ID Q67SU9_SYMTH Unreviewed; 506 AA.
AC Q67SU9;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=asparagine synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012737};
DE EC=6.3.5.4 {ECO:0000256|ARBA:ARBA00012737};
GN OrderedLocusNames=STH259 {ECO:0000313|EMBL:BAD39244.1};
OS Symbiobacterium thermophilum (strain T / IAM 14863).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC Symbiobacterium.
OX NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD39244.1, ECO:0000313|Proteomes:UP000000417};
RN [1] {ECO:0000313|EMBL:BAD39244.1, ECO:0000313|Proteomes:UP000000417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX PubMed=15383646; DOI=10.1093/nar/gkh830;
RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA Ikeda H., Hattori M., Beppu T.;
RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT that depends on microbial commensalism.";
RL Nucleic Acids Res. 32:4937-4944(2004).
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 -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the asparagine synthetase family.
CC {ECO:0000256|ARBA:ARBA00005752}.
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DR EMBL; AP006840; BAD39244.1; -; Genomic_DNA.
DR RefSeq; WP_011194394.1; NC_006177.1.
DR AlphaFoldDB; Q67SU9; -.
DR STRING; 292459.STH259; -.
DR MEROPS; C44.976; -.
DR KEGG; sth:STH259; -.
DR eggNOG; COG0367; Bacteria.
DR HOGENOM; CLU_014658_2_2_9; -.
DR OrthoDB; 9763290at2; -.
DR Proteomes; UP000000417; 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 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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Asparagine biosynthesis {ECO:0000256|ARBA:ARBA00022888};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR001589-
KW 2}; Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR001589-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000000417}.
FT DOMAIN 2..181
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT BINDING 95
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT BINDING 326..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-2"
FT SITE 328
FT /note="Important for beta-aspartyl-AMP intermediate
FT formation"
FT /evidence="ECO:0000256|PIRSR:PIRSR001589-3"
SQ SEQUENCE 506 AA; 55614 MW; 95BC057E7BBE9FAE CRC64;
MSGIAGILGK PDKARIVRML EQQAHRGPDG RGIWTATAGF GLGHVRLATV DVAGGGQPLS
NEDGSLWLAM TGAIYNHGAL RRELEGRHAF RTQSDAEVVV HLFEEYGPAC VERLDGMFAI
AIWGEEVGLF LARDPLGIQP LYWGEDEEGN VLFASEIKAL VGETRFVREF PPGHRWRAGE
PLEPYERLPA HTGELADPDQ IVLALDRLLH AAVRKQLAAD VPVGCLLSGG LDSSLVTAIA
RQHAEGELHT FAVGLEGSAD LEQARMVAGE LGTIHHERVL TEKEVTAVLP RVVDALESCD
PALVRSAVAT YYVAELAAGH VKVVLSGEGA DELFAGYDYL AEFERDAGAL GAELYEITAA
MHNCNLQRVD RMTQVHGVEA RMPFADQAVV DFAFRIHPRL KRRDGESKWI LRRVAEQYLP
PAIVWREKQK FAIGSGIAPL LEHYAAKAVP DAAFRRARSP KGVPFASKEE FLYWSLFRER
YGREDVLALM GRSRSLNQGQ RWVGAL
//
