ID C9Y4J9_CROTZ Unreviewed; 383 AA.
AC C9Y4J9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Probable alcohol dehydrogenase {ECO:0000313|EMBL:CBA26858.1};
DE EC=1.1.1.1 {ECO:0000313|EMBL:CBA26858.1};
DE EC=1.1.1.202 {ECO:0000313|EMBL:CBA26858.1};
DE EC=1.1.1.244 {ECO:0000313|EMBL:CBA26858.1};
GN Name=yiaY {ECO:0000313|EMBL:CBA26858.1};
GN OrderedLocusNames=Ctu_01340 {ECO:0000313|EMBL:CBA26858.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA26858.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; FN543093; CBA26858.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y4J9; -.
DR KEGG; ctu:CTU_01340; -.
DR PATRIC; fig|693216.3.peg.124; -.
DR HOGENOM; CLU_007207_0_0_6; -.
DR Proteomes; UP000002069; Chromosome.
DR GO; GO:0047516; F:1,3-propanediol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0050093; F:methanol dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd08188; PDDH; 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:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CBA26858.1}.
FT DOMAIN 12..375
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 383 AA; 40636 MW; C518731FDEDD7307 CRC64;
MTASVFYIPS INMIGMNSLD EALKTACEYG YRNALIVTDG MLSALGMAGQ LKEMLAQKGM
QSVIFDGTHP NPTTENVEAG LSMLRAHRCD CVISLGGGSP HDCAKGIALV AANGGDIRDY
EGVDRSRKPQ LPMIAINTTA GTASEMTRFC IITDQERHVK MAIVDKHVTP VMSVNDPALM
VGMPKSLTAA TGMDALTHAI EAYVSTAATP VTDACALKAI AMITRSLPQA VEEGDNVAAR
EAMAWAQFMA GMAFNNASLG YVHAMAHQLG GFYDLPHGVC NAILLPHVQR FNSAVAAHRL
RDCAQAMGVD VSAMNDAEGA DACIAAICAL ARRVHIPAGL RELRVRDEDI STLADNALKD
ACGFTNPVQA NHAEIMAIYR AAM
//