ID A0A0F9ZPU0_TRIHA Unreviewed; 718 AA.
AC A0A0F9ZPU0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=THAR02_05611 {ECO:0000313|EMBL:KKP02282.1};
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544 {ECO:0000313|EMBL:KKP02282.1, ECO:0000313|Proteomes:UP000034112};
RN [1] {ECO:0000313|Proteomes:UP000034112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6776 {ECO:0000313|Proteomes:UP000034112};
RX PubMed=26067977; DOI=10.1128/genomeA.00647-15;
RA Baroncelli R., Piaggeschi G., Fiorini L., Bertolini E., Zapparata A.,
RA Pe M.E., Sarrocco S., Vannacci G.;
RT "Draft whole-genome sequence of the biocontrol agent Trichoderma harzianum
RT T6776.";
RL Genome Announc. 3:E0064715-E0064715(2015).
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:KKP02282.1}.
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DR EMBL; JOKZ01000157; KKP02282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZPU0; -.
DR OMA; RENAYDY; -.
DR OrthoDB; 2727909at2759; -.
DR Proteomes; UP000034112; 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:UP000034112}.
FT DOMAIN 25..121
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 155..278
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 286..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..453
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 718 AA; 78197 MW; 07FCCCEABF1083E4 CRC64;
MDPVTYHMEE NSLTSLVPIF TVVRNPEDAA GNRDGPFDYV ILCVKALPDV YDLAAVIESV
VTPQHTCILV NTTHTLGIEA AIEERFPTNV VLSLVSGAEL TQLGQSEFEH KGSTDVWVGP
ASRNANIPQS IQEDMAQAIS MTLSSGQVNS QVSNNIRQQQ YERVIGPIAF HPISVIFETS
NHVALLEKMG VKDMISEVID ELLRLAEANG CKFAPNFKQS IMDDMAKPNQ PESIMWQDFI
ARRPMEVETY LGSPIRLARD AKVSVPRIET LYAILHNLNI VNRNRPKQDA APVGNGPSSP
NNPSPYPPRG PSQAGFRPMM PNGNGMPPRQ PRPRTSSNFS NAGGMRRPPP NANGGPNGYG
RPPQMNGGNS RAASRRGSME GNDLEEFSHL VLYDDIPEGQ EQSFGTDNSD LALRERELQL
RQRELALREQ EMRMRRGPPP PQASAPPSRR GPPPSRGGFD DDDEDDDYFD PSMAAPVPMI
DPDNFDMMSV TSRKNRKVPG PSQTQMRRNP EGDAPPSKSS RFRPFGRNRS SQMSQISQMP
TVTDNILDDP LLSFTSNRYG AVDRGAMSAG SRANSLTASR LDEMQFGPGG GGGQTMTMTS
GYPRRTSHSP GNQYSPSMRG GNSRPSPPNG FGPTNGQPSP PNGMRQPMPR YPPGQGTTVA
PQQVEQQIGV SSLNPPKSRN GRSLTGSASA SADSGEFGSE RSAYSSQGSL QQQQYQGQ
//