ID   ASNH_BACSU              Reviewed;         747 AA.
AC   P42113;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing] 2;
DE            EC=6.3.5.4;
GN   Name=asnH; Synonyms=yxaN; OrderedLocusNames=BSU39920;
GN   ORFNames=S14NR, VE7AR;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / BGSC1A1;
RX   PubMed=7584049; DOI=10.1093/dnares/2.2.61;
RA   Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y.;
RT   "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome
RT   between the gnt and iol operons.";
RL   DNA Res. 2:61-69(1995).
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   SEQUENCE REVISION TO 185.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB005554; BAA21593.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB16028.2; -; Genomic_DNA.
DR   PIR; A69591; A69591.
DR   RefSeq; NP_391871.2; NC_000964.3.
DR   RefSeq; WP_003244103.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P42113; -.
DR   SMR; P42113; -.
DR   STRING; 224308.BSU39920; -.
DR   PaxDb; 224308-BSU39920; -.
DR   EnsemblBacteria; CAB16028; CAB16028; BSU_39920.
DR   GeneID; 937677; -.
DR   KEGG; bsu:BSU39920; -.
DR   PATRIC; fig|224308.179.peg.4318; -.
DR   eggNOG; COG0367; Bacteria.
DR   InParanoid; P42113; -.
DR   OrthoDB; 9763290at2; -.
DR   PhylomeDB; P42113; -.
DR   BioCyc; BSUB:BSU39920-MONOMER; -.
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; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR01536; asn_synth_AEB; 1.
DR   PANTHER; PTHR43284:SF1; ASPARAGINE SYNTHETASE; 1.
DR   PANTHER; PTHR43284; ASPARAGINE SYNTHETASE (GLUTAMINE-HYDROLYZING); 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 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..747
FT                   /note="Asparagine synthetase [glutamine-hydrolyzing] 2"
FT                   /id="PRO_0000056933"
FT   DOMAIN          2..218
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         100
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250"
FT   BINDING         395..396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        185
FT                   /note="W -> C (in Ref. 1; BAA21593)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   747 AA;  85932 MW;  E1447AC0B72922CE CRC64;
     MCGLAGIINL AAPRSQECTF HILKGMADAI SYRGPDDEQY HIDSKVGFAF RRLSILDLVN
     GQQPFLNEDG SIVVMVNGEI YNYKELKASL HNHMFKTTSD CEVIVHLYEE KGIGFVDDII
     GMFSIAIWDK NKNKVFLVRD RFGIKPLFYT ELKHELIFAS EIKSLFSHPH CPRQFNWKEA
     LSDIWLSGEA ASNHKETTSF FVNIQNLDAG HYLEINLTTN ERKTASYWSL QDILLRQGYR
     ENLHPDDLIE GYRELLADSV HRCLQSDVEV GLFLSGGIDS AAVAHFAAEK QDLHTFTVLS
     QSTFTNEDAK YAHWLAKDLH LPNHQVLYQL GNDELLQPES YKHLLWICET PFCGPEQLYK
     FHLHKYAKAI RPNLKVMLTG QGSDEFNGGY STTLSPAENP SWEGFIESVN TMEMNRLHRL
     QGNIFRVWEE HFGLSPINLS YLKSNDSSQA DPWQSYVLTK YRDLQMYNCW HEDRIAAANH
     IENRVPFLDH RLVEWVCGIP DGLRKDLLWD KSVLRKSLTN ELHTSYTHRP KVPFFYGKDV
     RYTHKMMFHL LKKNNYQLIE EAFSHSDASS IIQVEHIHAI MTYLEDDPEF TNFEFLLRLV
     NMGLLSKMTK ETPSVQLDIT SHLESITIKD WHSQEGDIAS RLNISANKCE GQDILALNPG
     VTLLRPESDS EHCIYIAEEG FIQFIVSEED VGAWLHILCD INGKDTLHTI LDRHGVSLEE
     VAKYIQEAIE HNIILIKQKN LPEGAYR
//