ID A0A428J4M9_9BACI Unreviewed; 1148 AA.
AC A0A428J4M9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
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:RSK26895.1};
GN ORFNames=EJF36_08450 {ECO:0000313|EMBL:RSK26895.1};
OS Bacillus sp. HMF5848.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2495421 {ECO:0000313|EMBL:RSK26895.1, ECO:0000313|Proteomes:UP000274811};
RN [1] {ECO:0000313|EMBL:RSK26895.1, ECO:0000313|Proteomes:UP000274811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF5848 {ECO:0000313|EMBL:RSK26895.1,
RC ECO:0000313|Proteomes:UP000274811};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Bacillus sp. HMF5848 Genome sequencing and assembly.";
RL Submitted (DEC-2018) 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:RSK26895.1}.
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DR EMBL; RWIV01000001; RSK26895.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428J4M9; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000274811; 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:RSK26895.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000274811}.
FT DOMAIN 6..458
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..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 1078..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 1148 AA; 128741 MW; 3265A89A96FA73EB CRC64;
MLKGRKINKV LAANRGEIAI RVFRACNELN IRTVAIYSKE DAGAYHRYKA DEAYLIGEGK
KPIDAYLDIE GIIEVAKNNN VDAIHPGYGF LSENIHFAMR CEEEGIIFIG PNSEHLDMFG
DKVKARQQAI NAGIPVIPGS NGPIHNLEEV LQFGSKNGYP IIIKAALGGG GRGMRIVRNE
AGLKEAYERA KSEAKAAFGS DEVYVEKLVE NPKHIEVQIL GDMDGNIVHL YERDCSIQRR
HQKVVEVAPS VGLSESLRMR ICDAAVQLMN KVHYINAGTV EFLVSENDFY FIEVNPRVQV
EHTITEMITG IDIVQSQIKI AEGHNLHSST VGVPIQEKII THGYAIQSRV TTEDPLNNFM
PDTGRIMAYR SGGGFGVRLD AGNGFQGAVI TPYYDSLLVK LSTWALTFDQ AAAKMVRNLR
EFRIRGIKTN IPFLENVVKH ENFLTGKYDT SFIDSSPELF VFPKRKDRGT KMLTYIGEVT
VNGFPGIEKK KKPVFDKPRM PKVNYANQMQ AGTKQILDQY GADGLVSWIK EQDKVLLTDT
TFRDAHQSLL ATRVRTTDLK HIAEPVAHML PELFSLEMWG GATYDVAYRF LKEDPWDRLL
ILRNKVPNIL FQMLLRASNA VGYKNYPDNV IQEFVKKSAE AGIDVFRIFD SLNWVKGMTV
AIEAVRQSGK MAEAAICYTG DILDPSRSKY DLNYYKNIAR DLEDAGAHIL AIKDMAGLLK
PQAAYKLIST LKETIDIPIH LHTHDTSGNG IFMYAKAIEA GVDIVDTALG SMAGLTSQPS
ASSLYYALQG TKRQPNITVK NLELMSHYWE DVRKYYHDFE SGMKSPHSEI YMHEMPGGQY
SNLQQQAKAV GLGDRWEDVK DMYRRVNGMF GDIVKVTPSS KVVGDMALFM VQNNLTEDDV
YDRGDKLDFP DSVVELFEGF LGQPYGGFPR ELQRIILKGR ESIQVRPGEL LDPVDFEVVK
KQLFQTIHRQ ITSFDAISYA LYPKVFMEYV KTVEQFGDVS VLDTPTFLYG MRLGEEIEVE
IEQGKTLIVK LVSISQPQPD GYRVIYFELN GQSREVMIKD ENVRVAIASR PKVDYSKPEQ
IGASMPGTVI KVLVQKGEKV NKGDHLLITE AMKMETTIQA PFTGVIKDIF VEDGEAIQTG
DLLIELTS
//
