ASNH1_METJA
ID ASNH1_METJA Reviewed; 541 AA.
AC Q58516;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing] 1;
DE EC=6.3.5.4;
GN OrderedLocusNames=MJ1116;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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=AAB99117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB99117.1; ALT_INIT; Genomic_DNA.
DR PIR; C64439; C64439.
DR RefSeq; WP_064496729.1; NC_000909.1.
DR AlphaFoldDB; Q58516; -.
DR SMR; Q58516; -.
DR STRING; 243232.MJ_1116; -.
DR MEROPS; C44.001; -.
DR PRIDE; Q58516; -.
DR DNASU; 1452012; -.
DR EnsemblBacteria; AAB99117; AAB99117; MJ_1116.
DR GeneID; 1452012; -.
DR KEGG; mja:MJ_1116; -.
DR eggNOG; arCOG00071; Archaea.
DR HOGENOM; CLU_014658_4_0_2; -.
DR InParanoid; Q58516; -.
DR OMA; DWSGIYS; -.
DR OrthoDB; 12911at2157; -.
DR PhylomeDB; Q58516; -.
DR UniPathway; UPA00134; UER00195.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central.
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 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 3: Inferred from homology;
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..541
FT /note="Putative asparagine synthetase [glutamine-
FT hydrolyzing] 1"
FT /id="PRO_0000056937"
FT DOMAIN 2..213
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 68..72
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 92..94
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 363..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 541 AA; 62655 MW; 9B3FA64E39A957BB CRC64;
MCSISGIIVK DNQISAKYSI DMMKILKHRG RDNSGLLLDD EVIYFNDFED VEDLEEEMIG
NLSLAHNRLA IVGRYGVQPI PNEDETIWLV CNGEIYNYIE LREYLKQNHE FRTDSDNEVI
IHLYEEEKLE ELDGDYAFAI YDKSKNVVRL ARDMFGVKPL FYVDRDKYFA FASERKALWH
LLINIDGCER DLDELNSKIK TLKPNSQLIY YLDDNRFEII EGFKKLELNY MKERSYEEAK
EYLDRALKNS VLKRVRGLDK VGIICSGGVD SSLIAKLASL YCEVILYAVG TENSEDLIYA
ERLAKDLNLK LRKKIISEEE YEEYVFKVAK AIDEVDLMKI GVGIPIYVAS EMANEDGLKV
VLSGQGADEL FGGYARHERI YRERGEEELK KELLKDVYNL YKVNLERDDH CTMANGVELR
VPFLDEEVVE IALSIPIEYK MSELSNRPYA ESNISLKSEP INGLKNTNLN IKCVRSVRKK
ILRDVASQYL PDYIAYRPKK AAQYGSGGEK MIYKVAKKYG FSKKRINEFL DMLKRKIVSE
F
