CARA_YARLI
ID CARA_YARLI Reviewed; 448 AA.
AC Q6C9Y4;
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=YALI0D07370g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382130; CAG80716.1; -; Genomic_DNA.
DR RefSeq; XP_502528.1; XM_502528.1.
DR AlphaFoldDB; Q6C9Y4; -.
DR SMR; Q6C9Y4; -.
DR STRING; 4952.CAG80716; -.
DR EnsemblFungi; CAG80716; CAG80716; YALI0_D07370g.
DR GeneID; 2910891; -.
DR KEGG; yli:YALI0D07370g; -.
DR VEuPathDB; FungiDB:YALI0_D07370g; -.
DR HOGENOM; CLU_035901_1_0_1; -.
DR InParanoid; Q6C9Y4; -.
DR OMA; CFNTGMT; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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; ANK repeat; Arginine biosynthesis; ATP-binding;
KW Cytoplasm; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..448
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000290600"
FT REPEAT 218..249
FT /note="ANK"
FT DOMAIN 224..415
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 388
FT /evidence="ECO:0000250"
FT ACT_SITE 390
FT /evidence="ECO:0000250"
SQ SEQUENCE 448 AA; 48911 MW; B70B9F222EDA60F0 CRC64;
MFKNIARLAS MARSAPRTTA SFQTRFMATT ASGTASASAT PATFTLQNGP VFTGRSFGAN
RVVSGEAVFS TGMVGYPESM TDPSYRGQIL VFTQPLIGNY GVPSGKETDP FGLIKYFESP
HIQCIGIVVA DAALKYSHWT AVESLGEWCK REGVAAISGV DTRAIVTYLR EQGSSLGRIT
VGEEYDAEED AAFVDPGEIN LVRRVSTKQP FHVSAAADVE NPLHIAVIDC GVKENILRSL
VSRGASITVF PYEYPINDIA HHFDGIFISN GPGDPTHCQQ TVLNLRDIMY EKPELSELPI
FGICLGHQLL ALAAGAKTVK LKYGNRAHNI PALDLTTGQC HITSQNHGYA VDVNTLPAEF
KPYFINLNDQ SNEGMIHTEK PIFSTQFHPE AKGGPLDTSI LFDKYLGQVH QYRAARKSGV
DTRPNKLLVD LLPKQRIGVE IDAWDYVQ
