ID   A0A076EHF9_RHOOP        Unreviewed;      1134 AA.
AC   A0A076EHF9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   03-MAY-2023, entry version 39.
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; Actinomycetota; 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|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}.
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DR   EMBL; CP008947; AII04523.1; -; Genomic_DNA.
DR   RefSeq; WP_037245506.1; NZ_CP008947.1.
DR   AlphaFoldDB; A0A076EHF9; -.
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   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   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   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   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         200
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         235
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         533
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         605
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         703
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         732
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         734
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         867
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         703
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1093
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
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
//