ID A0A0D1Y1A0_EXOME Unreviewed; 1188 AA.
AC A0A0D1Y1A0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 28-JAN-2026, entry version 51.
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=PV10_02092 {ECO:0000313|EMBL:KIV94316.1};
OS Exophiala mesophila (Black yeast-like fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV94316.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV94316.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV94316.1,
RC ECO:0000313|Proteomes:UP000054302};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) 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 -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, involving
CC the ATP-dependent carboxylation of the covalently attached biotin in
CC the first step and the transfer of the carboxyl group to pyruvate in
CC the second. {ECO:0000256|ARBA:ARBA00002380}.
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|ARBA:ARBA00049382,
CC 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; KN847521; KIV94316.1; -; Genomic_DNA.
DR RefSeq; XP_016225890.1; XM_016366372.1.
DR AlphaFoldDB; A0A0D1Y1A0; -.
DR GeneID; 27319937; -.
DR VEuPathDB; FungiDB:PV10_02092; -.
DR HOGENOM; CLU_000395_1_1_1; -.
DR OrthoDB; 196847at2759; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000054302; 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:000018; Biotin carboxylase; 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:KIV94316.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054302}.
FT DOMAIN 36..488
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 158..355
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 574..842
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1111..1186
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-1"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 583
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 655
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT BINDING 751
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 781
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 783
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-3"
FT BINDING 916
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-2"
FT MOD_RES 751
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
FT MOD_RES 1152
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001594-4"
SQ SEQUENCE 1188 AA; 130173 MW; DE7DC7033345105F CRC64;
MASATAGTAT PDHEDGQGHH EHSVHQRLRA NSSIMQLKKI LVANRGEIPI RIFRTAHELS
LQTVAVFSYE DRLGMHRQKA DEAYMIGQRG QYTPVGAYLA GDEIIKIALA HGVQMIHPGY
GFLSENSEFA RKVEEAGIIF IGPSWKVIES LGDKVSARRI AIKANVPVVP GTEGPVEKFE
EVKAFTDEYG FPIIIKAAFG GGGRGMRVVR DQESLKDNFE RATSEAKSAF GNGTVFVERF
LDKPKHIEVQ LLGDNQGNVV HLYERDCSVQ RRHQKVVELA PAKDLPAETR DAILNDAVKL
AKSVNYRNAG TAEFLVDQQN RYYFIEINPR IQVEHTITEE ITGIDIVAAQ IQIAAGATLE
QLGLTQDRIS TRGFAIQCRI TTEDPANGFS PDTGKIEVYR SAGGNGVRLD GGNGFAGAII
TPHYDSMLVK CSCHGSTYEI VRRKMLRALV EFRIRGVKTN IPFLASLLTH PTFIEGTCWT
TFIDDTPELF KLVGSQNRAQ KLLQYLGDLA VNGSSIKGQI GESKFKGDII YPTLLDPQGN
KLDVSAPSTK GWKAILDKEG PAGFAKAIRA NKGCLIMDTT WRDAHQSLLA TRVRTVDLCN
IAKETSHALE NAYALECWGG ATFDVAMRFL YEDPWDRLRK MRKLVPNIPF QMLLRGANGV
AYKSLPDNAI YHFCKQAKKN GMDIFRVFDA LNDIDQLEVG MKAVQEAGGV VEGTICYSGD
MLDPNTKYTL QYYLDLVDKI VKIGTHTVAI KDMAGVLKPK AARILVGAIR KAHPDLPIHV
HTHDSAGTGV ASMVACAEAG ADAVDAATDS MSGMTSQPSI GAILASLEGG EFDLGLDGHN
VRALDQYWSQ LRLVYSPFEA GLTGPDPEVY EHGIPGGQLT NLIFQATQLG LGSQWIETKK
AYKQANDLLG DIVKVTPTSK VVGDLAQFMV SNKLDHDSVI AKAAELDFPE SVLEFLEGYM
GQPYGGFPEP LRSRALRGRR KMDKRPGLYL DPIDFAAVRK QLKEKFDTTS ESDVASYVMY
PKVFEDYRKF VDKYGDLSVL PTKFFLNKPE IGEEFHVELE KGKILILKLL AVGPLSEATG
QREVFYEVNG EVRQVTIDDN KAAVENTSRP KADPGDSSQV GAPIAGVVVE VRSKEGHEVK
KGDPVAVLSA MKMEMVISAP HSGKVGEIFV KEGDSVAASD LIAKIAKA
//
