GenomeNet

Database: UniProt
Entry: B0A6G0_9FIRM
LinkDB: B0A6G0_9FIRM
Original site: B0A6G0_9FIRM 
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}.
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; 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
//
DBGET integrated database retrieval system