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   27-MAR-2024, entry version 215.
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; Saccharomycetes;
OC   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; DOI=10.1016/s0021-9258(18)37984-5;
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 a
RT   'Lego' organization of the yeast Saccharomyces cerevisiae 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., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., 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., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., 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   -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC       the ATP-dependent carboxylation of the covalently attached biotin in
CC       the first step and the transfer of the carboxyl group to pyruvate in
CC       the second.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) + oxaloacetate
CC         + phosphate; Xref=Rhea:RHEA:20844, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, 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       P11154; 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}.
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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   AlphaFoldDB; P11154; -.
DR   SMR; P11154; -.
DR   BioGRID; 33185; 136.
DR   DIP; DIP-6425N; -.
DR   IntAct; P11154; 18.
DR   MINT; P11154; -.
DR   STRING; 4932.YGL062W; -.
DR   MaxQB; P11154; -.
DR   PaxDb; 4932-YGL062W; -.
DR   PeptideAtlas; P11154; -.
DR   EnsemblFungi; YGL062W_mRNA; YGL062W; YGL062W.
DR   GeneID; 852818; -.
DR   KEGG; sce:YGL062W; -.
DR   AGR; SGD:S000003030; -.
DR   SGD; S000003030; PYC1.
DR   VEuPathDB; FungiDB:YGL062W; -.
DR   eggNOG; KOG0369; Eukaryota.
DR   GeneTree; ENSGT00900000141164; -.
DR   HOGENOM; CLU_000395_0_1_1; -.
DR   InParanoid; P11154; -.
DR   OMA; GQHVFIE; -.
DR   OrthoDB; 1129179at2759; -.
DR   BioCyc; YEAST:YGL062W-MONOMER; -.
DR   BRENDA; 6.4.1.1; 984.
DR   Reactome; R-SCE-196780; Biotin transport and metabolism.
DR   Reactome; R-SCE-70263; Gluconeogenesis.
DR   SABIO-RK; P11154; -.
DR   UniPathway; UPA00138; -.
DR   BioGRID-ORCS; 852818; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P11154; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P11154; Protein.
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: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   CDD; cd06850; biotinyl_domain; 1.
DR   CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 1.10.472.90; Conserved carboxylase domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 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   NCBIfam; TIGR01235; pyruv_carbox; 1.
DR   PANTHER; PTHR43778; PYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR43778:SF2; PYRUVATE CARBOXYLASE, MITOCHONDRIAL; 1.
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; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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; Cytoplasm; Direct protein sequencing; Gluconeogenesis;
KW   Ligase; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..1178
FT                   /note="Pyruvate carboxylase 1"
FT                   /id="PRO_0000146824"
FT   DOMAIN          18..470
FT                   /note="Biotin carboxylation"
FT   DOMAIN          140..337
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          557..824
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   DOMAIN          1094..1169
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         255
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         565..569
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         566
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         638
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         734
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000250"
FT   BINDING         764
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         766
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         898
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         734
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1135
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066,
FT                   ECO:0000269|PubMed:3042770"
FT   CONFLICT        462
FT                   /note="T -> G (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493
FT                   /note="V -> D (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595
FT                   /note="R -> A (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        619
FT                   /note="E -> Q (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        664
FT                   /note="G -> S (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        772
FT                   /note="A -> R (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        879
FT                   /note="E -> Q (in Ref. 1; AAA34843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        909
FT                   /note="Q -> K (in Ref. 1; AAA34843)"
FT                   /evidence="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
//