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Database: UniProt
Entry: P11154
LinkDB: P11154
Original site: P11154 
ID   PYC1_YEAST              Reviewed;        1178 AA.
AC   P11154; D6VU79;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   13-FEB-2019, entry version 193.
DE   RecName: Full=Pyruvate carboxylase 1;
DE            EC=6.4.1.1;
DE   AltName: Full=Pyruvic carboxylase 1;
DE            Short=PCB 1;
GN   Name=PYC1; Synonyms=PYV; OrderedLocusNames=YGL062W;
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], PARTIAL PROTEIN SEQUENCE, AND
RP   BIOTINYLATION AT LYS-1135.
RX   PubMed=3042770;
RA   Lim F., Morris C.P., Occhiodoro F., Wallace J.C.;
RT   "Sequence and domain structure of yeast pyruvate carboxylase.";
RL   J. Biol. Chem. 263:11493-11497(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9234674;
RX   DOI=10.1002/(SICI)1097-0061(199707)13:9<861::AID-YEA125>3.0.CO;2-9;
RA   Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT   "The characterization of two new clusters of duplicated genes suggests
RT   a 'Lego' organization of the yeast Saccharomyces cerevisiae
RT   chromosomes.";
RL   Yeast 13:861-869(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
RA   Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
RA   Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
RA   Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
RA   Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
RA   Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
RA   Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
RA   Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
RA   Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
RA   Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
RA   Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
RA   Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
RA   Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
RA   Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
RA   Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
RA   Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
RA   Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
RA   Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
RA   Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
RA   van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
RA   Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
RA   Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
RA   Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1003-1178.
RX   PubMed=3036126; DOI=10.1016/0006-291X(87)91334-9;
RA   Morris C.P., Lim F., Wallace J.C.;
RT   "Yeast pyruvate carboxylase: gene isolation.";
RL   Biochem. Biophys. Res. Commun. 145:390-396(1987).
RN   [6]
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   -!- 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   -!- INTERACTION:
CC       P39940:RSP5; NbExp=2; IntAct=EBI-14358, EBI-16219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 12500 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
DR   EMBL; J03889; AAA34843.1; -; Genomic_DNA.
DR   EMBL; Z72584; CAA96765.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08040.1; -; Genomic_DNA.
DR   PIR; S64066; QYBYP.
DR   RefSeq; NP_011453.1; NM_001180927.1.
DR   ProteinModelPortal; P11154; -.
DR   SMR; P11154; -.
DR   BioGrid; 33185; 122.
DR   DIP; DIP-6425N; -.
DR   IntAct; P11154; 17.
DR   MINT; P11154; -.
DR   STRING; 4932.YGL062W; -.
DR   MaxQB; P11154; -.
DR   PaxDb; P11154; -.
DR   PRIDE; P11154; -.
DR   EnsemblFungi; YGL062W_mRNA; YGL062W_mRNA; YGL062W.
DR   GeneID; 852818; -.
DR   KEGG; sce:YGL062W; -.
DR   EuPathDB; FungiDB:YGL062W; -.
DR   SGD; S000003030; PYC1.
DR   GeneTree; ENSGT00900000141164; -.
DR   HOGENOM; HOG000282801; -.
DR   InParanoid; P11154; -.
DR   KO; K01958; -.
DR   OMA; EFVDACN; -.
DR   BioCyc; YEAST:YGL062W-MONOMER; -.
DR   BRENDA; 6.4.1.1; 984.
DR   SABIO-RK; P11154; -.
DR   UniPathway; UPA00138; -.
DR   PRO; PR:P11154; -.
DR   Proteomes; UP000002311; Chromosome VII.
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   ATP-binding; Biotin; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; Gluconeogenesis; Ligase; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome; Zinc.
FT   CHAIN         1   1178       Pyruvate carboxylase 1.
FT                                /FTId=PRO_0000146824.
FT   DOMAIN       18    470       Biotin carboxylation.
FT   DOMAIN      140    337       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      557    824       Pyruvate carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01151}.
FT   DOMAIN     1094   1169       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   REGION      565    569       Substrate binding. {ECO:0000250}.
FT   ACT_SITE    312    312       {ECO:0000250}.
FT   METAL       566    566       Divalent metal cation. {ECO:0000250}.
