ID A0A0R2CSY7_9LACO Unreviewed; 1142 AA.
AC A0A0R2CSY7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 28-JAN-2026, entry version 38.
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 ORFNames=FC80_GL000747 {ECO:0000313|EMBL:KRM90755.1};
OS Liquorilactobacillus cacaonum DSM 21116.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM90755.1, ECO:0000313|Proteomes:UP000051131};
RN [1] {ECO:0000313|EMBL:KRM90755.1, ECO:0000313|Proteomes:UP000051131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM90755.1,
RC ECO:0000313|Proteomes:UP000051131};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Genome Announc. 6:8322-8322(2015).
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=hydrogencarbonate + pyruvate + ATP = oxaloacetate + ADP +
CC phosphate + H(+); 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:KRM90755.1}.
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DR EMBL; AYZE01000014; KRM90755.1; -; Genomic_DNA.
DR RefSeq; WP_057828979.1; NZ_AYZE01000014.1.
DR AlphaFoldDB; A0A0R2CSY7; -.
DR STRING; 1423729.FC80_GL000747; -.
DR PATRIC; fig|1423729.3.peg.755; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000051131; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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 CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000018; Biotin carboxylase; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR FunFam; 3.20.20.70:FF:000033; Pyruvate carboxylase; 1.
DR FunFam; 3.30.470.20:FF:000012; Pyruvate carboxylase; 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; CPAse_ATP-bd.
DR InterPro; IPR055268; PCB-like.
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; NF006761; PRK09282.1; 1.
DR NCBIfam; NF009554; PRK12999.1; 1.
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|ARBA:ARBA00023267, ECO:0000256|PIRNR:PIRNR001594};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
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:KRM90755.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051131}.
FT DOMAIN 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 527..795
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1063..1138
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 290
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 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 536
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 608
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 868
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 1104
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1142 AA; 127344 MW; 5897388A520FB882 CRC64;
MKKILIANRG EIAIRIIRAC QELKIKTVAI YAKEDEFSVH RFKADEAYQV GEGKKPIEAY
LDMDDIIRVA KETEVDAIHP GYGFLAENEL FAEKCEAAGI IFIGPTKAQL ATFGDKVKAK
EAAHKAGLQT IPGSDGPVHT LEEVKLFTAE HGYPIMVKAA LGGGGRGMRI ISDESEIEES
FNRAQSEAKQ AFGDEELYIE KYLKNPKHIE VQILADKHGN VVHLFERDCS VQRRHQKVIE
VAPSSLNKAR RMEICEAAIS LMKSVNYQNA GTVEFLVTDT NFYFIEVNPR VQVEHTITEM
ITGIDIVQSQ IQIAAGADLF LDLEIPRQDK MNYHGFAIQC RVTTEDPENN FMPDTGKIET
YRSPGGFGVR LDGGNAYAGA VISPYFDSLL VKACVQSRTF NGAVLKMNRV LDEFRIRGIK
TNIPFMRNVI NHPDFISGKA DTTFIDSTPE LFHLTHLKNT PNQLLKYIGD ITVNGFPGAQ
RHEKVFVPKI ELIDNFAVSS RKENAKNILD KNGAVAAMDW VKEQSKLLLT DTSMRDAHQS
LFATRMRTKD MLPVAQVFDN ALPNIFSAEV WGGATFDVAY RFLDEDPWER LKKIRNAMPN
TLLQMLFRGS NAVGYKNYPD NVLQRFIKKS ASDGIDVFRI FDSLNWVTQM EKSIQFVRDT
GKIAEGTMCY TGDILNTAEN KYDLNYYRTL AKDLVSAGSQ IIGIKDMAGL LKTQAAFELI
STLKEEVDVP IHLHTHDTTG NAIATYLQAA RAGVDIVDVA ASALSGTTSQ PSMSSLFYAL
SGNKRQPDLD IENVEKINRY WLGIKPIYQD FMNGITAPQT DIYETEMPGG QYSNLQQQAK
ALGIKDFEEV KKTYKEVNEL LGDIVKVTPS SKVVGDFAIF MIQNKLDSNN IFERGQMLDF
PESVVNFFAG DLGQPVGGFP KKLQQIVLKD RKPITVRPGS LAKTVNFGEK NLELRDKLKH
LPTEEELLSY LLYPDVFVDY ASAIENFGDL SSLDTTTFYQ GMRTEETVHI EQGKGQILIV
KLASIGEADE DGKRVLYFIV NGQDQQIVIQ DKSKKGKIKK ILKAEPTNPK HIGATLNGSV
LSVLVTKGQI VSKGEPLIVT EAMKMETTIK APTNGKITHI YVKAGDILET QDLLIEIDPV
KS
//
