ID A9AB26_METM6 Unreviewed; 513 AA.
AC A9AB26;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 79.
DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing] {ECO:0000256|PIRNR:PIRNR001589};
DE EC=6.3.5.4 {ECO:0000256|PIRNR:PIRNR001589};
GN OrderedLocusNames=MmarC6_1737 {ECO:0000313|EMBL:ABX02549.1};
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158 {ECO:0000313|EMBL:ABX02549.1};
RN [1] {ECO:0000313|EMBL:ABX02549.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 {ECO:0000313|EMBL:ABX02549.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001778,
CC ECO:0000256|PIRNR:PIRNR001589};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR EMBL; CP000867; ABX02549.1; -; Genomic_DNA.
DR AlphaFoldDB; A9AB26; -.
DR STRING; 444158.MmarC6_1737; -.
DR KEGG; mmx:MmarC6_1737; -.
DR eggNOG; arCOG00071; Archaea.
DR HOGENOM; CLU_014658_4_0_2; -.
DR OMA; DWSGIYS; -.
DR OrthoDB; 8692at2157; -.
DR PhylomeDB; A9AB26; -.
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:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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; PTHR11772; ASPARAGINE SYNTHETASE; 1.
DR PANTHER; PTHR11772:SF2; ASPARAGINE SYNTHETASE [GLUTAMINE-HYDROLYZING]; 1.
DR Pfam; PF00733; Asn_synthase; 2.
DR Pfam; PF13537; GATase_7; 1.
DR PIRSF; PIRSF001589; Asn_synthetase_glu-h; 2.
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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRSR:PIRSR001589-1};
KW Asparagine biosynthesis {ECO:0000256|ARBA:ARBA00022888,
KW ECO:0000256|PIRSR:PIRSR001589-1};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001589};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PIRSR:PIRSR001589-1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ABX02549.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001589}.
FT DOMAIN 2..219
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-1"
FT BINDING 123
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 369..370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
SQ SEQUENCE 513 AA; 58756 MW; 44245F13E96F9AFC CRC64;
MCSISGIVAK DEEGSGSRSL LDNIQKHVIN MMKILKHRGP DYSGMMFDDE VLYFENFDDV
VENTETISRM AMGHNRLAIV GTAVQPIPND DESIWIICNG EIYNHIELRD ELSVEHEFKT
DTDSEAIIHA YEDELIDVLD GDYAYAIYDK EKNIIELRRD LIGVKPLYFI DTDEYFAFAS
EKKALHYLLM EINCLDYKSA FNYDISRLNP NSRLTFELDE NSWYIEEELE KVNSNYFEEN
DYELCKNELE TTILDSVLKR VNGLEKVGII YSGGVDSTLI SKLASESCEV ILYSVGSENS
EDLIYAERAA KDMGLNFRKK IISEDEFEEY VVKVARAIDE LDVMKISVGI PILAASEMAR
EDGIKVVLSG QGADELFAGY NRYQRILKEK GEDGLKNSII SDVFDIHKIN LERDDHCTMA
NGVELRVPFL DKFVIDVGLS IPVEYKIEEP RKKILRDIAS KYVPDYIAQR PKKAAQYGSG
SEKMVYAVAK KHGYSKKEIN KFFEEYLLEK IKF
//