ID E4KQ09_9LACT Unreviewed; 1164 AA.
AC E4KQ09;
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 Name=pyc {ECO:0000313|EMBL:EFR31191.1};
GN ORFNames=HMPREF9257_1162 {ECO:0000313|EMBL:EFR31191.1};
OS Eremococcus coleocola ACS-139-V-Col8.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Eremococcus.
OX NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR31191.1, ECO:0000313|Proteomes:UP000005990};
RN [1] {ECO:0000313|EMBL:EFR31191.1, ECO:0000313|Proteomes:UP000005990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR31191.1,
RC ECO:0000313|Proteomes:UP000005990};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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:EFR31191.1}.
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DR EMBL; AENN01000015; EFR31191.1; -; Genomic_DNA.
DR RefSeq; WP_006418394.1; NZ_AENN01000015.1.
DR AlphaFoldDB; E4KQ09; -.
DR STRING; 908337.HMPREF9257_1162; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000005990; 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; 1.10.472.90; Conserved carboxylase domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 2.
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 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:EFR31191.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005990}.
FT DOMAIN 3..455
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 551..820
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1089..1164
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 560
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 632
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 730
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 759
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 761
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 894
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 730
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1130
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1164 AA; 130364 MW; 4C3923ED4032D398 CRC64;
MNKIHKLLIA NRGEIATRII RASHELGIET IAIYSKEDVG ALHRQKADYS YLIGEDLGPI
EAYLDIEGII NLAKEKGVDA IHPGYGFLSE NQEFAQRCAE EGIIFVGPQV KHLQMFGNKT
QARETALAAD LPVIPGSQGG VASLSEVKSF VQEHGYPIMI KAVNGGGGKG MRIVRQADEL
EQAYDRAKSE AKTSFGDDSI YVERYVENPK HIEVQIIGDQ HGNLVHLFER DCSIQRRHQK
VVEIAPSFNL SPSMRDKLTR AALQLMNHIG YENAGTVEFL VAGDDYYFIE VNPRVQVEHT
VTELITGIDI VKSQILIADG EDLFGPAIHM PHQTDIQAKG FAIQCRITTE DPLNNFSPDS
GKIIGYHSPG GAGIRLDAGD AYGGAQISPF YDSLLVKVSS YSRSKKGAIE KMQRALSEIR
LVGLKTNIRF LENILKHPEF NQGDFDTTFI DNHPELFEFV PPRNRGVQLL KYIANVSVNG
FPGIKKGTKP DFPKRIVPEV EGHQYQLHKE SLDRPGKRWL RHKHQEQSYK HLLDQAGPQA
VVEKILAEST PLLTDTTLRD AHQSLLGTRL RTSDMLLVAP FMNETMQDYF SLEMWGGATF
DVAYNFLKES PWQRLQVLRQ AIPDIPFQML LRASNAVGYK NYPDNLVATF IAESAKQGID
VFRIFDSLNW LESLKLPIEK ALETGKLVEG TICYTGDILN PNRSKVYTLD YYVKLAKELE
KQGVHVLALK DMAGLLKPEA AYQLIKALKS EVKMPIHLHT HDTTGNGIMT YSRAIDAGVD
IVDTANAALS GQNSQPNTNS LFYARQGNDR QLKIDTQANE SLSNYWKITR NYYQPFESNL
KSAWTKVYDY EMPGGQYSNI QMQAQSMNLG DQFDEVLEMY HRVNLLFGDI VKVTPSSKVV
GDMALFMVQN KLDEDSLFEK GKTLDFPDSV VSFFKGEIGQ PARGMNEALR QLVLKGQTYS
EARPGSLLDD YDFEAARQSL SQQAYNEIED HDLLSLALYP KVYKDYLKFV DEYGQVTVLD
SPTFFYGLKP YEKIAVVLEE GKTLLIELTS IGPVNETGQR PVYFNLNGMP EQVIVQDQNA
QTGLKVRPKA DSENPNHIGA QMPGSVYKIE VKQGQAVESN QVLMITEAMK METAIRAPKA
GHIKAIHCQE KEQIVAGDLL IEIE
//