ID R4K7G3_CLOPA Unreviewed; 1142 AA. AC R4K7G3; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 10-FEB-2021, entry version 38. DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594}; DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057, ECO:0000256|PIRNR:PIRNR001594}; GN ORFNames=Clopa_4405 {ECO:0000313|EMBL:AGK99117.1}; OS Clostridium pasteurianum BC1. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK99117.1, ECO:0000313|Proteomes:UP000013523}; RN [1] {ECO:0000313|EMBL:AGK99117.1, ECO:0000313|Proteomes:UP000013523} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC1 {ECO:0000313|EMBL:AGK99117.1, RC ECO:0000313|Proteomes:UP000013523}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J., RA Taghavi S., Francis A., van der Lelie D., Woyke T.; RT "Complete sequence of chromosome of Clostridium pasteurianum BC1."; RL Submitted (JAN-2012) 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 + 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; CP003261; AGK99117.1; -; Genomic_DNA. DR RefSeq; WP_015617389.1; NC_021182.1. DR STRING; 86416.Clopa_4405; -. DR EnsemblBacteria; AGK99117; AGK99117; Clopa_4405. DR KEGG; cpas:Clopa_4405; -. DR PATRIC; fig|86416.3.peg.4411; -. DR eggNOG; COG1038; Bacteria. DR HOGENOM; CLU_000395_0_1_9; -. DR OrthoDB; 361205at2; -. DR BioCyc; CPAS86416:G1HHA-4218-MONOMER; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000013523; Chromosome. 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; 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; PS00866; CPSASE_1; 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 ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-ProRule:PRU00409}; 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, ECO:0000256|PIRSR:PIRSR001594-2, KW ECO:0000256|PROSITE-ProRule:PRU00409}; KW Pyruvate {ECO:0000313|EMBL:AGK99117.1}. FT DOMAIN 3..456 FT /note="Biotin carboxylation" FT /evidence="ECO:0000259|PROSITE:PS50979" FT DOMAIN 123..320 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT DOMAIN 528..796 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50991" FT DOMAIN 1067..1142 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT ACT_SITE 295 FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1" FT METAL 537 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 706 FT /note="Divalent metal cation; via carbamate group" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 735 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT METAL 737 FT /note="Divalent metal cation" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3" FT BINDING 119 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 203 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 238 FT /note="ATP" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 609 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" FT BINDING 870 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2" SQ SEQUENCE 1142 AA; 127343 MW; C16AD5572E784BD0 CRC64; MKEFKRVLVA NRGEIAIRIF RACKELGIRT VAIYSNEDKY SLFRTKADEA YLIGENKSPV EAYLNIEEII SLALKKGVDA IHPGYGFLSE NAEFAKKCAE AGIEFIGPTS EMMDKLGDKI KSKIAAKAVG VSTIPGYERD IKTVEEAKKL AKECGYPIML KAAAGGGGRG MRIVRNEEEL PDAFMSAKSE AKKAFGIDVM FMEKYLEKPK HIEVQVLGDK YGNIVHLHER DCSIQRRHQK VIEFTPAFSL SDEKRNKICE DALKIARSVN YRSAGTLEFL VDANGNHYFI EMNPRVQVEH TITEMITGID IVQSQILIAE GYELGSEEIG IYSQDDIKIN GYSIQCRITT EDPFHNFAPD TGKIEVYRTS SGFGIRLDGG NGFSGAVISP YYDSLLVKNI SWSRTFKDCV RKTIRAIKET NITGVKTNIG FLINVLNHPT FLKGECDTGF IDENPELINI LPHEDEEGRL LKFIGEKVVN ETKGIKKEYD VPVVPKVEIQ DTLIGTKQLL DTKGTEGLVS WIKDQSKLLL TDTTMRDANQ SLMATRVRTR DMIKIAEATS AYGKDLFSLE MWGGATFDVA YRFLGESPWE RLAQLRKKIP NVLFQMLIRG ANAVGYKNYP DNVIREFIRE SANNGIDVFR IFDSLNWLKG MEVSIDEVLK SGKVAEACIC YTGDILNDKK TKYNLDYYIK LAKEIEKTGA HILGIKDMSA LLKPHAAYKL VGALKQEIGM PIHLHTHDTT GNGVATVLMA AEAGVDIVDT AFNSMSGLTS QPALNSVAAA LKNTRRDTGI DLRGIQRVSD YWAAVRPVYY KFESELKSGS AEIYEYEIPG GQYSNLKPQV ESFGLGHKFN EIKAMYKKVN DMLGDIVKVT PSSKMVGDFA IFMVQNDITP ENIYDKAVNM AFPDSVVAYF KGMMGQPMEG FPKKLQDLVL KGEEPITCRP GELLPEEDFN KIEEYLKDKY DIAPNKKDAL SYALYPDVFE DYLNYIKEFG DLSRLGSDVY FHGLSEGETC EAEVANGKTY MIKLSGMGKV DQEGNKTLYF EVDGNRREIK IKDRDSKNAQ ETFSTKMADS SNPLEVGAPI PGTILKVLVS EGEKVSENQP LMIVEAMKME TRVSASASGT VELINASEGQ QVKAGELLIS LK //