ID ASNH2_METJA Reviewed; 515 AA. AC Q58456; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 3. DT 27-MAR-2024, entry version 130. DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing] 2; DE EC=6.3.5.4; GN OrderedLocusNames=MJ1056; 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=AAB99058.1; Type=Erroneous initiation; Evidence={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; L77117; AAB99058.1; ALT_INIT; Genomic_DNA. DR PIR; G64431; G64431. DR AlphaFoldDB; Q58456; -. DR SMR; Q58456; -. DR STRING; 243232.MJ_1056; -. DR MEROPS; C44.001; -. DR PaxDb; 243232-MJ_1056; -. DR EnsemblBacteria; AAB99058; AAB99058; MJ_1056. DR KEGG; mja:MJ_1056; -. DR eggNOG; arCOG00071; Archaea. DR HOGENOM; CLU_014658_3_1_2; -. DR InParanoid; Q58456; -. DR PhylomeDB; Q58456; -. 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; 3.60.20.10; 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; PF13522; GATase_6; 1. DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 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 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..515 FT /note="Putative asparagine synthetase [glutamine- FT hydrolyzing] 2" FT /id="PRO_0000056938" FT DOMAIN 2..229 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 92..94 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250" FT BINDING 306 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 378..379 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT SITE 380 FT /note="Important for beta-aspartyl-AMP intermediate FT formation" FT /evidence="ECO:0000250" SQ SEQUENCE 515 AA; 60473 MW; EE9EFBD4E643EDEB CRC64; MCGINGIIRF GKEVIKEEIN KMNKAIKHRG PDDEGIFIYN FKNYSIGLGH VRLAILDLSE KGHQPMGYNV DEDKIIYRDD ELDRADIIIV YNGEIYNYLE LKEKFNLETE TGTDTEVILK LYNKLGFDCV KEFNGMWAFC IFDKKKGLIF CSRDRLGVKP FYYYWDGNEF IFSSELKGIL AVKEINKKEN INKDAVELYF ALGFIPSPYS IYKNTFKLEA RQNLIFDLDK REIRKYYYWE LPDYKPIYDK KKLIEEGKKL LYDAVKIRMR SDVPVGAFLS GGLDSSTVVG VMREFTDLSK LHTFSIGFEG KYDETPYIKI VVDYFKTQHH HYYFKERDFE ELIDKYSWIY DEPFGDYSGF PTYKVSEMAR KFVTVVLSGD GGDEVFGGYM THLNGYRMDF IRKLPKFLRV VGSKLPVKKD LNGIANLYLL KEAFRLSLIN PEEFYAESIK EDAIRPEIYK KWTIEKLRYC LNKGDNKLGE ALRIFDLLFN TLCDNFLVKV DRASMLTLWK LEVHF //