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Database: UniProt
Entry: A9AB26_METM6
LinkDB: A9AB26_METM6
Original site: A9AB26_METM6 
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
//
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