ID A0A380NI61_9FIRM Unreviewed; 1148 AA.
AC A0A380NI61;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=cfiB {ECO:0000313|EMBL:SUP40287.1};
GN ORFNames=NCTC12020_00260 {ECO:0000313|EMBL:SUP40287.1};
OS Veillonella criceti.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=103891 {ECO:0000313|EMBL:SUP40287.1, ECO:0000313|Proteomes:UP000255367};
RN [1] {ECO:0000313|EMBL:SUP40287.1, ECO:0000313|Proteomes:UP000255367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12020 {ECO:0000313|EMBL:SUP40287.1,
RC ECO:0000313|Proteomes:UP000255367};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-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};
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DR EMBL; UHIO01000001; SUP40287.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A380NI61; -.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000255367; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000255367}.
FT DOMAIN 3..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 125..320
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 1074..1143
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 295
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 1109
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1148 AA; 128628 MW; 12A4693CF1054002 CRC64;
MKEIKSVLVA NRGEIAIRVF RACNEMGIRT VAIYSKEDSL SLHRNQADEA YLVGRGKKPV
DAYLDIEDII RIAHEHDVDA IHPGYGFLAE NARFAKRCEE EGIIFIGPRL EHLEMFGDKV
NARIQAKLAG IPMIPGSDGP LNNFEELEEF AKTHGFPLMI KAVNGGGGRG MRAVESMGEL
REAYDRAKSE AKMAFGDDDV YVEKLIVEPK HIEVQIMGDA HGNVVHLYER DCSVQRRHQK
VVEMAPAFAL PLETRQRICE AAVKIMKNVK YVGAGTVEFL VTNDGNFYFI EVNPRIQVEH
TITELITGID IVHTQIRVAE GYSLFDEEVG IPSQDKIECN GQAIQCRITT EDPSNNFMPD
TGKLVAYRSS GGFGIRLDGG NAFTGSVITP YYDSLLVKAS SWALTPEESI QKMLRCLREF
RIRGVKTNIH FLINVLESPE FVAGTCNVNF IDEHPELFIF KQVRDRGTKM LRYIADVTVN
GYQGLGRQDV PDFEPIQMPP LLSIKPPAGT KQKFDELGPE GFSKWLMDQK QVYFTDTTWR
DAHQSLFATR LRTVDMARVV GEAARGVPNL FSLECWGGAT FDVAYRFLHE DPWERLRMFR
KEVPNVLLQM LLRGANAVGY TSYPDNVVRQ FIKLAAANGV DVFRVFDSLN SLDNMHVAID
EVRNQNKIAE VSLCYTGDIL DASRPKYNLD YYVKMAKEVE KAGANIIAIK DMAGLLKPQA
AYNLVSALKD AVDLPIHLHT HEGAGNAIYS YGRAIDAGVD VVDVAYSAFA NGTSQPSMNS
LYYGLSGHER QPEMDANYME HMSHYFASIR PYYKGVDKTN PYPSTEVYQH EMPGGQFSNL
QQQAKSVGLG ERWDEVKKVY HQVSMMFGDI IKVTPSSKVV GDMTLFMVQN DLTEEDIYNK
GETLDFPQSV VEFFQGYLGV PYQGFPEKLQ KIILKGKKPL KGRPGASLEP VDFEDVRKKL
LDMGSPATDE DVIAYCLYPK VYSDYVEFNS DYDDISVLDT PTFFFGMRRG ESIHVTIEKG
KMLIIKLIHV SEVDEDGNRI ISFEFNGQPR DIKVRDKHVK TTGVVRHKVD KTQPGEVGAT
LSGSVVKILV KSGQSVLKGE PLIVTEAMKM ETTITSPIDG IVGEVYVREG SRIESGDCLI
KIQDRSNS
//