ID F9UQ80_LACPL Unreviewed; 1143 AA.
AC F9UQ80;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 13-SEP-2023, entry version 60.
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=pycA {ECO:0000313|EMBL:CCC79369.1};
GN OrderedLocusNames=lp_2136 {ECO:0000313|EMBL:CCC79369.1};
OS Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
OS (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=220668 {ECO:0000313|EMBL:CCC79369.1, ECO:0000313|Proteomes:UP000000432};
RN [1] {ECO:0000313|EMBL:CCC79369.1, ECO:0000313|Proteomes:UP000000432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000313|Proteomes:UP000000432};
RX PubMed=12566566; DOI=10.1073/pnas.0337704100;
RA Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P.,
RA Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W., Stiekema W.,
RA Lankhorst R.M., Bron P.A., Hoffer S.M., Groot M.N., Kerkhoven R.,
RA de Vries M., Ursing B., de Vos W.M., Siezen R.J.;
RT "Complete genome sequence of Lactobacillus plantarum WCFS1.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003).
RN [2] {ECO:0000313|EMBL:CCC79369.1, ECO:0000313|Proteomes:UP000000432}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-793 / NCIMB 8826 / WCFS1
RC {ECO:0000313|Proteomes:UP000000432};
RX PubMed=22156394; DOI=10.1128/JB.06275-11;
RA Siezen R.J., Francke C., Renckens B., Boekhorst J., Wels M.,
RA Kleerebezem M., van Hijum S.A.F.T.;
RT "Complete resequencing and reannotation of the Lactobacillus plantarum
RT WCFS1 genome.";
RL J. Bacteriol. 194:195-196(2012).
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};
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DR EMBL; AL935263; CCC79369.1; -; Genomic_DNA.
DR RefSeq; WP_011101664.1; NC_004567.2.
DR RefSeq; YP_004889883.1; NC_004567.2.
DR AlphaFoldDB; F9UQ80; -.
DR STRING; 220668.lp_2136; -.
DR EnsemblBacteria; CCC79369; CCC79369; lp_2136.
DR GeneID; 77215526; -.
DR KEGG; lpl:lp_2136; -.
DR PATRIC; fig|220668.9.peg.1810; -.
DR eggNOG; COG1038; Bacteria.
DR HOGENOM; CLU_000395_0_2_9; -.
DR OrthoDB; 9807469at2; -.
DR PhylomeDB; F9UQ80; -.
DR Proteomes; UP000000432; Chromosome.
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; PS00866; CPSASE_1; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:CCC79369.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000432}.
FT DOMAIN 1..451
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 529..797
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1072..1141
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 291
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 116
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 538
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 610
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 707
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
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 738
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 871
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 707
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1107
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1143 AA; 127200 MW; 490F3AF66DACD1A9 CRC64;
MKKVLIANRG EIATRVIRAC HELGLQTVAI YAKEDEFSVH RFKADEAYLV GEGKAPIAAY
LDIEDIIRIA KENHVDAIHP GYGFLSENAT FARRIAEEGM TFVGPKPEHL EMFGDKITAK
RVARDAGVQT IPSTLHPVTS LNEALQFTQQ YGYPIMIKAA MGGGGRGMRI VHEASELQEA
FDRARSEAMQ SFGDDEIYLE KFIANPKHIE VQILADAHGN VMHLFERDCS VQRRNQKVIE
FAPAVALPIE LRQKICNAAV DLMKSVHYLN AATVEFLVEG DQFYFMEVNP RVQVEHTVTE
MITEIDIVHA QLKIAMGGDL FEDLRLPHQD ALTYKGAAIQ CRITTEDPAN DFMPDTGRIE
TYRSPGGNGV RLDAGNTYSG AIVTPYFDSL LVKACVAARN FKAAVHKMRR VLVEFDIRGV
KTNIPFMLNV IDNPTFQAGE AGTRFIDQTP TLFKFPDDTQ REDKMLKYIG NVTVNGFADV
AQHSKKYYPD VEFKDDFQPI APDIVTAKDV LDQQGVQGLQ QWLLAQKQVL LTDTTMRDAH
QSLFATRMRT KDMLAVAAAS QKALPQLFSY EMWGGATFDV AYRFLNENPW NRLKELRQAM
PRTLFQMLFR GSNAVGYQNY PDNVIREFIL EAAKSGIDVF RIFDSLNWIP QMEKSIQAVK
ETGKIAEATI CYTGDIMDPD RQKYNLDYYR QLALDLQSTG ADIIAIKDMA GVLKPEAAYE
LVSTLKDALS VPVHLHTHDT TGNGIFTYAR AVEAGVDVVD VAASALSGTT SQPSMSSLYY
ALAHNDRQPD VDINNVEAIN RYWQGVRPYY QDFSNGMTGP QTDIYQTQMP GGQYSNLQQQ
AKAVGLGDRW EEVKTMYATV NDMFGDIIKV TPSSKVVGDM ALFMMENHLT PDDVYNQGTK
LDFPASVINF FAGNLGQPVG GFPKKLQQIV LKGQPALTVR PGSLAKPADF AAVKAELSAK
LGHEASHQEV LSYILYPKVF MDYDASHKRY GHVSLLDTPT FFQGMRLGET VNIELAKGKT
MIVKLNQISD PDVDGVRTLY FSINGQNQEI MVKDNAIHQS ATSTRKAEPT NEDEVGATMS
GSVLKLLVKK GQTVKKGEPL LVTEAMKMET TIQAPEDGVI EHIYVNAGDV IQTDDLLLEI
APQ
//
