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 27-MAR-2024, entry version 211. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 236. 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; 4932-YBR218C; -. DR PeptideAtlas; P32327; -. DR EnsemblFungi; YBR218C_mRNA; YBR218C; YBR218C. DR GeneID; 852519; -. DR KEGG; sce:YBR218C; -. DR AGR; SGD:S000000422; -. 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 OrthoDB; 1129179at2759; -. DR BioCyc; YEAST:YBR218C-MONOMER; -. DR BRENDA; 6.4.1.1; 984. DR UniPathway; UPA00138; -. DR BioGRID-ORCS; 852519; 5 hits in 10 CRISPR screens. 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 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; 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 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 //