ID A0A428T3K1_9HYPO Unreviewed; 774 AA.
AC A0A428T3K1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Alcohol dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP52_011358 {ECO:0000313|EMBL:RSL96604.1};
OS Fusarium oligoseptatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL96604.1, ECO:0000313|Proteomes:UP000287144};
RN [1] {ECO:0000313|EMBL:RSL96604.1, ECO:0000313|Proteomes:UP000287144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL96604.1,
RC ECO:0000313|Proteomes:UP000287144};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RSL96604.1}.
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DR EMBL; NKCK01000136; RSL96604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428T3K1; -.
DR STRING; 1325735.A0A428T3K1; -.
DR Proteomes; UP000287144; 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:UP000287144}.
FT DOMAIN 10..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 200..322
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 325..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..505
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 734..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 83580 MW; C90226BFC63B3555 CRC64;
MAPVSPRLRI LSVGGNPVSA FLSWRLQATN ACDVTLVWKS GYEHVAQYGI SFKSPTFGNE
RFKPRHVVRN PEDAASAREG PFDYVVLCVK ALPDVYDLAS VIDSVVTPQH TCILINTTNT
LGVEAALEER FPTNVVLSLV SGAELAQLGQ SEFEHKGPTD IWIGPASRNA NIPQSIQEDM
AQALAVTLSS GQVECKVSPN IRQQQYERVM GPIAFHPISV IFETPNHAAL LEKVGVRDMV
SEVLDELLRL AASNGCKFDA DFKQKTIDEM TKASGESIMW QDYVARRPME IETYLGSPVK
LARDNKVSVP RIETLYAILH NLNTVNRNRP KPGDPNANIM PPSSPTAPQL PRMPSQNSHR
PMMNGMPNGN GMPPRGPRPR NSSNLSQAGM RRGPPSMNGG PPNGYPRPPP SMNGGGSRQP
SRRGSLEENS LEEFSHLVLY DDIPEGSESS VAGDNSDIAL RERELALRQR ELAIREQEMR
MRRGPPGPPG PHGPPGGPGG PGPRRGPHPM RNSKQVFDDD DDDDDDYFDP TANPAPPLID
PDNFDMMSVT SRKNRKAPEQ NPAQFRRNPD NLPPPTRGGR FRPSFGRNRT SQVGHTHAPM
TTENILEDPL LSCSSNRYGA VDRGAMSAGS RANSLTAARL DDLQYGPGPG GPPGMNGAYP
RRASQSPGNP YSPSMRGGSR RGSPPNGYGP GMNGRPSPPD GVRQPVPRHP PGQGNAVAPH
QVEQHIGVSA LPQTKPRNVR SLTGSASASA GSGESESANS SQGSLPPRPP IGVR
//