(data stored in ACNUC7421 zone)

SWISSPROT: C1ART4_RHOOB

ID   C1ART4_RHOOB            Unreviewed;      1134 AA.
AC   C1ART4;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   Name=pyc {ECO:0000313|EMBL:BAH48761.1};
GN   OrderedLocusNames=ROP_05140 {ECO:0000313|EMBL:BAH48761.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48761.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48761.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48761.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) 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; AP011115; BAH48761.1; -; Genomic_DNA.
DR   RefSeq; WP_012687768.1; NC_012522.1.
DR   ProteinModelPortal; C1ART4; -.
DR   STRING; 632772.ROP_05140; -.
DR   EnsemblBacteria; BAH48761; BAH48761; ROP_05140.
DR   KEGG; rop:ROP_05140; -.
DR   PATRIC; fig|632772.20.peg.567; -.
DR   eggNOG; ENOG4108JIJ; Bacteria.
DR   eggNOG; COG1038; LUCA.
DR   HOGENOM; HOG000282801; -.
DR   KO; K01958; -.
DR   OMA; EFVDACN; -.
DR   OrthoDB; POG091H02XZ; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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;
DR   PRODOM; C1ART4.
DR   SWISS-2DPAGE; C1ART4.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594, ECO:0000313|EMBL:BAH48761.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:BAH48761.1}.
FT   DOMAIN        2    450       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      122    318       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      525    794       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1054   1128       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    293    293       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       534    534       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       704    704       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       733    733       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       735    735       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     118    118       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     201    201       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     236    236       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     606    606       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     868    868       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1134 AA;  121701 MW;  A7B0357F79B684D0 CRC64;
     MTFSKVLVAN RGEIAIRAFR AAYELGAGTV AVFPYEDRNS IHRLKADESY QIGEEGHPVR
     AYLSVDEIVS AAKQAGADAI YPGYGFLSEN PDLAAACAEA GITFVGPSAE VLELTGNKAR
     AIAAAKAAGL PVLASSEPSA DVDELLAAAE TMQFPLFVKA VAGGGGRGMR RVAERAQLKE
     SIEAAAREAE SAFGDPTVFL EQAVVDPRHI EVQILADGQG NVIHLFERDC SLQRRHQKVI
     ELAPAPNLPE ELRAKICADA VAFAKEINYA CAGTVEFLLD TRGNHVFIEM NPRIQVEHTV
     TEEVTDVDLV QSQLRIASGE TLADLGLSQD KITLRGAALQ CRITTEDPAN GFRPDTGRIT
     AYRTPGGAGI RLDGGATLGA EVGAYFDSML VKLTCRGRDF ETAVARARRA VTEFRIRGVS
     TNIPFLQAVL DDPDFKAGRA TTSFIEERPE LLTLRSSADR GTKILSYLAD VTVNKPHGER
     PSAVYPRDKL PQIDLSTPPP DGSRQKLLAL GPEGFAKALR EQKALAVTET TFRDAHQSLL
     ATRVRTSGLL DVAGHVARLT PELLSIEAWG GATYDVALRF LHEDPWYRLS ALREAVPNIC
     LQMLLRGRNT VGYTPYPEKV TRAFVEEATN SGIDIFRIFD ALNNVDQMRP AIDAVRETGT
     SVAEVALSYT GDLSNPHEKL YTLDYYLRLA EEIVEAGAHI IAIKDMAGLL RAPAATTLVT
     ALRKNFDLPV HVHTHDTPGG QLATYLAAWQ AGADAVDGAS AAMAGTTSQP ALSAIVAAAA
     HSEHDTGLDL QAVCDLEPYW EALRKVYAPF ESGLPAPTGR VYTHEIPGGQ LSNLRTQAVA
     LGLGDKFEEV EAKYAAADRM LGRLVKVTPS SKVVGDLALH LVGSGASTEE FKDNPAKFDL
     PDSVVGFLRG ELGTPPGGWP EPFRTRALEG RGEAKPEVPL SAEDEKALAG TSAERRATLN
     RLLFPGPTKE FLEHRDKYGD TSQLSANQFF YGLRRGDEHR VRLAQGVELL IGLEAISEPD
     ERGYRTVMAI LNGQLRPVSV RDRSISSEIP AAEKADKNNP GHVPAPFAGV VTLAVTEGQH
     VAAGDTIATI EAMKMEAAIT APRGGTVTRL AIGSVQQVEG GDLLAVVATT DAAE
//

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