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Entry: B1C9J0_9FIRM
LinkDB: B1C9J0_9FIRM
Original site: B1C9J0_9FIRM 
ID   B1C9J0_9FIRM            Unreviewed;      1141 AA.
AC   B1C9J0;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 70.
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:EDS72561.1};
GN   ORFNames=ANASTE_02283 {ECO:0000313|EMBL:EDS72561.1};
OS   Anaerofustis stercorihominis DSM 17244.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC   Anaerofustis.
OX   NCBI_TaxID=445971 {ECO:0000313|EMBL:EDS72561.1, ECO:0000313|Proteomes:UP000005178};
RN   [1] {ECO:0000313|EMBL:EDS72561.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72561.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Anaerofustis stercorihominis (DSM 17244).";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS72561.1, ECO:0000313|Proteomes:UP000005178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17244 {ECO:0000313|EMBL:EDS72561.1,
RC   ECO:0000313|Proteomes:UP000005178};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2008) 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   -!- 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:EDS72561.1}.
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DR   EMBL; ABIL02000006; EDS72561.1; -; Genomic_DNA.
DR   RefSeq; WP_007051031.1; NZ_DS560019.1.
DR   AlphaFoldDB; B1C9J0; -.
DR   STRING; 445971.ANASTE_02283; -.
DR   eggNOG; COG1038; Bacteria.
DR   HOGENOM; CLU_000395_0_1_9; -.
DR   OrthoDB; 9807469at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000005178; 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   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:EDS72561.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005178}.
FT   DOMAIN          3..454
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          123..318
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          526..794
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   DOMAIN          1063..1141
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   ACT_SITE        293
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         201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         535
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         607
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   BINDING         704
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         733
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         735
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT   BINDING         868
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT   MOD_RES         704
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT   MOD_RES         1107
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ   SEQUENCE   1141 AA;  127873 MW;  8738BAEB188E6F62 CRC64;
     MKKFKRVLIA NRGEIAIRII RAVQELGMKA ICIYCEEDKL SLFRSKADEA YLIKGINSPT
     DAYLNIEAII ELAKAKNIDA IHPGYGFLSE NPIFAAECEK AGIKFIGPSS DVIELLGNKV
     NAKEAAIEAG VSVLDGVKVE TVEEAKEISS KIGYPVIIKA SAGGGGRGMR VCEREDDLRN
     QFESAVREAK KAFNNGEVFI EKYVRAPRHV EAQILADEYG HIVHLFERDC SIQRRHQKII
     EFSPSQSISE ETRKAICEES VNLAKHVGYT NAGTVEFLVD ENEKHYFMEV NPRIQVEHTV
     TELVTNVDLV QAQILIAEGY KLTDEEINIK SQEDIKMSGA AIECRVTTEN VLNNFMPDTG
     KIDVYKTGSG PGVRLDGGNG FVGSEITPYF DSLLVKTTTY ARDFDKARKK MIRTLKEHEI
     EGVSTNKDFL INVLEHEDFK KGICNTNFIE DHPELFNISA FDNQTVKLLE YLAKTTLAKN
     SSDREILPKI EVPIYKDMPN LSGTKQILDE KGPEGLVQWI KDQKQLLFMD TTMRDAQQSL
     FATRMRTNDF LKIAESVSRY EKDIYALELW GGATFDTSYR FLKESPWSRL ELLREMIPNI
     LFQMLLRGSN AVGYKNYPDN VIKAFIKQSA ESGIDVFRVF DSLNWLDQIK PSVEEVLKLG
     KVAEVAICYS GDILDKNKTK YTLDYYVKKA KEVEAMGAHI LAIKDMSGLL KPAAAMRLAK
     ALKDEISIPI HFHTHDTAGN GVSSMLMASA AGVDIVDAAV SSMSGTTSQP SLDSIVAAVE
     HTPRESNINV DDIQVISDYY EKARKYYTGF ESGLKTGTTQ IYKYEVPGGQ YSNLKSQVES
     FGLGHRFTDV LEKYKEANEL LRDIIKVTPT SKVVGDFAIF MLQNDLDKEN IYEKGKDLAF
     PDSVVDFFKG MIGQPEWGFD EKLREVVLKG AEFVDKRPGL LLPDEDFDKI KAEYKEEFNM
     DLNNKQVLSA ALYPKVYKEY LRFKETYGDL TYMSSDAFFS GLSKGEETEV FFGEGKSHVI
     KLVRTGRTHA DGNRRMVFEV DGFRRALYVE DPNAIRSQVM SQAVEMADSN NDKHIGSPIP
     GSVIKVNVAI GDKVEKNQAV CVVEAMKMET EVVSPAEGVI KDVLVQELDS VKAGQLLIEL
     E
//
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