CARB_YEAST
ID CARB_YEAST Reviewed; 1118 AA.
AC P03965; D6VWS8;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-1986, sequence version 1.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE EC=6.3.5.5;
DE AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, ammonia chain;
GN Name=CPA2; OrderedLocusNames=YJR109C; ORFNames=J2002;
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=6358221; DOI=10.1016/s0021-9258(17)43886-5;
RA Lusty C.J., Widgren E.E., Broglie K.E., Nyunoya H.;
RT "Yeast carbamyl phosphate synthetase. Structure of the yeast gene and
RT homology to Escherichia coli carbamyl phosphate synthetase.";
RL J. Biol. Chem. 258:14466-14477(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2689869; DOI=10.1128/mcb.9.11.4882-4888.1989;
RA Kinney D.M., Lusty C.J.;
RT "Arginine restriction induced by delta-N-(phosphonacetyl)-L-ornithine
RT signals increased expression of HIS3, TRP5, CPA1, and CPA2 in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 9:4882-4888(1989).
RN [5]
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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mn(2+) ions per subunit. {ECO:0000250};
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 18000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; K01178; AAA66902.1; -; Genomic_DNA.
DR EMBL; Z49609; CAA89639.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08894.1; -; Genomic_DNA.
DR PIR; A01199; SYBYCP.
DR RefSeq; NP_012643.3; NM_001181767.3.
DR AlphaFoldDB; P03965; -.
DR SMR; P03965; -.
DR BioGRID; 33865; 53.
DR ComplexPortal; CPX-579; Carbamoyl-phosphate synthase arginine-specific.
DR DIP; DIP-1023N; -.
DR IntAct; P03965; 34.
DR MINT; P03965; -.
DR STRING; 4932.YJR109C; -.
DR CarbonylDB; P03965; -.
DR iPTMnet; P03965; -.
DR MaxQB; P03965; -.
DR PaxDb; P03965; -.
DR PRIDE; P03965; -.
DR EnsemblFungi; YJR109C_mRNA; YJR109C; YJR109C.
DR GeneID; 853573; -.
DR KEGG; sce:YJR109C; -.
DR SGD; S000003870; CPA2.
DR VEuPathDB; FungiDB:YJR109C; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_3_1; -.
DR InParanoid; P03965; -.
DR OMA; IEPAGIH; -.
DR BioCyc; MetaCyc:YJR109C-MON; -.
DR BioCyc; YEAST:YJR109C-MON; -.
DR Reactome; R-SCE-500753; Pyrimidine biosynthesis.
DR UniPathway; UPA00068; UER00171.
DR PRO; PR:P03965; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P03965; protein.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; 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:0004151; F:dihydroorotase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR GO; GO:0006526; P:arginine biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IDA:ComplexPortal.
DR GO; GO:0006228; P:UTP biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.1380; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; SSF48108; 1.
DR SUPFAM; SSF52335; SSF52335; 1.
DR SUPFAM; SSF52440; SSF52440; 2.
DR TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Cytoplasm;
KW Ligase; Manganese; Metal-binding; Nucleotide-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..1118
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000145091"
FT DOMAIN 154..346
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 698..890
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 960..1118
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT BINDING 174..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 303
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 319
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 321..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 848
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 861
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1118 AA; 123915 MW; 887FAAE00AC07674 CRC64;
MTSIYTSTEP TNSAFTTEDY KPQLVEGVNS VLVIGSGGLS IGQAGEFDYS GSQAIKALKE
DNKFTILVNP NIATNQTSHS LADKIYYLPV TPEYITYIIE LERPDAILLT FGGQTGLNCG
VALDESGVLA KYNVKVLGTP IKTLITSEDR DLFASALKDI NIPIAESFAC ETVDEALEAA
ERVKYPVIVR SAYALGGLGS GFANNASEMK ELAAQSLSLA PQILVEKSLK GWKEVEYEVV
RDRVGNCITV CNMENFDPLG VHTGDSMVFA PSQTLSDEEF HMLRSAAIKI IRHLGVIGEC
NVQYALQPDG LDYRVIEVNA RLSRSSALAS KATGYPLAYT AAKIGLGYTL PELPNPITKT
TVANFEPSLD YIVAKIPKWD LSKFQYVDRS IGSSMKSVGE VMAIGRNYEE AFQKALRQVD
PSLLGFQGST EFGDQLDEAL RTPTDRRVLA IGQALIHENY TVERVNELSK IDKWFLYKCM
NIVNIYKELE SVKSLSDLSK DLLQRAKKLG FSDKQIAVTI NKHASTNINE LEIRSLRKTL
GIIPFVKRID TLAAEFPAQT NYLYTTYNAT KNDVEFNENG MLVLGSGVYR IGSSVEFDWC
AVNTAKTLRD QGKKTIMINY NPETVSTDFD EVDRLYFEEL SYERVMDIYE LEQSEGCIIS
VGGQLPQNIA LKLYDNGCNI MGTNPNDIDR AENRHKFSSI LDSIDVDQPE WSELTSVEEA
KLFASKVNYP VLIRPSYVLS GAAMSVVNNE EELKAKLTLA SDVSPDHPVV MSKFIEGAQE
IDVDAVAYNG NVLVHAISEH VENAGVHSGD ASLVLPPQHL SDDVKIALKD IADKVAKAWK
ITGPFNMQII KDGEHTLKVI ECNIRASRSF PFVSKVLGVN FIEIAVKAFL GGDIVPKPVD
LMLNKKYDYV ATKVPQFSFT RLAGADPFLG VEMASTGEVA SFGRDLIESY WTAIQSTMNF
HVPLPPSGIL FGGDTSREYL GQVASIVATI GYRIYTTNET TKTYLQEHIK EKNAKVSLIK
FPKNDKRKLR ELFQEYDIKA VFNLASKRAE STDDVDYIMR RNAIDFAIPL FNEPQTALLF
AKCLKAKIAE KIKILESHDV IVPPEVRSWD EFIGFKAY
