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}.
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; 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
//