ID B0A6G0_9FIRM Unreviewed; 1151 AA.
AC B0A6G0;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 78.
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=SAMN02745147_2594 {ECO:0000313|EMBL:SKA60748.1};
OS Intestinibacter bartlettii DSM 16795.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Intestinibacter.
OX NCBI_TaxID=445973 {ECO:0000313|EMBL:SKA60748.1, ECO:0000313|Proteomes:UP000190760};
RN [1] {ECO:0000313|EMBL:SKA60748.1, ECO:0000313|Proteomes:UP000190760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16795 {ECO:0000313|EMBL:SKA60748.1,
RC ECO:0000313|Proteomes:UP000190760};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
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DR EMBL; FUXV01000008; SKA60748.1; -; Genomic_DNA.
DR RefSeq; WP_007285337.1; NZ_FUXV01000008.1.
DR AlphaFoldDB; B0A6G0; -.
DR STRING; 261299.ERS852493_02491; -.
DR eggNOG; COG1038; Bacteria.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000190760; 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:UniProtKB-UniPathway.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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:SKA60748.1}.
FT DOMAIN 4..457
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 124..321
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 531..799
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1068..1143
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 540
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 612
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 709
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 738
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 740
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 873
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 709
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 1151 AA; 129078 MW; 8C3693298399C89B CRC64;
MQKKFNKILV ANRGEIAIRI FRACAELGIK SVGIYSKEDK YSLFRTKADE SYLIGEDKGP
IDVYLDMDGI IALAKEKNVD AIHPGYGFLA ENSEFVRKCE ENGIAFIGPS ADIMDKMGDK
INSKKVAHAA DVPTIPGVDK VIETVEEAKK VADYVGYPVM VKASNGGGGR GMRVVYNEKD
LALEYETACS ESRKAFGKAV IFIEKYIVDP KHIEVQILGD KEGNIVHLYE RDCSVQRRHQ
KIIEYAPAFS LPKEVRENIC NDAVKIAKSV GYVNAGTLEF LVDAEGNHYF IEMNPRVQVE
HTVTEEVTGI DIVQSQILIA EGYTLDSEEI DIKSQDDIKV SGYSIQCRIT TEDPKNSFMP
DTGKIQVYRT GSGAGIRLDG GNGCAGFDIS PYYDSLLVKT VSWDRTFKKA INKMLRSIRE
FRIRGVKTNV GFLINVLENP LFQEGKCSTK FIDEHPELFN IKESKNRATK LLQFIGNVIV
NENKCAQKPV FTTPHKPIIR TDIPDIEGSR QQLERLGKKA YIDKIRNEKK LLLTDTSMRD
AHQSLVATRL RTYDFLQAAP ATEAYMKDLF SLEMWGGATY DVAYRFLNES PWIRLQKLRK
EIPDILFQML FRASNGVGYT NYPDNVITKF IKEAAEQGID VIRIFDSLNW VENMKLSIDA
GLETGKIVEA TMCYTGDILD PSKSKYNLEY YINMAQELEA LGTDIICIKD MAGLLKPQAA
YTLIKALKDN VKAPIHLHTH DTSGNGVATC LMASKAGVDI VDTALQSMAG LTSQPSLNAV
VEALRFDERD TNIDLFGYEQ IGDYYYDLRE VYKKFESGLT TSFAQIYQYE MPGGQYSNLK
AQADSLGLKD EFDSVKENYK KANKILGDII KVTPSSKVVG DLAIFMTKNK LDEENIIEEG
KKLSFPDSVV DYCKGMIGQP VGGIPQDLQE VVLKGEAPIT ERPGKLMPLA DFEADKKYLD
EKFSMDSNIR NILSYELYPK VYEDYLRHLQ EYNDISKLES HVFFYGLDKD EECDVEIEEG
KSLSIRLIGV GEVKENGYRT VIFRMNGSLR EVEIKDNNYS GLIRQVELAD MDDPLQIGAA
IPGKVVKTLV KKGDVVEENQ PLIVIEAMKM ETNIVAKVAG KISSIEVKEG DMVTDKQLLM
TMEAVEVEAE A
//