ID E3ZP52_LISSE Unreviewed; 1146 AA.
AC E3ZP52;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=NT03LS_1232 {ECO:0000313|EMBL:EFS00595.1};
OS Listeria seeligeri FSL N1-067.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=702453 {ECO:0000313|EMBL:EFS00595.1};
RN [1] {ECO:0000313|EMBL:EFS00595.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFS00595.1};
RX PubMed=21126366; DOI=10.1186/1471-2164-11-688;
RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H.,
RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.;
RT "Comparative genomics of the bacterial genus Listeria: Genome evolution is
RT characterized by limited gene acquisition and limited gene loss.";
RL BMC Genomics 11:688-688(2010).
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:EFS00595.1}.
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DR EMBL; ADXJ01000510; EFS00595.1; -; Genomic_DNA.
DR RefSeq; WP_003746811.1; NZ_CM001051.1.
DR PATRIC; fig|702453.3.peg.993; -.
DR HOGENOM; CLU_000395_0_1_9; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000004302; Chromosome.
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:EFS00595.1}.
FT DOMAIN 3..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 532..800
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1067..1144
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 541
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 613
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 710
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 739
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 741
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 874
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 710
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1110
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1146 AA; 128021 MW; 84C75AA1F5990632 CRC64;
MNRIKKVLVA NRGEIAIRVM RACTELKIKT VAIYSQEDTG SFHRYKSDEA YLVGAGKKPI
DAYLDIENII EIAKESGADA IHPGYGFLSE NIEFARRCEQ EGIIFVGPKS KHLDMFGDKI
KAKEQALLAG IPVIPGSDGP VAGIKEVEEF GEKNGYPLMI KASLGGGGRG MRVVESKEHV
KESFERASSE AKAAFGNDEV YVEKCVMNPK HIEVQILGDT HGNIVHLFER DCSIQRRHQK
VVEVAPCNAI TSELRNRICD AAVKLMNNVD YINAGTVEFL VEGDDFYFIE VNPRVQVEHT
ITEMITGIDI VQSQLFIADG YALHDQLVAI PRQEDIHIHG SAIQSRITTE DPLNNFMPDT
GRVDTYRSTG GFGVRLDAGN GFQGTVVTPF YDSLLVKLCT WGMTFEQATR KMRRNLIEFR
IRGVKTNIPF LLNVVRHPDF ASGNYNTSFI DTTPELFKFP HIRDRGTKTL RYIGNVTVNG
FPGIKHRDKP VYTEPRLPKI PFGSQIAPGT KQILDAKGPE GVVDWVKKQE EVLLTDTTLR
DAHQSLLATR VRSKDIFQIA DSMAHLLPNM FSFEMWGGAT FDVAYRFLNE DPWVRLETLR
KQIPNVMFQM LLRGANAVGY KNYPDNVIRE FVKQSAQSGV DVFRVFDSLN WIKGMEVSID
AVREAGKVVE AAICYTGDID DETRTKYTID YYKDMAKELV AQGTHILGIK DMAGLLKPQA
AYRLIGELKD TVDVPIHLHT HDTSGNGIYT YAAAVSAGVD IVDVASSAMS GATSQPSMTG
LYYGLVNGNR QTNLDAQNSQ IINHYWEDVR HYYKDFDNAL NSPQTEVYIH EMPGGQYTNL
QQQAIAVGLG DRWDEVKEMY TEVNQMFGDI VKVTPSSKVV GDLALFMVQN ELTEEDVYEK
GDTIDFPDSV IEFFMGEIGQ PYGGFPEKLQ KLVLKGRKPL TDRPGALMEP VNFADVKAEL
KEKMGYEPSE KDVISYILYP KVFLDYQEMI SKYGDVTVLD TPTFYKGMRL GETIEXELEK
GKILLIKLNS VGEPIADGTR VIYFELNGQP REINIQDMNV QSTVIARRKI DTTNPEHVGA
TMTGSVIQVV VKKGESVKKG DPLLITEAMK METTIQAPFD GEVSSIHVSD GDAIESGDLL
IEVNRI
//
