ID A0A076EHF9_RHOOP Unreviewed; 1134 AA. AC A0A076EHF9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 25-MAY-2022, entry version 34. DE RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594}; DE EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594}; GN ORFNames=EP51_07920 {ECO:0000313|EMBL:AII04523.1}; OS Rhodococcus opacus (Nocardia opaca). OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus. OX NCBI_TaxID=37919 {ECO:0000313|EMBL:AII04523.1, ECO:0000313|Proteomes:UP000028488}; RN [1] {ECO:0000313|EMBL:AII04523.1, ECO:0000313|Proteomes:UP000028488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=R7 {ECO:0000313|EMBL:AII04523.1, RC ECO:0000313|Proteomes:UP000028488}; RA Di Gennaro P., Zampolli J., Presti I., Cappelletti M., D'Ursi P., Orro A., RA Mezzelani A., Milanesi L.; RT "Genome Sequence of Rhodococcus opacus Strain R7, a Biodegrader of RT Mono- and Polycyclic Aromatic Hydrocarbons."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. 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 + N(6)-biotinyl-L-lysyl-[protein] = CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate; CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145, CC ChEBI:CHEBI:456216; EC=6.3.4.14; CC Evidence={ECO:0000256|ARBA:ARBA00024172}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502; CC Evidence={ECO:0000256|ARBA:ARBA00024172}; 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|ARBA:ARBA00000564, CC ECO:0000256|PIRNR:PIRNR001594}; CC -!- COFACTOR: CC Name=biotin; Xref=ChEBI:CHEBI:57586; CC Evidence={ECO:0000256|ARBA:ARBA00001953, CC ECO:0000256|PIRNR:PIRNR001594}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000256|ARBA:ARBA00004742}. 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; CP008947; AII04523.1; -; Genomic_DNA. DR RefSeq; WP_037245506.1; NZ_CP008947.1. DR EnsemblBacteria; AII04523; AII04523; EP51_07920. DR eggNOG; COG1038; Bacteria. DR UniPathway; UPA00138; -. DR Proteomes; UP000028488; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro. 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; PS00867; CPSASE_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001594}; KW Biotin {ECO:0000256|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:AII04523.1}. FT DOMAIN 1..449 FT /note="Biotin carboxylation" FT /evidence="ECO:0000259|PROSITE:PS50979" FT DOMAIN 121..317 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 524..793 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50991" FT DOMAIN 1053..1127 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT REGION 929..950 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 292 FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1" FT METAL 533 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 703 FT /note="Divalent metal cation; via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 732 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 734 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 117 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 200 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 235 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 605 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 867 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" SQ SEQUENCE 1134 AA; 121798 MW; 56CF87CFA6CDEA56 CRC64; MFSKVLVANR GEIAIRAFRA AYELGAGTVA VFPYEDRNSI HRLKADESYQ IGEEGHPVRA YLSVDEIVSA AKQAGADAIY PGYGFLSENP DLAAACAEAG ITFVGPSAEV LELTGNKARA IAAAKAAGLP VLASSEPSAD VDELLAAAET MQFPLFVKAV AGGGGRGMRR VAERAQLKES IEAAAREAES AFGDPTVFLE QAVVDPRHIE VQILADGQGN VIHLFERDCS LQRRHQKVIE LAPAPNLSEE LRAKICADAV AFAKEINYAC AGTVEFLLDT RGNHVFIEMN PRIQVEHTVT EEVTDVDLVQ SQLRIASGET LADLGLSQDK ITLRGAALQC RITTEDPANG FRPDTGRITG YRTPGGAGIR LDGGTSVGAE VSAYFDSMLV KLTCRGRDFE TAVARARRAV TEFRIRGVST NIPFLQAVLD DPDFKAGRVT TSFIEERPQL LTLRSSADRG TKILTYLADV TVNKPHGERP SAVYPRDKLP QIDLSTPPPD GSRQKLLALG PEGFAKALRE QKALAVTETT FRDAHQSLLA TRVRTSGLLD VAGHVARLTP ELLSIEAWGG ATYDVALRFL HEDPWYRLAA LREAVPNICL QMLLRGRNTV GYTPYPEKVT RAFVEEATNS GIDIFRIFDA LNNVDQMRPA IDAVRETGTA LAEVALSYTG DLSNPNENLY TLDYYLRLAE EIVEAGAHII AIKDMAGLLR APAATTLVTA LRKNFDLPVH VHTHDTPGGQ LATYLAAWQA GADAVDGASA AMAGTTSQPA LSAIVAAAAH SQYDTGLDLQ AVCDLEPYWE ALRKVYKPFE SGLPAPTGRV YTHEIPGGQL SNLRTQAVAL GLGDKFEEVE AKYAAADRML GRLVKVTPSS KVVGDLALHL VGSGASTEEF KENPAKFDIP DSVVGFLRGE LGTPPGGWPE PFRTRALEGR GAAKPEVPLS AEDEKALSGT SAERRATLNR LLFPGPTKEF LEHRDKYGDT SQLSANQFFY GLRRGDEHRV RLAPGVELII GLEAISEPDE RGYRTVMCIL NGQLRPVSVR DRSISSEIPA AEKADKNNPG HVPAPFAGVV TLAVTEGQHI TAGDTIATIE AMKMEAAITA PRSGTVSRLA IGSVQQVEGG DLLAVVSTGE SASE //