ID A8Y4B9_CAEBR Unreviewed; 1166 AA. AC A8Y4B9; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 16-DEC-2008, sequence version 2. DT 26-FEB-2020, entry version 88. DE RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594}; DE EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594}; GN Name=pyc-1 {ECO:0000313|WormBase:CBG23262}; GN Synonyms=Cbr-pyc-1 {ECO:0000313|EMBL:CAP39739.2}; GN ORFNames=CBG23262 {ECO:0000313|WormBase:CBG23262}, CBG_23262 GN {ECO:0000313|EMBL:CAP39739.2}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP39739.2, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP39739.2, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP39739.2, RC ECO:0000313|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). CC -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent CC carboxylation of the covalently attached biotin in the first step and CC the transfer of the carboxyl group to pyruvate in the second. CC {ECO:0000256|PIRNR:PIRNR001594}. 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 Evidence={ECO:0000256|PIRNR:PIRNR001594}; CC -!- COFACTOR: CC Name=biotin; Xref=ChEBI:CHEBI:57586; CC Evidence={ECO:0000256|PIRNR:PIRNR001594, CC ECO:0000256|SAAS:SAAS00197451}; 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; HE601533; CAP39739.2; -; Genomic_DNA. DR STRING; 6238.CBG23262; -. DR WormBase; CBG23262; CBP05523; WBGene00041648; Cbr-pyc-1. DR eggNOG; ENOG410IU5D; Eukaryota. DR eggNOG; COG1038; LUCA. DR HOGENOM; CLU_000395_0_1_1; -. DR InParanoid; A8Y4B9; -. DR OMA; YAIQSRV; -. DR OrthoDB; 254436at2759; -. DR Proteomes; UP000008549; Chromosome V. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. 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; 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; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00867; CPSASE_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|PIRSR:PIRSR001594- KW 2, ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00234148}; KW Biotin {ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|SAAS:SAAS00231970}; KW Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000256|SAAS:SAAS00232059}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3}; KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594, KW ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-ProRule:PRU00409, KW ECO:0000256|SAAS:SAAS00234082}; KW Reference proteome {ECO:0000313|Proteomes:UP000008549}. FT DOMAIN 31..472 FT /note="Biotin carboxylation" FT /evidence="ECO:0000259|PROSITE:PS50979" FT DOMAIN 151..348 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 550..819 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50991" FT DOMAIN 1090..1165 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT ACT_SITE 323 FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1" FT METAL 559 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 728 FT /note="Divalent metal cation; via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 758 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 760 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 147 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 231 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 266 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 631 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 895 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" SQ SEQUENCE 1166 AA; 128139 MW; 8F17F22121E446A3 CRC64; MRFARIPPIF ANVVRQTQHR NYANGVIKPR EFNKVMVANR GEIAIRVFRA LTELNKTSVA IYAEQDKNSI HRLKADESYL VGKGLPPVAA YLTIDQIIET ALKHDIDAIH PGYGFLSERS DFAAACQNAG IVFIGPSPDV MARMGDKVAA RQAAIEAGVQ VVPGTPGPIT TADEAVEFAK QYGTPIILKA AYGGGGRGIR RVDKLEEVEE AFRRSFSEAQ AAFGDGSLFV EKFVERPRHI EVQLLGDHHG NIVHLYERDC SVQRRHQKVV EIAPAPALPE GVREKILADA LRLAKHVGYQ NAGTVEFLVD QKGNYYFIEV NARLQVEHTV TEEITGVDLV QAQIRIAEEN HTIHTTGSAI QCRVTTEDPA KGFQPDSGRI EVFRSGEGMG IRLDSASAFA GSVISPHYDS LMVKVIASAR NHPNAAAKMI RALKEFRIRG VKTNIPFLLN VLRQPSFLDA SVDTYFIDEH PELFQFKPSQ NRAQKLLSYL GEVKVNGPTT PLATDLKPAA VSPPIPYIPA GAKPPAGLRD VLVQKGPAEF AKEVRKTPGC MITDTTFRDA HQSLLATRVR TYDMAAISPF VAQSFNGLFS LENWGGATFD VSMRFLHECP WERLQTLRRL IPNIPFQCLL RGANAMGYSN YPDNVIYKFC DLAVKNGMDV FRVFDSLNYL PNLLVGMEAV GKAGGVVEAA IAYTGDVTDK SRDKYDLKYY LNLADQLVKA QAHILSIKDM AGVLKPEAAK LLIGALRDKF PDVPIHVHTH DTSGAGVAAM LECAKAGADV VDAAVDSMSG MTSQPSMGAI VASLQGTKHD TGLSLDDISK YSAYWESTRQ LYAPFECATT MKSGNADVYK HEIPGGQYTN LQFQAFSLGL GPKFDEVKRM YREANLALGD IIKVTPSSKI VGDLAQFMVQ NNLTRETLVD RADDLSFPKS VVDFMQGNVG QPPYGFPEPL RTKVLRGKPK VDGRPGENAK PVDLDALKTE LEEKHGRKLT EEDVMSYSMF PSVFDEFETF RQQYGPVDKL PTRLFLTGLE IAEEVDVEIE SGKTLAIQLL AEGKLNKRGE REVFFDLNGQ MRSIFVVDKE ASKEIVTRPR ALPGVRGHIG APMPGDVLEL KIKEGDKVTK KQPLFVLSAM KMEMVIDSPI AGTVKAIHAA QGTKCTAGDL VIEIEP //