ID A0A1W2BV35_9FIRM Unreviewed; 1143 AA.
AC A0A1W2BV35;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 28-JAN-2026, entry version 34.
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=SAMN02745168_2393 {ECO:0000313|EMBL:SMC76586.1};
OS Papillibacter cinnamivorans DSM 12816.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC Oscillospiraceae; Papillibacter.
OX NCBI_TaxID=1122930 {ECO:0000313|EMBL:SMC76586.1, ECO:0000313|Proteomes:UP000192790};
RN [1] {ECO:0000313|EMBL:SMC76586.1, ECO:0000313|Proteomes:UP000192790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12816 {ECO:0000313|EMBL:SMC76586.1,
RC ECO:0000313|Proteomes:UP000192790};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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=hydrogencarbonate + pyruvate + ATP = oxaloacetate + ADP +
CC phosphate + H(+); 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; FWXW01000006; SMC76586.1; -; Genomic_DNA.
DR RefSeq; WP_084235068.1; NZ_FWXW01000006.1.
DR AlphaFoldDB; A0A1W2BV35; -.
DR STRING; 1122930.SAMN02745168_2393; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000192790; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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 CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR FunFam; 2.40.50.100:FF:000003; Acetyl-CoA carboxylase biotin carboxyl carrier protein; 1.
DR FunFam; 3.30.1490.20:FF:000003; acetyl-CoA carboxylase isoform X1; 1.
DR FunFam; 3.40.50.20:FF:000010; Propionyl-CoA carboxylase subunit alpha; 1.
DR FunFam; 3.20.20.70:FF:000033; Pyruvate carboxylase; 1.
DR FunFam; 3.30.470.20:FF:000012; Pyruvate carboxylase; 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; CPAse_ATP-bd.
DR InterPro; IPR055268; PCB-like.
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; NF006761; PRK09282.1; 1.
DR NCBIfam; NF009554; PRK12999.1; 1.
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 Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|PIRNR:PIRNR001594};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001594-3};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR001594}; Pyruvate {ECO:0000313|EMBL:SMC76586.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192790}.
FT DOMAIN 8..461
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 128..325
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 1065..1143
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 208
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 1143 AA; 126824 MW; AA9185EF677B3134 CRC64;
MAQTEVKDFK KVLVANRGEI AIRIFRACYD LGLNTVAIYS KEDVYNLFRT KADESYQVDE
SHSPLGAYLD IDWIIAEAKR RGADAIHPGY GFLSENPNFA KACEDNGIKF IGPPSSVLAQ
MGDKLNAKAI AIRCGVPIIP GSTVPLKDGQ DALEKAVNYG FPVILKAAAG GGGRGMRRCS
KPEEVIPAFD LVRSEAKKAF GNDDIFIEKF IEEPKHVEVQ ILADEHGNVV HLYERDCSLQ
RRYQKVVEFT PAFAVPEETR KKLYADAVKI AKEVGYINAG TVEFLVDKSG NHFFIEMNPR
IQVEHTVTEM VTGIDLVRAQ ILIAEGKPLS TPEIGIKSQN DVKARGYSIQ CRITTEDPQN
NFAPDTGKIT AYRSGGGYGV RLDAGNAYSG AEISPYYDSL LVKITTIDNT FEGACRKALR
SISETRVRGV KTNMAFISNI LSNPTFRAGK CHTKFIDETP ELFKIEDSQD RATKMLKYIA
NIVVNDPTAG RKLYETPRFP KVTEQPRPGL KQMLDKEGPE AVQKWVLAQK KLLVCDTTMR
DAHQSLLATR VRTRDMVKGA EGMADALADA FSLEMWGGAT FDVAYRFLHE DPWERIDLLR
EKIPNILFQM LLRGANAVGY TNYPDNLIRE FIREAAKSGI DVFRIFDSLN WIPGMEIAID
EVLKCGKIAE ASICYTGDIL DPSRDKYTVK YYVDMAKELE KRGAHTLCIK DMSGLIKPYA
AKKLVTALKN EIGIPVHLHT HDTSGNQVAA LLMAAEAGVD IVDVAISSMS SLTSQPSMNA
VVAALERQER DTGLDLQKLQ GLTDYWSDIR ERYDVFEAGI KSPATDIYRY EIPGGQYTNL
KPQVESLGLG HRFDEVKEKY KTVNDMLGDI VKVTPSSKMV GDLAIFMVQN DLTPENIVSK
GENLTFPDSV VSYFKGMMGQ PAWGFPEDLQ RVVLKGVEPI RGRPGELLPP VDFEAARKTI
EKFQHNPTWR DILSWCLYPK VLEDYFKTYR EHGYIMRLGS HVYFHGLAVG ETNKVNIEDG
KTLVIKYLGL GDLNPDGTRN VQFELNGARR EVAVPDNTAP VSAQAVTIAD PEDKSQIGAS
IPGAVSKVMV KAGDAVKENQ VLAVIEAMKM ETSVVARMDG VIKEVFIKPG QSVKAGELLI
VMK
//
