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Database: UniProt
Entry: P32327
LinkDB: P32327
Original site: P32327 
ID   PYC2_YEAST              Reviewed;        1180 AA.
AC   P32327; D6VQL4;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   13-FEB-2019, entry version 188.
DE   RecName: Full=Pyruvate carboxylase 2;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase 2;
DE            Short=PCB 2;
GN   Name=PYC2; OrderedLocusNames=YBR218C; ORFNames=YBR1507;
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], AND CHARACTERIZATION.
RX   PubMed=1921979; DOI=10.1007/BF00272171;
RA   Stucka R., Dequin S., Salmon J.-M., Gancedo C.;
RT   "DNA sequences in chromosomes II and VII code for pyruvate carboxylase
RT   isoenzymes in Saccharomyces cerevisiae: analysis of pyruvate
RT   carboxylase-deficient strains.";
RL   Mol. Gen. Genet. 229:307-315(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8554526; DOI=10.1042/bj3120817;
RA   Val D.L., Chapman-Smith A., Walker M.E., Cronan J.E. Jr.,
RA   Wallace J.C.;
RT   "Polymorphism of the yeast pyruvate carboxylase 2 gene and protein:
RT   effects on protein biotinylation.";
RL   Biochem. J. 312:817-825(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
RA   Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
RA   Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
RA   Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
RA   Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
RA   Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
RA   Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
RA   Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
RA   Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
RA   Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
RA   Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
RA   van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
RA   Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
RA   Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
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).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction,
CC       involving the ATP-dependent carboxylation of the covalently
CC       attached biotin in the first step and the transfer of the carboxyl
CC       group to pyruvate in the second.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By glucose.
CC   -!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
DR   EMBL; X59890; CAA42544.1; -; Genomic_DNA.
DR   EMBL; U35647; AAC49147.1; -; Genomic_DNA.
DR   EMBL; Z36087; CAA85182.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07334.1; -; Genomic_DNA.
DR   PIR; S46094; S46094.
DR   RefSeq; NP_009777.1; NM_001178566.1.
DR   ProteinModelPortal; P32327; -.
DR   SMR; P32327; -.
DR   BioGrid; 32915; 220.
DR   DIP; DIP-6426N; -.
DR   IntAct; P32327; 9.
DR   MINT; P32327; -.
DR   STRING; 4932.YBR218C; -.
DR   CarbonylDB; P32327; -.
DR   iPTMnet; P32327; -.
DR   MaxQB; P32327; -.
DR   PaxDb; P32327; -.
DR   PRIDE; P32327; -.
DR   EnsemblFungi; YBR218C_mRNA; YBR218C_mRNA; YBR218C.
DR   GeneID; 852519; -.
DR   KEGG; sce:YBR218C; -.
DR   EuPathDB; FungiDB:YBR218C; -.
DR   SGD; S000000422; PYC2.
DR   GeneTree; ENSGT00900000141164; -.
DR   HOGENOM; HOG000282801; -.
DR   InParanoid; P32327; -.
DR   KO; K01958; -.
DR   OMA; GQPHGGF; -.
DR   BioCyc; YEAST:YBR218C-MONOMER; -.
DR   BRENDA; 6.4.1.1; 984.
DR   Reactome; R-SCE-196780; Biotin transport and metabolism.
DR   Reactome; R-SCE-70263; Gluconeogenesis.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:P32327; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IMP:SGD.
DR   GO; GO:0006094; P:gluconeogenesis; IMP:SGD.
DR   GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Biotin; Complete proteome; Cytoplasm;
KW   Gluconeogenesis; Ligase; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Reference proteome; Zinc.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
FT   CHAIN         2   1180       Pyruvate carboxylase 2.
FT                                /FTId=PRO_0000146825.
FT   DOMAIN       19    471       Biotin carboxylation.
FT   DOMAIN      141    338       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      558    825       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1095   1170       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      566    570       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    313    313       {ECO:0000250}.
FT   METAL       567    567       Divalent metal cation. {ECO:0000250}.
FT   METAL       735    735       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       765    765       Divalent metal cation. {ECO:0000250}.
