ID   CARA_KLULA              Reviewed;         409 AA.
AC   Q6CIQ1;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 110.
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=KLLA0F24882g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382126; CAG98896.1; -; Genomic_DNA.
DR   RefSeq; XP_456188.1; XM_456188.1.
DR   AlphaFoldDB; Q6CIQ1; -.
DR   SMR; Q6CIQ1; -.
DR   STRING; 28985.XP_456188.1; -.
DR   EnsemblFungi; CAG98896; CAG98896; KLLA0_F24882g.
DR   GeneID; 2895188; -.
DR   KEGG; kla:KLLA0_F24882g; -.
DR   eggNOG; KOG0370; Eukaryota.
DR   HOGENOM; CLU_035901_1_1_1; -.
DR   InParanoid; Q6CIQ1; -.
DR   OMA; CFNTGMT; -.
DR   UniPathway; UPA00068; UER00171.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IEA:EnsemblFungi.
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   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:EnsemblFungi.
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..409
FT                   /note="Carbamoyl-phosphate synthase arginine-specific small
FT                   chain"
FT                   /id="PRO_0000290596"
FT   DOMAIN          197..389
FT                   /note="Glutamine amidotransferase type-1"
FT   ACT_SITE        277
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        362
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44921 MW;  B08D9B8A9C973AD8 CRC64;
     MPNFKSTAPK AKFAIYNNSN PDSESGFVEF QGYSFGAPVS CSGEAVFTTS LVGYPESMTD
     PSYKGQILVF TQPLIGNYGV PSGEERDDFN LLKYLESPHI HVRGIVVAEY AWRYSHWTAV
     ESLATWCQRE NVTAIGGIDT RAVVQILREQ GSSPSTITVQ GSFIPKPIKP ETDLVKIVST
     KKPFFVKALS SVKTPFNVAL IDCGVKENII RCLVERGANV TVFPYDYPIT SVANQFDGIF
     ISNGPGDPVQ CMESTVPELK KLLETNTLQD LPIFGICLGH QLLALASGGK TIKLGYGNRA
     HNIPALDLTT GQCHITSQNH GYAVDVDTLP ESGFKPFFQN LNDKSNEGMI HVSRPIFSTQ
     FHPEAKGGPR DSAVLFDRYF DNMSQYRALK GPKVKLTLNT SSLATERVF