ID R1GBD7_BOTPV Unreviewed; 618 AA.
AC R1GBD7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative 2-dehydropantoate 2-reductase protein {ECO:0000313|EMBL:EOD43184.1};
GN ORFNames=UCRNP2_10115 {ECO:0000313|EMBL:EOD43184.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD43184.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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DR EMBL; KB916885; EOD43184.1; -; Genomic_DNA.
DR RefSeq; XP_007589346.1; XM_007589284.1.
DR AlphaFoldDB; R1GBD7; -.
DR KEGG; npa:UCRNP2_10115; -.
DR eggNOG; ENOG502QT3Z; Eukaryota.
DR HOGENOM; CLU_021479_0_0_1; -.
DR OMA; RENAYDY; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708:SF25; PROTEIN PAM1-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000013521}.
FT DOMAIN 10..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 200..323
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 331..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 66956 MW; 551E72B280139D97 CRC64;
MAPATPRLRI LSVGGNAVSA FLSWRLQATN SCDVTLVWKS GFEHVAQYGI SMKSKLYGNE
RFKPRAVVRS PEEAAGISKA PFDYVFLCVK ALPDVYDIAS VIESVVSPQH TCILINTTHA
LGVEAFLEQR FPTNVVLSLV SGAELQQLGA SEFEHSGSSE IWVGPASDNP SIPSSIQSDM
ADALAMTLGS GQVDCRVSPN IRQQQYERMI GNIAFHPTSV LFETANHAEL VEKVGVRSVI
SGVVDELLQI ATAQGCTFGP DFKDKTIEAM TRPQEANSTM YQDFAAKRPM EVETYLGSPM
KLAQEANVPV PRIETLYAML HHLNIVNQQR PAAPVSPQQG GGLPPRMSSA PMPRGPPPAN
GMNGMNGHPM KNGPRPGSRA PSMTGGPPPQ MMRRGPPPPN GFPPQRPHMG NGYGPPGPPM
NRRGSFEGND LEEFSHLMLY DAVPEDGADL PNGMVNGGPY PGGDMSNGDL ALREKELALR
QRELALRERE YQMRAVAGPR RPMPPASHAG DFDEEDDGDF FDPMASRTGP AIDPDNFDMM
SVTSRRTRKA PSAQQLRKNP EMGGPPPMNG RPRGGPYGRP GMNKRTSARL MSDVPGLHDS
IMNNALIGYS SDRHLVIP
//