ID A0A2D3VJK5_9PEZI Unreviewed; 363 AA.
AC A0A2D3VJK5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Probable alcohol dehydrogenase, class V {ECO:0000313|EMBL:CZT22269.1};
GN ORFNames=RCC_08138 {ECO:0000313|EMBL:CZT22269.1};
OS Ramularia collo-cygni.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Ramularia.
OX NCBI_TaxID=112498 {ECO:0000313|EMBL:CZT22269.1, ECO:0000313|Proteomes:UP000225277};
RN [1] {ECO:0000313|EMBL:CZT22269.1, ECO:0000313|Proteomes:UP000225277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=URUG2 {ECO:0000313|EMBL:CZT22269.1,
RC ECO:0000313|Proteomes:UP000225277};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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DR EMBL; FJUY01000013; CZT22269.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2D3VJK5; -.
DR STRING; 112498.A0A2D3VJK5; -.
DR OrthoDB; 5353053at2759; -.
DR Proteomes; UP000225277; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF85; CINNAMYL ALCOHOL DEHYDROGENASE 6-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_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 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000225277};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 39..156
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 197..323
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 363 AA; 39566 MW; 01E46D3C42D697A5 CRC64;
MAAKEDYKFA GWMGIDKESA KGNMVWQEFP DDRKPFEETD VDIQITHSGI CGSDLHTLRS
GWGPTPYPVC VGHEIVGKAV RVGSKVEKGI KVGDRVGVGA QNLSCLKPDC EECSSGLENH
CTQTTNTFAG KYPDGSTSYG GYADYHRAPS HFVFKIPEGI DSADAAPMLC GGITVYSPLK
NNDCGPGKKV GIIGVGGLGH FGVLYAKALG ADKVVGISRR NDKREDVLKM GADEYIATEE
DKDWAKKHSR SLDLIICTVS SPSMPLMQYL QLLRVKGTFI QVGAPEDKLP DMNAFAFIAK
GVKFGGSMIG PPAQIEEMLK FTAEKNVKPW INKYSMKEAN KAIVDFEAGK ARYRISLVNE
HFL
//