ID A0A2P8ABR7_9PEZI Unreviewed; 761 AA.
AC A0A2P8ABR7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:PSK57910.1};
GN ORFNames=B9Z65_9112 {ECO:0000313|EMBL:PSK57910.1};
OS Elsinoe australis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK57910.1, ECO:0000313|Proteomes:UP000243723};
RN [1] {ECO:0000313|EMBL:PSK57910.1, ECO:0000313|Proteomes:UP000243723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:PSK57910.1,
RC ECO:0000313|Proteomes:UP000243723};
RA Cheng Q.;
RT "Draft genome sequence of Elsinoe australis.";
RL Submitted (MAY-2017) 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=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|ARBA:ARBA00000564};
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:PSK57910.1}.
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DR EMBL; NHZQ01000037; PSK57910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8ABR7; -.
DR STRING; 40998.A0A2P8ABR7; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000243723; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:InterPro.
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 Gene3D; 3.10.600.10; pyruvate carboxylase f1077a mutant domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
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; 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; PF00364; Biotin_lipoyl; 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; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW Pyruvate {ECO:0000313|EMBL:PSK57910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000243723}.
FT DOMAIN 1..62
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 148..416
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 685..760
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 761 AA; 83574 MW; E94D95E1E34855A0 CRC64;
MLVKCTCHGS TYEIARRKIL RALVEFRIRG VKTNIPFLAS LLTHPTFIGG TCWTTFIDDT
PELFALIGSQ NRAQKLLSYL GDLAVNGSQI KGQIGEPKFK GDIILPKITD KTGHAFDVSE
PSTKGWRNIL VEKGPEAFAK AVRANKGCLI MDTTWRDAHQ SLLATRVRTV DMLNIAKETS
HALSNAWALE CWGGATFDVA MRFLYEDPWD RLRKMRKLVP NIPFQMLLRG ANGVAYSSLP
DNAIYHFCEQ AKKCGMDIFR VFDALNDMEQ LEVGVKAVLK AGGVAEGTVC YSGDMLNPKK
KYNLEYYMGL VDRIVKMGAH ILGIKDMAGV LKPQAATLLV GSIRKKYPEL PIHVHSHDSA
GTAVASMIAC AQAGADAVDA ATDSMSGMTS QPSIGAIVAS LEGGEFDTGL DTTALRAIDS
YWAQLRLLYS PFEAGLTGPD PEVYEHEIPG GQLTNLIFQA SQQGLGEQWA QTKKAYEEAN
DILGDIVKVT PTSKVVGDLA QFMVANGLSY DDVIEKASEL DFPSSVLEFF EGLMGQPYGG
FPEPLRSKAL RNRRKMDKRP GLYLDPMDFD GIRKKLKDAY GGCTETDVAS YAMYPKVFED
YKKWTQKYGD LSVLPTRYFL ARPEIGEEFH VELEKGKVLI LKLLAIGPLS EQTGQREVFY
EMNGEVRQVT VDDQHAAVEN KSRPKADMGD SSQVGAPMSG VIVEMRVKDG GEVSKGDPIA
ILSAMKMEMV ISAPHSGKIG DLLVKEGDSV DSQDLVCKIV K
//
