ID A0A9N8PUU1_9PEZI Unreviewed; 1230 AA.
AC A0A9N8PUU1;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Pyruvate carboxylase {ECO:0000256|ARBA:ARBA00072910};
DE EC=6.4.1.1 {ECO:0000256|ARBA:ARBA00013057};
GN ORFNames=AWRI4620_LOCUS6082 {ECO:0000313|EMBL:CAD0111827.1};
OS Aureobasidium uvarum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=2773716 {ECO:0000313|EMBL:CAD0111827.1, ECO:0000313|Proteomes:UP000745764};
RN [1] {ECO:0000313|EMBL:CAD0111827.1}
RP NUCLEOTIDE SEQUENCE.
RA Onetto C.;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:CAD0111827.1}.
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DR EMBL; CAINUL010000014; CAD0111827.1; -; Genomic_DNA.
DR OrthoDB; 196847at2759; -.
DR Proteomes; UP000745764; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-KW.
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; 3.10.600.10:FF:000002; Pyruvate carboxylase; 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 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; 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 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|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000745764};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..531
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 184..381
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 617..885
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 1154..1229
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1230 AA; 135520 MW; FDCA6A061F44F2F7 CRC64;
MSDIEALKRM KAENPNQDSA IEEGVDTHSQ NTVHARLRAN SSVMKAKKIL VANRGEIPIR
IFRTAHELSL QTVAVYSHED RLSMHRQKAD EAYVIGKRGE YTPVAAYLAS DEIVRIAKAH
NVNLIHPGYG FLSENAEFAR KVEAAGMIVS SPMPRKSHTN SLSLXFVGPT PDTIDALGDK
VSARELAIKC KVPVVPGTDG PVEKFEEVKG FTDKHGFPII IKAAFGGGGR GMRVVWKQEE
LKEAFERATS EAKSAFGNGT VFVERFLYRP KHIEVQLLGD SHGNVVHLFE RDCSVQRRHQ
KVVELAPAKD LPEETRQAIL NDAVALAKSV NYRNAGTAEF LVDQENRHYF IEINPRIQVE
HTITEEITGI DIVAAQIQIA AGASLEQLGL TQDRISVRGF AFQCRITTED PSXGFSPDTG
RIEVYRSAGG NGVRLDGGKN KNSMTCVAQL MIRXGNGFAG AVITPHYDSM LVKCSCRGST
YEITRRKMLR ALVEFRIRGV KTNIPFLASL LTHPTFIAGE CWTTFIDDTP ELFALVNSQN
RAQKLLGYLG DLAVNGSQIK GQIGEPKFKG DIIIPTLHDA QKNVLDVSEP CKQGWRSIIV
EQGPAAFAKA VRANKGCLIM DTTWRDAHQS LLATRVRTVD FLNIAKETSY ALSNAWALEC
WGGATFDVAM RFLYEDPWDR LRKMRKLVPN IPFQMLLRGA NGVAYSSLPD NAITHFCEQA
KKNGVDIFRV FDALNDVEQL EVGVKAVLKA GGVAEGTVCY SGDMLNPSKK YNLEYYMGVV
EKIVNMGAHI LGIKDMAGVL KPKAATMLIG SIRKKYPDLP IHVHTHDSAG TGVASMVACA
QAGADAVDAA TDSMSGMTSQ PSIGALVASL EGSDHDPGLN PHHLRMIDHY WAQLRLLYSP
FEAGLTGPDP EVYEHEIPGG QLTNLIFQAS QQGLGEQWAQ TKKAYEQAND LLGDIVKVTP
TSKVVGDLAQ FMVSNKLSYN DVLEKAEQLD FPSSVLEFFE GLMGQPYGGF PEPLRTKALR
ERRKMDKRPG LYLEPVNFDE VRNKLKEMFG GYTETDVASY VMYPKVFEDF KKWTLKFGDL
SVLPTKYFLA KPEIGEEFHV ELEKGKVLII KLLAIGPLSE QTGQREVFYE MNGEVRQVTV
DDNHAAVENK SRKKADLGDS SQVGAPMSGV VVELRVKEGS EVNKGDPIAI LSAMKMEMVI
SAPHSGKVGE LSVKESDSVD GQDLICKIVK
//