FT   METAL       767    767       Divalent metal cation. {ECO:0000250}.
FT   BINDING     137    137       ATP. {ECO:0000250}.
FT   BINDING     221    221       ATP. {ECO:0000250}.
FT   BINDING     256    256       ATP. {ECO:0000250}.
FT   BINDING     639    639       Substrate. {ECO:0000250}.
FT   BINDING     899    899       Substrate. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   MOD_RES     735    735       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1136   1136       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
FT   CONFLICT     15     15       S -> C (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    132    132       D -> E (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    238    238       N -> K (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    268    268       L -> F (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    546    546       S -> C (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    642    642       N -> T (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    771    773       GTA -> STR (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    831    831       W -> R (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT    839    839       S -> P (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT   1001   1001       Y -> N (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT   1155   1155       K -> R (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT   1178   1178       Q -> P (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
FT   CONFLICT   1180   1180       K -> KVIFTR (in Ref. 1; CAA42544).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1180 AA;  130167 MW;  AD60DA3A60F5E001 CRC64;
     MSSSKKLAGL RDNFSLLGEK NKILVANRGE IPIRIFRSAH ELSMRTIAIY SHEDRLSMHR
     LKADEAYVIG EEGQYTPVGA YLAMDEIIEI AKKHKVDFIH PGYGFLSENS EFADKVVKAG
     ITWIGPPAEV IDSVGDKVSA RHLAARANVP TVPGTPGPIE TVQEALDFVN EYGYPVIIKA
     AFGGGGRGMR VVREGDDVAD AFQRATSEAR TAFGNGTCFV ERFLDKPKHI EVQLLADNHG
     NVVHLFERDC SVQRRHQKVV EVAPAKTLPR EVRDAILTDA VKLAKVCGYR NAGTAEFLVD
     NQNRHYFIEI NPRIQVEHTI TEEITGIDIV SAQIQIAAGA TLTQLGLLQD KITTRGFSIQ
     CRITTEDPSK NFQPDTGRLE VYRSAGGNGV RLDGGNAYAG ATISPHYDSM LVKCSCSGST
     YEIVRRKMIR ALIEFRIRGV KTNIPFLLTL LTNPVFIEGT YWTTFIDDTP QLFQMVSSQN
     RAQKLLHYLA DLAVNGSSIK GQIGLPKLKS NPSVPHLHDA QGNVINVTKS APPSGWRQVL
     LEKGPSEFAK QVRQFNGTLL MDTTWRDAHQ SLLATRVRTH DLATIAPTTA HALAGAFALE
     CWGGATFDVA MRFLHEDPWE RLRKLRSLVP NIPFQMLLRG ANGVAYSSLP DNAIDHFVKQ
     AKDNGVDIFR VFDALNDLEQ LKVGVNAVKK AGGVVEATVC YSGDMLQPGK KYNLDYYLEV
     VEKIVQMGTH ILGIKDMAGT MKPAAAKLLI GSLRTRYPDL PIHVHSHDSA GTAVASMTAC
     ALAGADVVDV AINSMSGLTS QPSINALLAS LEGNIDTGIN VEHVRELDAY WAEMRLLYSC
     FEADLKGPDP EVYQHEIPGG QLTNLLFQAQ QLGLGEQWAE TKRAYREANY LLGDIVKVTP
     TSKVVGDLAQ FMVSNKLTSD DIRRLANSLD FPDSVMDFFE GLIGQPYGGF PEPLRSDVLR
     NKRRKLTCRP GLELEPFDLE KIREDLQNRF GDIDECDVAS YNMYPRVYED FQKIRETYGD
     LSVLPTKNFL APAEPDEEIE VTIEQGKTLI IKLQAVGDLN KKTGQREVYF ELNGELRKIR
     VADKSQNIQS VAKPKADVHD THQIGAPMAG VIIEVKVHKG SLVKKGESIA VLSAMKMEMV
     VSSPADGQVK DVFIKDGESV DASDLLVVLE EETLPPSQKK
//
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