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Database: UniProt
Entry: W9HFC5_9PROT
LinkDB: W9HFC5_9PROT
Original site: W9HFC5_9PROT 
ID   W9HFC5_9PROT            Unreviewed;       391 AA.
AC   W9HFC5;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EWY42603.1};
GN   ORFNames=N825_01605 {ECO:0000313|EMBL:EWY42603.1};
OS   Skermanella stibiiresistens SB22.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Skermanella.
OX   NCBI_TaxID=1385369 {ECO:0000313|EMBL:EWY42603.1, ECO:0000313|Proteomes:UP000019486};
RN   [1] {ECO:0000313|EMBL:EWY42603.1, ECO:0000313|Proteomes:UP000019486}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB22 {ECO:0000313|EMBL:EWY42603.1,
RC   ECO:0000313|Proteomes:UP000019486};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Skermanella stibiiresistens.";
RL   Submitted (AUG-2013) 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}.
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:EWY42603.1}.
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DR   EMBL; AVFL01000001; EWY42603.1; -; Genomic_DNA.
DR   RefSeq; WP_037446036.1; NZ_AVFL01000001.1.
DR   AlphaFoldDB; W9HFC5; -.
DR   STRING; 1385369.N825_01605; -.
DR   PATRIC; fig|1385369.3.peg.313; -.
DR   OrthoDB; 9773078at2; -.
DR   Proteomes; UP000019486; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08283; FDH_like_1; 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; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR   PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 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|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019486};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          26..149
FT                   /note="Alcohol dehydrogenase-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08240"
FT   DOMAIN          197..270
FT                   /note="Alcohol dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00107"
SQ   SEQUENCE   391 AA;  42811 MW;  BDDBE8B89A1D0104 CRC64;
     MKALVWHGKE DIRYDTVSDP EIEHPRDAIV KVTSCAICGS DLHLFHNFIP AMMPGDIMGH
     EMMGEVVEVG SGVNGHLKKG DRVVVPFTII CGECDQCKRG NFSVCQNSNR KKHLADKVFG
     HATAGLFGYT HLTGGYPGGQ AEYLRVPFAD ATHIKVPDGI PDEKLLFLGD IFPTGWQAAV
     QCDIQPTDTV AIWGCGPVGQ MAIRSAVLLG AQRVVAIDRV PERLEMAEAG GAITINFDEE
     SVVERLNELT GGEGPEKCID AVGLEAHVTP SLPDTVYDRA KQMVGMESDR PHVLREMIYV
     CRPAGVISIP GVYGGLVDKI PMGQLMNKGL TIRTGQTHVN RWTDDLLRRI EEGQIDPSFV
     ITHTVSLEEG PEMYKVFRDK QDSCVKVVLK P
//
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