ID A0A395S0C2_9HYPO Unreviewed; 770 AA.
AC A0A395S0C2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:RGP65725.1};
GN ORFNames=FLONG3_9088 {ECO:0000313|EMBL:RGP65725.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP65725.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP65725.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP65725.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP65725.1}.
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DR EMBL; PXOG01000229; RGP65725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395S0C2; -.
DR STRING; 694270.A0A395S0C2; -.
DR Proteomes; UP000266234; 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:UP000266234}.
FT DOMAIN 10..166
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 199..321
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 326..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 83554 MW; 8D1A27F131F326E6 CRC64;
MTNRELMSVC SVGGNPVSAF LSWRLQATNA CDVTLVWKSG YDHVAQYGIS FKSPIFGNER
FKPRHVVRNP EDAANARDGP FDYVVLCVKA LPDVYDLASV IDSVVTPQHT CILVNTTHTL
GVEAALEERF PTNVVLSLVS GAELTQLGQS EFEHKGPTDI WIGPANTPQN IPKTIQEDMA
QALAMTLSSG QVECKVSPNI RQQQYERVIG PIAFHPVSVI FETPNHALLL EKVGVRGMVS
DVIDELLRLA NAHGCKFEPD FKQKTMDEMT KASGESIMWQ DYVARRPMEV ETYLGSPVKL
AKDSNITLPR IETLYSILHN LNLVNRNRPK PGDPNANIMP PASPSAQTVP RMPSQNSHRP
MMNGMPNGSG MPPRQPRPRN SSNFSQGGMR RGPPPMNGGP PNGYGRGPPS INGGGSRQPS
RRGSMEETNL EEFSHLVLYD DIPEGSEPSV TGDPSDINIR EREMALRQRE MALREQEMRM
RRGPPPSGPP GGPGPRRGPH PMRNSKQVFD EDEDDDDDYF DPTTNAGPPM IDPDNFDMMS
VTSRKNRKAP GPTPGQFRRN PDDMPPPTRG GRFRPNFGRN RSSQVGGHSS MTTENILEDP
LMSCSSDRYG SVDRGAMNAG SRANSLTASR LDEMQYGPGP GGPPGMNGAF PRRASQSPGN
PYPPSMRGGS RRGSPPGGYG PGPGMNGRPS PPDGVRQPVP RHPPGQGNSV APQQVEQHIG
VSALHQTKPR NVRSLTGSAS ASAGSGEFDS EQSANSSQGS LPPRPPIGVR
//
