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
//