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Database: UniProt
Entry: L7KJ12_9ACTN
LinkDB: L7KJ12_9ACTN
Original site: L7KJ12_9ACTN 
ID   L7KJ12_9ACTN            Unreviewed;      1129 AA.
AC   L7KJ12;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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   Name=pyc {ECO:0000313|EMBL:GAC48589.1};
GN   ORFNames=GOACH_06_00860 {ECO:0000313|EMBL:GAC48589.1};
OS   Gordonia aichiensis NBRC 108223.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1220583 {ECO:0000313|EMBL:GAC48589.1, ECO:0000313|Proteomes:UP000010988};
RN   [1] {ECO:0000313|EMBL:GAC48589.1, ECO:0000313|Proteomes:UP000010988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108223 {ECO:0000313|EMBL:GAC48589.1,
RC   ECO:0000313|Proteomes:UP000010988};
RA   Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia aichiensis NBRC 108223.";
RL   Submitted (DEC-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|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953,
CC         ECO:0000256|PIRNR:PIRNR001594};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC48589.1}.
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DR   EMBL; BANR01000006; GAC48589.1; -; Genomic_DNA.
DR   RefSeq; WP_005173972.1; NZ_BANR01000006.1.
DR   AlphaFoldDB; L7KJ12; -.
DR   STRING; 1220583.GOACH_06_00860; -.
DR   eggNOG; COG1038; Bacteria.
DR   OrthoDB; 9760256at2; -.
DR   Proteomes; UP000010988; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   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; 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   NCBIfam; TIGR01235; pyruv_carbox; 1.
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   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 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|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:GAC48589.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010988}.
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          526..795
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1055..1129
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
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         535
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         607
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         705
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
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         736
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         869
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         705
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1095
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1129 AA;  120580 MW;  A113CDAA156415F6 CRC64;
     MFEKVLVANR GEIAIRAFRA AYELGADTVA VFPYEDRNSL HRLKADESYQ IGVPGHPVRA
     YLSVDEIIGA ALHSGADAVY PGYGFLSENA ELAAACAEHG ITFVGPSAHV LELTGNKAEA
     VAAAKAAGLP VLASSEPSAD VDELVAASAD MTFPLFVKAV AGGGGRGMRR VARREDLAEA
     ISAASREADT AFGDPTVFLE QAVINPRHIE VQILADTQGN VIHLFERDCS VQRRHQKVVE
     LAPAPNLDPQ LRERICADAV AFARQIGYSC AGTVEFLVDE QGNHVFIEMN PRIQVEHTVT
     EEITDIDLVG AQMRVASGQS LHELGLDQES ISIRGAALQC RITTEDPADG FRPDVGRITA
     YRTPGGAGIR LDGSAVLGGE ISGNFDSMLV KLSCRGRDFD TAVRRARRAL AEFRIRGVAT
     NIPFLQAVLD DPDFAAGHVT TSFIEDRPWL LTSRGSADRG TRILSYLADV TVNKPHGERP
     STVYPRDKLP AVDRSRLLAP PDGSRQRLLA LGPTGFARDL RQQPAVGVTD TTFRDAHQSL
     LATRVRTSGM LAVAPYVAAM TPELLSVECW GGATYDVALR FLKEDPWDRL AQLREAMPNI
     CLQMLLRGAN TVGYTPYPQK VTTAFVAEAT EVGIDIFRIF DALNNIDAMR PAIDAVLETD
     RAVAEVAMSY TGDLANPDEK LYTLDYYLRL AEQIVDAGAH VLAIKDMAGL LRAPAAELLV
     SALRREFDLP IHVHTHDTPG GQLATYLAAV NAGADAVDGA SAPLAGTTSQ PPLSAIVAAF
     GHTERDTGLD LGAVCDLEPY WEAVRKVYAP FESGVPAPTG RVYSHEIPGG QLSNLRQQAI
     ALGLGNRFEA VEEAYAAADA MLGRLIKVTP SSKVVGDLAL ALVGQGIAPA DFAANPGSYD
     IPDSVIGFLR GELGEPAGGW PEPLRTRALA GRTAPRPVEE LSSADSAALD VAGRGRQETL
     NRLLFPGPTR EFEEHQETYG DTSQLSANQF FYGLRYGDEH RVELEPGVEL LIGLEAISDA
     DEKGMRTVMC VLNGQLRPVA VRDRSVDSKV AAAERADRAN PNHVGAPFAG VVSLSVDVGD
     EIAAGAAIGT IEAMKMEATI TAPVGGKVAR VAVSQVQQVA PGDLLIEIG
//
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