ID K3VQP6_FUSPC Unreviewed; 401 AA.
AC K3VQP6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Pyruvate carboxyltransferase domain-containing protein {ECO:0000259|PROSITE:PS50991};
GN ORFNames=FPSE_02427 {ECO:0000313|EMBL:EKJ77349.1};
OS Fusarium pseudograminearum (strain CS3096) (Wheat and barley crown-rot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=1028729 {ECO:0000313|EMBL:EKJ77349.1, ECO:0000313|Proteomes:UP000007978};
RN [1] {ECO:0000313|EMBL:EKJ77349.1, ECO:0000313|Proteomes:UP000007978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CS3096 {ECO:0000313|EMBL:EKJ77349.1,
RC ECO:0000313|Proteomes:UP000007978};
RX PubMed=23028337; DOI=10.1371/journal.ppat.1002952;
RA Gardiner D.M., McDonald M.C., Covarelli L., Solomon P.S., Rusu A.G.,
RA Marshall M., Kazan K., Chakraborty S., McDonald B.A., Manners J.M.;
RT "Comparative pathogenomics reveals horizontally acquired novel virulence
RT genes in fungi infecting cereal hosts.";
RL PLoS Pathog. 8:E1002952-E1002952(2012).
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
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:EKJ77349.1}.
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DR EMBL; AFNW01000059; EKJ77349.1; -; Genomic_DNA.
DR RefSeq; XP_009253821.1; XM_009255546.1.
DR AlphaFoldDB; K3VQP6; -.
DR EnsemblFungi; EKJ77349; EKJ77349; FPSE_02427.
DR GeneID; 20361046; -.
DR KEGG; fpu:FPSE_02427; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_711901_0_0_1; -.
DR OrthoDB; 2781767at2759; -.
DR Proteomes; UP000007978; Chromosome 3.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044283; P:small molecule biosynthetic process; IEA:UniProt.
DR CDD; cd07948; DRE_TIM_HCS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR048253; DRE_TIM_HCS_fun_bact.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF48; HOMOCITRATE SYNTHASE, CYTOSOLIC ISOZYME-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000007978};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 123..376
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 42462 MW; 954297244AE07AC3 CRC64;
MQTANNPISH HTSHTMGEGA ASSNSGDNSC GANSVGHHTS HTMGQGASSS SSGANGGGGV
AEAQRVNDGI TLGASLTDVE TDNNDNDNES DDASSLGDSL ASLDGTAGSV ATSMRSSGSL
SDFKIIDTTL REGEQFATAY FTTETKMKIA KALDDIGVEY LELTSPASSP QSKADAQAIC
KMGLKAKVLV HIRCNMDDAR IAVETGVDGI NMCIGTSAQL MKHSHGKDLD WIAAKAKEVI
EFTQAHGLEV RFSGEDSFRS DFSEILKLYS LMDRLGAHRV GIADTVGGAS WREVYDKVST
LRQMIGCDIE THFHNDTGCA TSNAYTALEA GATHIDTTVL GIGERNGITP LGKLFQCMLG
FGHEYVATKY RLDKLPALEK LVAEAVDIEI PWDTPDLSVF L
//