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 01-MAY-2013, entry version 139.
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;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6358221;
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 96604 / S288c / FY1679;
RX PubMed=8641269;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N.,
RA Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H.,
RA Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A.,
RA Hennemann A., Herbert C.J., Heumann K., Hilger F., Hollenberg C.P.,
RA Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L.,
RA Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V.,
RA Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M.,
RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W.,
RA Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M.,
RA Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A.,
RA Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M.,
RA Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX PubMed=2689869;
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
RT Saccharomyces 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.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC -!- COFACTOR: Binds 3 manganese ions per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC carbamoyl 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
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: In eukaryotes this enzyme is synthesized by two
CC pathway-specific (arginine and pyrimidine) under separate control.
CC -!- MISCELLANEOUS: Present with 18000 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
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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 ProteinModelPortal; P03965; -.
DR SMR; P03965; 63-355, 714-904, 964-1085.
DR DIP; DIP-1023N; -.
DR IntAct; P03965; 27.
DR MINT; MINT-639311; -.
DR STRING; 4932.YJR109C; -.
DR PaxDb; P03965; -.
DR PeptideAtlas; P03965; -.
DR PRIDE; P03965; -.
DR EnsemblFungi; YJR109C; YJR109C; YJR109C.
DR GeneID; 853573; -.
DR KEGG; sce:YJR109C; -.
DR KEGG; sce:YJR112W; -.
DR CYGD; YJR109c; -.
DR SGD; S000003870; CPA2.
DR eggNOG; COG0458; -.
DR GeneTree; ENSGT00390000015604; -.
DR HOGENOM; HOG000234583; -.
DR KO; K01955; -.
DR KO; K11562; -.
DR OMA; SSPTAYM; -.
DR OrthoDB; EOG4T7CBC; -.
DR UniPathway; UPA00068; UER00171.
DR NextBio; 974349; -.
DR Genevestigator; P03965; -.
DR GermOnline; YJR109C; Saccharomyces cerevisiae.
DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IMP:SGD.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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; IPR016185; PreATP-grasp_dom.
DR Pfam; PF00289; CPSase_L_chain; 2.
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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1 1118 Carbamoyl-phosphate synthase arginine-
FT specific large chain.
FT /FTId=PRO_0000145091.
FT DOMAIN 154 346 ATP-grasp 1.
FT DOMAIN 698 890 ATP-grasp 2.
FT NP_BIND 174 229 ATP (Potential).
FT NP_BIND 321 371 ATP (Potential).
FT METAL 303 303 Manganese 1 (By similarity).
FT METAL 317 317 Manganese 1 (By similarity).
FT METAL 317 317 Manganese 2 (By similarity).
FT METAL 319 319 Manganese 2 (By similarity).
FT METAL 848 848 Manganese 3 (By similarity).
FT METAL 861 861 Manganese 3 (By similarity).
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
//
