ID   A0A076EHF9_RHOOP        Unreviewed;      1134 AA.
AC   A0A076EHF9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   02-NOV-2016, entry version 13.
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;
OC   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.,
RA   Orro A., 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
CC       and the transfer of the carboxyl group to pyruvate in the second.
CC       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate +
CC       oxaloacetate. {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
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DR   EMBL; CP008947; AII04523.1; -; Genomic_DNA.
DR   STRING; 632772.ROP_05140; -.
DR   EnsemblBacteria; AII04523; AII04523; EP51_07920.
DR   eggNOG; ENOG4108JIJ; Bacteria.
DR   eggNOG; COG1038; LUCA.
DR   Proteomes; UP000028488; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0004075; F:biotin carboxylase activity; 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:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
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.
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|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2};
KW   Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028488};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:AII04523.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2};
KW   Pyruvate {ECO:0000313|EMBL:AII04523.1}.
FT   DOMAIN        1    449       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      121    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      524    793       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1053   1127       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    292    292       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       533    533       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       703    703       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       732    732       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       734    734       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     117    117       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     200    200       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     235    235       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     605    605       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     867    867       Substrate. {ECO:0000256|PIRSR:
FT                                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
//