ID D3S6T9_METSF Unreviewed; 507 AA.
AC D3S6T9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing] {ECO:0000256|PIRNR:PIRNR001589};
DE EC=6.3.5.4 {ECO:0000256|PIRNR:PIRNR001589};
GN OrderedLocusNames=MFS40622_0048 {ECO:0000313|EMBL:ADC68749.1};
OS Methanocaldococcus sp. (strain FS406-22).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=644281 {ECO:0000313|EMBL:ADC68749.1, ECO:0000313|Proteomes:UP000002189};
RN [1] {ECO:0000313|EMBL:ADC68749.1, ECO:0000313|Proteomes:UP000002189}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS406-22 {ECO:0000313|EMBL:ADC68749.1,
RC ECO:0000313|Proteomes:UP000002189};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Leigh J.,
RA Whitman W.B., Woyke T.;
RT "Complete sequence of chromosome of Methanocaldococcus sp. FS406-22.";
RL Submitted (FEB-2010) 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; CP001901; ADC68749.1; -; Genomic_DNA.
DR RefSeq; WP_012979664.1; NC_013887.1.
DR AlphaFoldDB; D3S6T9; -.
DR STRING; 644281.MFS40622_0048; -.
DR MEROPS; C44.001; -.
DR GeneID; 8803882; -.
DR KEGG; mfs:MFS40622_0048; -.
DR eggNOG; arCOG00071; Archaea.
DR HOGENOM; CLU_014658_4_0_2; -.
DR OrthoDB; 8692at2157; -.
DR Proteomes; UP000002189; 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: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}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001589}.
FT DOMAIN 2..214
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 117
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 364..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
SQ SEQUENCE 507 AA; 58844 MW; 1C622C3182C08227 CRC64;
MCSISGIIVK ESQIPAKYAI DMMKILKHRG RDNSGLLLDD EVIYFNNFED VEDLEEEEMI
GNLNLAHNRL AIVGRYGVQP IPNEDEDIWL VCNGEIYNYI ELREYLKENH EFRTDSDNEV
IIHLYEDEQL EELDGDYAFA IYDKSKDIVL LGRDVFGVKP LFYVDTPNYF AFASERKALW
HLLINIDGYE RDLDVLNSKI KTLKPNSQLI YYLDDNKFDI IENFKKMELN YMKERSYEEA
KEYLDRALKN AVLKRVRGLD RVGIICSGGV DSSLIAKLSS LYCEVILYAV GTENSEDLIY
AERLAKDLNL KIRKKIISEE EYERYVFKVA KAIDEVDLMK IGVGIPIYVA SEMANEDGLK
VVLSGQGADE LFGGYARHER IYREKGEEEL KKELLKDVYN LYKVNLERDD HCTMANGVEL
RVPFLDEEVV EIALSIPIEY KMSELRKRIL RDVASQYLPD YIAYRPKKAA QYGSGGEKMI
YKVAKKYGFS KKKINEFLDM LKRKIVE
//
