ID   A0A023B2Q7_GRENI        Unreviewed;       578 AA.
AC   A0A023B2Q7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Putative alcohol dehydrogenase {ECO:0000313|EMBL:EZG51530.1};
DE            EC=1.1.1.284 {ECO:0000313|EMBL:EZG51530.1};
GN   ORFNames=GNI_124390 {ECO:0000313|EMBL:EZG51530.1};
OS   Gregarina niphandrodes (Septate eugregarine).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Gregarinasina;
OC   Eugregarinorida; Gregarinidae; Gregarina.
OX   NCBI_TaxID=110365 {ECO:0000313|EMBL:EZG51530.1, ECO:0000313|Proteomes:UP000019763};
RN   [1] {ECO:0000313|EMBL:EZG51530.1, ECO:0000313|Proteomes:UP000019763}
RP   NUCLEOTIDE SEQUENCE.
RA   Omoto C.K., Sibley D., Venepally P., Hadjithomas M., Karamycheva S.,
RA   Brunk B., Roos D., Caler E., Lorenzi H.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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:EZG51530.1}.
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DR   EMBL; AFNH02000926; EZG51530.1; -; Genomic_DNA.
DR   RefSeq; XP_011131968.1; XM_011133666.1.
DR   AlphaFoldDB; A0A023B2Q7; -.
DR   EnsemblProtists; EZG51530; EZG51530; GNI_124390.
DR   GeneID; 22914389; -.
DR   VEuPathDB; CryptoDB:GNI_124390; -.
DR   eggNOG; KOG0024; Eukaryota.
DR   OMA; AMYGHRD; -.
DR   OrthoDB; 948431at2759; -.
DR   Proteomes; UP000019763; Unassembled WGS sequence.
DR   GO; GO:0106322; F:S-(hydroxymethyl)glutathione dehydrogenase NAD activity; IEA:UniProtKB-EC.
DR   GO; GO:0106321; F:S-(hydroxymethyl)glutathione dehydrogenase NADP activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF1; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G03930)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EZG51530.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019763}.
FT   DOMAIN          57..176
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   REGION          288..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          514..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..548
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..578
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   578 AA;  62742 MW;  7019081E6F3C07F7 CRC64;
     MMNAAANLAE RVLGHTNTDC KTEGEVSATE SMLACTWQGK SKLEMREVPR PTITDDEDAI
     IRTTGSTVCG SDLHLFKGDM VSMKTNDIMG HECMGIVEDI GPAVTTVKKG DRVVLAFNVA
     CGKCEYCNKQ LYTACDNTNN SRVMEKLYGH KTAGILGYSH MLAGYPGCQA EYVRALYANT
     NLLKVPDQMT DEQALLLADI VPTSYHAVSD TGVQEGDVVG VWGCGPIGML VVQWLVNVFK
     ASRVIVIDSV QDRLDLVKER FDVETINFEK TKNVVAAIQE LTAKDQGERL SVASSPNAPE
     DIDIGKSVDI EGSKPEVEGE KEGEGEESKT GAGLKSSDSK GLRSSESKGD GKGEKKTEYI
     NGGLDRAIDC GAFRYTKGIM HKLERALAFE TDSSEVINEM IRATKKFGTI GLIADYVGYC
     NHLLIGGIME KGIRMVGCGQ APIQRYWTTC IEHIMSGRFD PTVVYSHRAS LEQTPLVYKL
     FDNKQMWKVF LETKASNPPT PGLPTLRVLS ESKSAKVDAT AKPSSSKSLK PSKSHGADTG
     DHKKNIKKAH TIGTTKKKSK SSANDGTASP ATEQEPNN
//