ASNH_BACSU
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 03-AUG-2022, entry version 139.
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; Firmicutes; 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}.
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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; P42113; -.
DR PRIDE; P42113; -.
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 OMA; YANNIPP; -.
DR PhylomeDB; P42113; -.
DR BioCyc; BSUB:BSU39920-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 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..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
