR; P54420; -.
DR   IntAct; P54420; 3.
DR   MINT; P54420; -.
DR   STRING; 224308.BSU30540; -.
DR   jPOST; P54420; -.
DR   PaxDb; P54420; -.
DR   PRIDE; P54420; -.
DR   DNASU; 937236; -.
DR   EnsemblBacteria; CAB15032; CAB15032; BSU_30540.
DR   GeneID; 937236; -.
DR   KEGG; bsu:BSU30540; -.
DR   PATRIC; fig|224308.179.peg.3312; -.
DR   eggNOG; COG0367; Bacteria.
DR   InParanoid; P54420; -.
DR   OMA; DIHTWMR; -.
DR   PhylomeDB; P54420; -.
DR   BioCyc; BSUB:BSU30540-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   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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..632
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing] 1"
FT                   /id="PRO_0000056932"
FT   DOMAIN          2..214
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         52..56
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         288
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         361..362
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            363
FT                   /note="Important for beta-aspartyl-AMP intermediate
FT                   formation"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        79..81
FT                   /note="EIY -> VNL (in Ref. 2; AAB17067)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   632 AA;  72666 MW;  155F11E6988901EA CRC64;
     MCGFVGVFNK HPLAQTADQE ELIKQMNQMI VHRGPDSDGY FHDEHVGFGF RRLSIIDVEN
     GGQPLSYEDE TYWIIFNGEI YNYIELREEL EAKGYTFNTD SDTEVLLATY RHYKEEAASK
     LRGMFAFLIW NKNDHVLYGA RDPFGIKPLY YTTINDQVYF ASERKSLMVA QNDIEIDKEA
     LQQYMSFQFV PEPSTLDAHV KKVEPGSQFT IRPDGDITFK TYFKANFKPV QTEEDKLVKE
     VRDAIYDSVN VHMRSDVPVG SFLSGGIDSS FIVSVAKEFH PSLKTFSVGF EQQGFSEVDV
     AKETAAALGI ENISKVISPE EYMNELPKIV WHFDDPLADP AAIPLYFVAK EAKKHVTVAL
     SGEGADELFG GYNIYREPLS LKPFERIPSG LKKMLLHVAA VMPEGMRGKS LLERGCTPLQ
     DRYIGNAKIF EESVKKQLLK HYNPNLSYRD VTKTYFTESS SYSDINKMQY VDIHTWMRGD
     ILLKADKMTM ANSLELRVPF LDKVVFDVAS KIPDELKTKN GTTKYLLRKA AEGIVPEHVL
     NRKKLGFPVP IRHWLKNEMN EWVRNIIQES QTDAYIHKDY VLQLLEDHCA DKADNSRKIW
     TVLIFMIWHS INIEKRYMPE ELSHQPKEVI FV