CARA_YEAST
ID CARA_YEAST Reviewed; 411 AA.
AC P07258; D6W302;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 192.
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=YOR303W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3881260; DOI=10.1111/j.1432-1033.1985.tb08663.x;
RA Werner M., Feller A., Pierard A.;
RT "Nucleotide sequence of yeast gene CP A1 encoding the small subunit of
RT arginine-pathway carbamoyl-phosphate synthetase. Homology of the deduced
RT amino acid sequence to other glutamine amidotransferases.";
RL Eur. J. Biochem. 146:371-381(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6086650; DOI=10.1016/s0021-9258(17)42769-4;
RA Nyunoya H., Lusty C.J.;
RT "Sequence of the small subunit of yeast carbamyl phosphate synthetase and
RT identification of its catalytic domain.";
RL J. Biol. Chem. 259:9790-9798(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RX PubMed=3555844; DOI=10.1016/0092-8674(87)90618-0;
RA Werner M., Feller A., Messenguy F., Pierard A.;
RT "The leader peptide of yeast gene CPA1 is essential for the translational
RT repression of its expression.";
RL Cell 49:805-813(1987).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two pathway-
CC specific (arginine and pyrimidine) under separate control.
CC -!- MISCELLANEOUS: Present with 2580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR EMBL; X01764; CAA25905.1; -; Genomic_DNA.
DR EMBL; K02132; AAA34525.1; -; Genomic_DNA.
DR EMBL; Z75211; CAA99621.1; -; Genomic_DNA.
DR EMBL; M16690; AAA34527.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11068.1; -; Genomic_DNA.
DR PIR; S67207; SYBYCS.
DR RefSeq; NP_014947.3; NM_001183722.3.
DR AlphaFoldDB; P07258; -.
DR SMR; P07258; -.
DR BioGRID; 34691; 32.
DR ComplexPortal; CPX-579; Carbamoyl-phosphate synthase arginine-specific.
DR DIP; DIP-1024N; -.
DR IntAct; P07258; 5.
DR MINT; P07258; -.
DR STRING; 4932.YOR303W; -.
DR MaxQB; P07258; -.
DR PaxDb; P07258; -.
DR PRIDE; P07258; -.
DR EnsemblFungi; YOR303W_mRNA; YOR303W; YOR303W.
DR GeneID; 854479; -.
DR KEGG; sce:YOR303W; -.
DR SGD; S000005829; CPA1.
DR VEuPathDB; FungiDB:YOR303W; -.
DR eggNOG; KOG0370; Eukaryota.
DR GeneTree; ENSGT00940000157241; -.
DR HOGENOM; CLU_035901_1_1_1; -.
DR InParanoid; P07258; -.
DR OMA; CFNTGMT; -.
DR BioCyc; MetaCyc:YOR303W-MON; -.
DR BioCyc; YEAST:YOR303W-MON; -.
DR UniPathway; UPA00068; UER00171.
DR PRO; PR:P07258; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P07258; protein.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD.
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; IDA:ComplexPortal.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..411
FT /note="Carbamoyl-phosphate synthase arginine-specific small
FT chain"
FT /id="PRO_0000112372"
FT DOMAIN 185..376
FT /note="Glutamine amidotransferase type-1"
FT ACT_SITE 264
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 349
FT /evidence="ECO:0000250"
FT ACT_SITE 351
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 45362 MW; 0793442274770614 CRC64;
MSSAATKATF CIQNGPSFEG ISFGANKSVA GETVFTTSLV GYPESMTDPS YRGQILVFTQ
PLIGNYGVPS GEARDEYNLL KYFESPHIHV VGIVVAEYAY QYSHWTAVES LAQWCQREGV
AAITGVDTRE LVQYLREQGS SLGRITLADH DPVPYVNPMK TNLVAQVTTK KPFHVSALPG
KAKANVALID CGVKENIIRC LVKRGANVTV FPYDYRIQDV ASEFDGIFLS NGPGNPELCQ
ATISNVRELL NNPVYDCIPI FGICLGHQLL ALASGASTHK LKYGNRAHNI PAMDLTTGQC
HITSQNHGYA VDPETLPKDQ WKPYFVNLND KSNEGMIHLQ RPIFSTQFHP EAKGGPLDTA
ILFDKFFDNI EKYQLQSQAK SSISLKVTYS TDKSRLQSIN VTKLAKERVL F
