ID A0A2C9XRJ4_9ENTE Unreviewed; 1142 AA.
AC A0A2C9XRJ4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A5844_000251 {ECO:0000313|EMBL:OTP12036.1};
OS Enterococcus sp. 10A9_DIV0425.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1987383 {ECO:0000313|EMBL:OTP12036.1, ECO:0000313|Proteomes:UP000194933};
RN [1] {ECO:0000313|EMBL:OTP12036.1, ECO:0000313|Proteomes:UP000194933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10A9_DIV0425 {ECO:0000313|EMBL:OTP12036.1,
RC ECO:0000313|Proteomes:UP000194933};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 10A9_DIV0425.";
RL Submitted (MAY-2017) 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:OTP12036.1}.
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DR EMBL; NGMO01000001; OTP12036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9XRJ4; -.
DR STRING; 1987383.A5844_000251; -.
DR Proteomes; UP000194933; 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; 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:OTP12036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000194933}.
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 528..796
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1071..1140
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 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 537
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 609
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 706
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 735
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 737
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 870
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 706
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1106
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1142 AA; 127827 MW; 20C23BAD56FAC9FE CRC64;
MRKVLVANRG EIAVRVFRAC TELGIQTVGI YAQEDEYSVH RFKADEAYLV GEGKKPIDAY
LDIEGILEIA KACGADAIHP GYGLLSENLH FATRCQEEGI TFVGPELHHL DIFGDKIKAK
TAAIEAGIAS IPGTDGPVKD VNEVLAFVEQ YGYPVMIKAA LGGGGRGMRV AYDEKGAREG
YERAKSEAKA AFGSDEVYVE KYISNPKHIE VQILGDKHGN IIHLFERDCS VQRRHQKVVE
VAPCVSVDDQ QRQRICEAAV QLMKHVGYVN AGTVEFLVEK DEFYFIEVNP RVQVEHTITE
MITDVDIVTT QLLIAQGKDL HTEIGLPKQS EIKINGSAIQ CRITTEDPLN HFLPDTGKID
TYRSPGGFGV RLDVGNAYAG YVVTPYFDSL LVKVCTHAAD FTTAIQKMER CLREFRIRGI
KTNIPFMLNV ILHPEFQSGL AKTTFIDNTS ELFIFPRLRD RGNKTMKYIG EITVNGFPGI
KRGEKPYYDA PRMPKELIKR PEFVTAKNVL DTNGAEGLVE WIKQQDNLLL TDTTFRDAHQ
SLLATRVRTK DFKEIARLTG EGLPELFSSE MWGGATFDVA YRFLNEDPWK RLRKIRSLMP
NTLLQMLFRG SNAVGYSNYP DNVLVEFVKE AAAQGIDVFR IFDSLNWVPQ MEKSIQAVRD
TGKIAEATIC YTGDINDPSR AKYNVQYYKD MAKELEQLGA HIIAIKDMAG LLKPQAAYRL
ISELKDTTDL PIHLHTHDTS GNGIITYSAA TKAGVDIVDV AMSAMSGNTS QPSMSSLYYA
LVNGPRVPEI TIQNVQQLNH YWEDVRMYYK PFENGLNAPE TEVYMHEMPG GQYSNLQQQA
KAVGLGHRWD EIKKMYHTVN LMFGDIVKVT PSSKVVGDMA LFMVQNDLTE EDIYAKGESL
SFPESVVTFF QGELGQPVGG FPEKLQKIIL KGRPAFTERP GLLAEPVDFE QVKAELANKI
GYEPKQEEVL SYLMYPQVFL DYQNAYNQFG DVTLLDTPTF FQGIRLGETV NVQIEKGKIL
IIRLDEIGEP DIEGNRVLFF NLNGQRREIM IKDTSIVSAV QTRRKAEPTN REQIGATMSG
SVLDVLVKKG DMVRKGDTLM ITEAMKMETS IEAPFDGEVI HLYVTSGDPI SSGDLLIEVT
EK
//
