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Database: UniProt
Entry: A0A2G8SNW2_9APHY
LinkDB: A0A2G8SNW2_9APHY
Original site: A0A2G8SNW2_9APHY 
ID   A0A2G8SNW2_9APHY        Unreviewed;       384 AA.
AC   A0A2G8SNW2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 15.
DE   RecName: Full=Alcohol dehydrogenase iron-type/glycerol dehydrogenase GldA domain-containing protein {ECO:0000259|Pfam:PF00465};
GN   ORFNames=GSI_02167 {ECO:0000313|EMBL:PIL35440.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL35440.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL35440.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL35440.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(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:PIL35440.1}.
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DR   EMBL; AYKW01000003; PIL35440.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8SNW2; -.
DR   STRING; 1077348.A0A2G8SNW2; -.
DR   OrthoDB; 5473018at2759; -.
DR   Proteomes; UP000230002; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08192; MAR-like; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF97; FE-ADH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT   DOMAIN          21..365
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   384 AA;  40808 MW;  658A3135DC101170 CRC64;
     MSITSPNLSG FYAYTETLKG VHYGPGSVKT ALPKLLASVG GNRAFIITGK TLYTATNVVK
     TVENVLKEHN AYSATFYEIG QHAPIAGVRN GVKAFKDAGA DVIVSVGGGS PVDAAKAILY
     FIQQETGGRC LPQIAIPTTL SAAEYSIGAG FTNEQGEKSR ITSTELAPAG IILDAELTLA
     TPERLWLSTG LRALDHAVEN LYRPGPGVPI PLKYLCCVAI ADLFTYLPKS KANAQDVEVR
     QRLQVASWMS VWPIKDERRG PLGLSHALGH KLGATYGIPH GITSCLTLAP VVNLKAEVAS
     QADKEALAAV LFYLRQESTG SVNGDVRKLS SLIQQLVVDL GLKSTLSEYN VPNDDLPKIA
     QLAVGGDNND PLVNNVISLL QGIF
//
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