CARA_DEBHA
ID CARA_DEBHA Reviewed; 429 AA.
AC Q6BJG4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain;
DE Short=CPS-A;
DE EC=6.3.5.5;
DE AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain;
GN Name=CPA1; OrderedLocusNames=DEHA2G02618g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR EMBL; CR382139; CAG90105.1; -; Genomic_DNA.
DR RefSeq; XP_461657.1; XM_461657.1.
DR AlphaFoldDB; Q6BJG4; -.
DR SMR; Q6BJG4; -.
DR STRING; 4959.XP_461657.1; -.
DR EnsemblFungi; CAG90105; CAG90105; DEHA2G02618g.
DR GeneID; 2904523; -.
DR KEGG; dha:DEHA2G02618g; -.
DR VEuPathDB; FungiDB:DEHA2G02618g; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_035901_1_0_1; -.
DR InParanoid; Q6BJG4; -.
DR OMA; CFNTGMT; -.
DR OrthoDB; 566537at2759; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; -; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; SSF52021; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Glutamine amidotransferase; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..429
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000290594"
FT DOMAIN 218..406
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 295
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 379
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 47132 MW; 5B8B9DDEE57A3C18 CRC64;
MIRVIQPPLI ASKQLFRRYL ATGGTFTNKT SQLDRATLTI KDGPVFSGYS FGANKNISGE
AVFTTSLVGY PESMTDPSYK GQILCFTQPL IGNYGVPSST LKDEFNLLKH MESPSVQCIG
IVVADVALEY SHWTAVESLQ QWCQRSGVAA ISGVDTRQLV SYLREKGSSL AKITIGEEYD
ADEDAAFEDP GSVNLVHKVS TKAPFHISCP EKYAKGLHIA VLDCGAKENI LRCLVERGAS
LTVFPYNYPI DKIANKFDGI FISNGPGDPT HCSSTTENLA KTMEKYHDLP IFGICLGHQL
LALASGARTI KMKYGNRAHN IPALDLTTGK CHITSQNHGY SVDAETLDSD WEPYFTNLND
LSNEGMKHKS RPIFSTQFHP EAKGGPLDTA FLFDKFFENI EQYRATNGLN LGNVDDSLLV
DILPKGRVL
