ID   A0A2B7XEU7_9EURO        Unreviewed;       747 AA.
AC   A0A2B7XEU7;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   13-SEP-2023, entry version 18.
DE   RecName: Full=Alcohol dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GX51_01766 {ECO:0000313|EMBL:PGH07465.1};
OS   Blastomyces parvus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060905 {ECO:0000313|EMBL:PGH07465.1, ECO:0000313|Proteomes:UP000224080};
RN   [1] {ECO:0000313|EMBL:PGH07465.1, ECO:0000313|Proteomes:UP000224080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH130 {ECO:0000313|EMBL:PGH07465.1,
RC   ECO:0000313|Proteomes:UP000224080};
RA   Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT   "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL   Submitted (OCT-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:PGH07465.1}.
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DR   EMBL; PDNC01000014; PGH07465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B7XEU7; -.
DR   STRING; 2060905.A0A2B7XEU7; -.
DR   OrthoDB; 2727909at2759; -.
DR   Proteomes; UP000224080; 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:UP000224080}.
FT   DOMAIN          10..164
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          198..321
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          328..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..358
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..398
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..633
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        658..672
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   747 AA;  81542 MW;  CAD9C46FEB93D21A CRC64;
     MSKRRDTNCV VVGGNAISAF LSWRLQATNA CDVTLVWKSG FDSVSQYGVT FRSKIFGNER
     FKPFRVVRTP EEAGSTDQPF DYVILCVKAL PDIYDLASVI ESVVTPQHTC ILVNTTSTLG
     VEAHLEHRFP TNVVLSLVSG IEITQTGPSE FEHAASTNTW VGPSSKNAMI PSSIQNDMAV
     ALAITLSTGQ VDCKVSENIR QEQYERMIGP IAFYPTSVIF ECPNHADLLE KIGLRQLISD
     VIEELVSLAK AQGCTFSEKF KESIIEKMIA RSDSPSTMYQ DFLARRPMEV ETYLGSPIKL
     ATETGIKIPR IETLYAMLHH LNISNQAKQP QLHEPTSPGP VHPPPRLSSA PPPRPPMNGM
     RGSRMGPGPG MGMPPPRRGP SSMGMHPRPP PNGFPPRGPP SMQRELSEEH NLDEFSHLML
     YDDALEDGAQ NGGYGPMPNG GGPPPDLALR ERELALRQRE LQLREQEISM RRVPRRTSTA
     RDAFDDMDDD DYFDPMDHRG PPLPQIDPDN FDMLSVTSRR NRKAPSQNPG QFRKNPEMGG
     GGRPPSAFSR HFGGGGRNRA TSRIMDEIPG VHDSLLNNPM MGYSSNRYGN VDRKEIRDES
     RANSLTASRM SEVGQGNFHP PSRRTSQSPG TSFHPAGRGM GRPPPNHDPY NGQPVMSPAG
     KPSPPGMMRA PIPKYPPGQG NAVAPQQVEQ HLGVSNSYPA KGTPKVRSLT GSASASAGSG
     DSANIDSENS AHSSQSSLGP RQSSLAR
//