ASNH2_METJA
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 03-AUG-2022, entry version 123.
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};
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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 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 OMA; IEHSHQP; -.
DR PhylomeDB; Q58456; -.
DR UniPathway; UPA00134; UER00195.
DR Proteomes; UP000000805; 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 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
