PYC1_YEAST
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 03-AUG-2022, entry version 209.
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; 125.
DR DIP; DIP-6425N; -.
DR IntAct; P11154; 18.
DR MINT; P11154; -.
DR STRING; 4932.YGL062W; -.
DR MaxQB; P11154; -.
DR PaxDb; P11154; -.
DR PRIDE; P11154; -.
DR EnsemblFungi; YGL062W_mRNA; YGL062W; YGL062W.
DR GeneID; 852818; -.
DR KEGG; sce:YGL062W; -.
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 BioCyc; YEAST:YGL062W-MON; -.
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 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 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; 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
