PYC2_YEAST
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 03-AUG-2022, entry version 204.
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; Saccharomycetes;
OC 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 carboxylase-
RT 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., Wallace J.C.;
RT "Polymorphism of the yeast pyruvate carboxylase 2 gene and protein: effects
RT 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; DOI=10.1002/j.1460-2075.1994.tb06923.x;
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., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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., Dephoure N.,
RA 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 SPECTROMETRY
RP [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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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 -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: By glucose.
CC -!- MISCELLANEOUS: Present with 17000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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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 AlphaFoldDB; P32327; -.
DR SMR; P32327; -.
DR BioGRID; 32915; 226.
DR DIP; DIP-6426N; -.
DR IntAct; P32327; 10.
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; YBR218C.
DR GeneID; 852519; -.
DR KEGG; sce:YBR218C; -.
DR SGD; S000000422; PYC2.
DR VEuPathDB; FungiDB:YBR218C; -.
DR eggNOG; KOG0369; Eukaryota.
DR GeneTree; ENSGT00900000141164; -.
DR HOGENOM; CLU_000395_0_1_1; -.
DR InParanoid; P32327; -.
DR OMA; YAIQSRV; -.
DR BioCyc; YEAST:YBR218C-MON; -.
DR BRENDA; 6.4.1.1; 984.
DR UniPathway; UPA00138; -.
DR PRO; PR:P32327; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32327; 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 Acetylation; ATP-binding; Biotin; Cytoplasm; Gluconeogenesis; Ligase;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1180
FT /note="Pyruvate carboxylase 2"
FT /id="PRO_0000146825"
FT DOMAIN 19..471
FT /note="Biotin carboxylation"
FT DOMAIN 141..338
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 558..825
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT DOMAIN 1095..1170
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 313
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 566..570
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 639
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 735
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /note="via carbamate group"
FT /evidence="ECO:0000250"
FT BINDING 765
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 767
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250"
FT BINDING 899
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 735
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 1136
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 15
FT /note="S -> C (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="D -> E (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> K (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="L -> F (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="S -> C (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 642
FT /note="N -> T (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 771..773
FT /note="GTA -> STR (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="W -> R (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 839
FT /note="S -> P (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1001
FT /note="Y -> N (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="K -> R (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1178
FT /note="Q -> P (in Ref. 1; CAA42544)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="K -> KVIFTR (in Ref. 1; CAA42544)"
FT /evidence="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