FT   METAL       734    734       Divalent metal cation; via carbamate
FT                                group. {ECO:0000250}.
FT   METAL       764    764       Divalent metal cation. {ECO:0000250}.
FT   METAL       766    766       Divalent metal cation. {ECO:0000250}.
FT   BINDING     136    136       ATP. {ECO:0000250}.
FT   BINDING     220    220       ATP. {ECO:0000250}.
FT   BINDING     255    255       ATP. {ECO:0000250}.
FT   BINDING     638    638       Substrate. {ECO:0000250}.
FT   BINDING     898    898       Substrate. {ECO:0000250}.
FT   MOD_RES     734    734       N6-carboxylysine. {ECO:0000250}.
FT   MOD_RES    1135   1135       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066,
FT                                ECO:0000269|PubMed:3042770}.
FT   CONFLICT    462    462       T -> G (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    493    493       V -> D (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    595    595       R -> A (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    619    619       E -> Q (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    664    664       G -> S (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    772    772       A -> R (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    879    879       E -> Q (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
FT   CONFLICT    909    909       Q -> K (in Ref. 1; AAA34843).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1178 AA;  130099 MW;  BC7110A8AFB23E04 CRC64;
     MSQRKFAGLR DNFNLLGEKN KILVANRGEI PIRIFRTAHE LSMQTVAIYS HEDRLSTHKQ
     KADEAYVIGE VGQYTPVGAY LAIDEIISIA QKHQVDFIHP GYGFLSENSE FADKVVKAGI
     TWIGPPAEVI DSVGDKVSAR NLAAKANVPT VPGTPGPIET VEEALDFVNE YGYPVIIKAA
     FGGGGRGMRV VREGDDVADA FQRATSEART AFGNGTCFVE RFLDKPKHIE VQLLADNHGN
     VVHLFERDCS VQRRHQKVVE VAPAKTLPRE VRDAILTDAV KLAKECGYRN AGTAEFLVDN
     QNRHYFIEIN PRIQVEHTIT EEITGIDIVA AQIQIAAGAS LPQLGLFQDK ITTRGFAIQC
     RITTEDPAKN FQPDTGRIEV YRSAGGNGVR LDGGNAYAGT IISPHYDSML VKCSCSGSTY
     EIVRRKMIRA LIEFRIRGVK TNIPFLLTLL TNPVFIEGTY WTTFIDDTPQ LFQMVSSQNR
     AQKLLHYLAD VAVNGSSIKG QIGLPKLKSN PSVPHLHDAQ GNVINVTKSA PPSGWRQVLL
     EKGPAEFARQ VRQFNGTLLM DTTWRDAHQS LLATRVRTHD LATIAPTTAH ALAGRFALEC
     WGGATFDVAM RFLHEDPWER LRKLRSLVPN IPFQMLLRGA NGVAYSSLPD NAIDHFVKQA
     KDNGVDIFRV FDALNDLEQL KVGVDAVKKA GGVVEATVCF SGDMLQPGKK YNLDYYLEIA
     EKIVQMGTHI LGIKDMAGTM KPAAAKLLIG SLRAKYPDLP IHVHTHDSAG TAVASMTACA
     LAGADVVDVA INSMSGLTSQ PSINALLASL EGNIDTGINV EHVRELDAYW AEMRLLYSCF
     EADLKGPDPE VYQHEIPGGQ LTNLLFQAQQ LGLGEQWAET KRAYREANYL LGDIVKVTPT
     SKVVGDLAQF MVSNKLTSDD VRRLANSLDF PDSVMDFFEG LIGQPYGGFP EPFRSDVLRN
     KRRKLTCRPG LELEPFDLEK IREDLQNRFG DVDECDVASY NMYPRVYEDF QKMRETYGDL
     SVLPTRSFLS PLETDEEIEV VIEQGKTLII KLQAVGDLNK KTGEREVYFD LNGEMRKIRV
     ADRSQKVETV TKSKADMHDP LHIGAPMAGV IVEVKVHKGS LIKKGQPVAV LSAMKMEMII
     SSPSDGQVKE VFVSDGENVD SSDLLVLLED QVPVETKA
//
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