ID A0A1I4IUV7_9BACI Unreviewed; 1149 AA.
AC A0A1I4IUV7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=SAMN04488054_102223 {ECO:0000313|EMBL:SFL57566.1};
OS Salibacterium qingdaonense.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=266892 {ECO:0000313|EMBL:SFL57566.1, ECO:0000313|Proteomes:UP000199668};
RN [1] {ECO:0000313|EMBL:SFL57566.1, ECO:0000313|Proteomes:UP000199668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6134 {ECO:0000313|EMBL:SFL57566.1,
RC ECO:0000313|Proteomes:UP000199668};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOTY01000002; SFL57566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4IUV7; -.
DR STRING; 266892.SAMN04488054_102223; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000199668; 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; 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 Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:SFL57566.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199668}.
FT DOMAIN 6..459
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 536..804
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1079..1148
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 298
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 545
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 617
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 714
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 743
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 745
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 878
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 714
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1114
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1149 AA; 129152 MW; 13985B967062BBB2 CRC64;
MNGLGNIQKV MVANRGEIAI RIFRACTELH IRTVAVYSQE DTGAFHRYKA DEAYLVGEGQ
KPIDAYLDIE SIIETAKATN VDAIHPGYGF LSENLEFAER CKEEGIIFIG PGTEHLHMFG
DKVRARETAI EAGIPVIPGS DGPVSGLDEV KQFADKHGYP FIIKASLGGG GRGMRIVRSG
EALEDSYDRA KSEAKSAFGS DIVYVEKFIE NPKHIEVQIL GDHDGNIVHL YERDCSVQRR
HQKVVEVAPS VALSEELREN ISAAAVKLAE NINYYNAGTV EFLVNEKEEF FFIEVNPRVQ
VEHTITELVT GVDIVQSQLY IAAGKSLHGE ELAIPRQKDI RTHGYAIQSR VTTEDPANNF
LPDTGRINAY RSSGGFGVRL DAGNGFQGAV ITPHYDSLLV KVSTWALNFE GAAAKMLRNL
REFRIRGIKT NIAFLENVVQ HEQFLAGTYD TSFIDSAPEL FVFPKRKDRG TKMLSFIGET
IVNGYPGLED AKKPVFEQPE LPEIKKSEPF PEGAKQILDQ KGPEGLADWV KNQKEVLLTD
TTFRDAHQSL LATRFRTNDL QKAAEPTARL LPNLFSEEMW GGATFDVAMR FLHEDPWERL
LTLREKMPNV LMQMLLRSSN AVGYKNYPDN VIREFVEKSA TAGIDVFRIF DSLNWVEGMR
LTINEVREQN KIAEAAMCYT GDILEPKRDK YDLKYYKGLA KELEQAGAHM LGIKDMAGLL
KPEAAYQLIS ELKETIDIPI HLHTHDTSGN GIFSYARAIE AGVDVVDVAV SSMAGLTSQP
SANSLYYALK GSPRQPQVDI KALEELSQYW DYTRKYYQGF ESGMNAPHTE VYEHEMPGGQ
YSNLQQQAKA VGLQGRWNEV KKMYRRVNDM FGDIVKVTPS SKVVGDMALY MVQNDLTEDD
IYEKGENLDF PDSVVELFQG YLGQPYQGFP KELQRIILKG RQPITNRPGE NMEPVNFNEI
KEDLYHKLDR QVTSHDMISY ALYPKVYMDF EKFRQQFGDV SVLDTPTFFY GLRLGEEIEV
EIEQGKTLIV KLISISRPHD DGNRIVYFEL NGQPREVMIK DQNADTTGAE RPKVDKSDEN
QIGASMPGTV VKKLVGKGEK VKKGDHLMIT EAMKMETTVQ APFDAEIKNV YVTDGDTIET
GDLLIYLEK
//
