ID A0A0A2VEG9_9BACI Unreviewed; 1147 AA.
AC A0A0A2VEG9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=N780_00165 {ECO:0000313|EMBL:KGP92050.1};
OS Pontibacillus chungwhensis BH030062.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385513 {ECO:0000313|EMBL:KGP92050.1, ECO:0000313|Proteomes:UP000030153};
RN [1] {ECO:0000313|EMBL:KGP92050.1, ECO:0000313|Proteomes:UP000030153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030062 {ECO:0000313|EMBL:KGP92050.1,
RC ECO:0000313|Proteomes:UP000030153};
RA Wang Q., Wang G.;
RT "Genome of Pontibacillus chungwhensis.";
RL Submitted (AUG-2013) 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:KGP92050.1}.
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DR EMBL; AVBG01000003; KGP92050.1; -; Genomic_DNA.
DR RefSeq; WP_036780888.1; NZ_AVBG01000003.1.
DR AlphaFoldDB; A0A0A2VEG9; -.
DR STRING; 1385513.N780_00165; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000030153; 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; 3.40.50.20; -; 1.
DR Gene3D; 6.10.140.310; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 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; IPR013815; ATP_grasp_subdomain_1.
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|ARBA:ARBA00023267, 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:KGP92050.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030153}.
FT DOMAIN 6..458
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 535..803
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1072..1147
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 297
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 544
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 616
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 713
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 742
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 744
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 877
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 713
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1113
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1147 AA; 128911 MW; 810417BBB8C5AF19 CRC64;
MGERKKINKV LVANRGEIAI RVFRACTELD IRTVAVYSKE DSGSYHRYKA DEAYLVGEGK
KPIDAYLDIE GIIEIAKSVG VDAIHPGYGF LSENIHFARR CEEEGLTFIG PTSEHLNMFG
DKVKARYQAI QADIPVIPGT DGPVTDIEEV KAFGRKHGYP IMIKAALGGG GRGMRIVRSE
AALQDGYDRA KSEAKAAFGN DDVYVEKLVE NPKHIEVQIL GDADGNIVHL YERDCSVQRR
HQKVVEVAPS VSLHNDIRER MCEAAVKLMN NVTYLNAGTV EFLVSGDEFY FIEVNPRVQV
EHTITELITG IDIVQAQIMI AEGYNLFDKP ISIPKQEDIR THGFAIQSRV TTEDPLNNFM
PDTGKIMAYR SGGGFGVRLD AGNGFQGAVI SPYYDSLLVK VSTWALSFDQ AAHKMVRNLR
EFRIRGIKTN IPFLENVILH NKFLSGEYNT TFIDQSPELF VFPKRKDRGT KMLSYIGATT
VNGFEGTSHR KKPALPKPRE PVVKHSEPIA AGTKQLLDEQ GPEAVAEWLK NRKEVLYTDT
TFRDAHQSLL ATRVRGKDLE HIAEPTARLL PNLFSVEMWG GATFDVSYRF LKEDPWKRLL
TMREKMPNML FQMLLRASNA VGYKNYPDNV IKEFVEKSAQ AGIDVFRIFD SLNWVEGMKL
AIEAVRDTGK IAEAAMCYTG DILDPSRPKY DLAYYTSLAK ELEDAGAHIL AIKDMAGVMK
PEAAFQLVSA LKETVNIPIH LHTHDTSGNG IFTYARAIEA GVDVVDVAAS TMAGLTSQPS
ASSLYYALEG NDRKPNIDVN AYEELGHYWH DIRKYYQDFE SGMMAPHSEV YQHEMPGGQY
SNLQQQAKAV GLESRWDEVK RMYRRVNDMF GDIVKVTPSS KVVGDMALFM VQNELTEDDV
YEKGESIDFP DSVLEFFQGY LGQPYQGFPQ ELQRIILKGK EPLSVRPGEL LEPVDFKDLK
ENLFQKLDRQ VTSFDMISYA LYPKVFMDYH QFYEQYGDMS VLDTLTFFYG MRLGEEIEVE
IEQGKTLIVK LVSIGEAQPD ATRVVYFELN GQPREVVIKD QNIKASVEAR PQVDKQNPKH
IGATMPGTVV SVISNKGETV NKGDHLMITE AMKMETTVQA PFDGKIKNIY VKNGEAIHVG
DLLIEFE
//
