SWISSPROT: C8U2W4_ECO10

ID   C8U2W4_ECO10            Unreviewed;       362 AA.
AC   C8U2W4;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   SubName: Full=Predicted oxidoreductase {ECO:0000313|EMBL:BAI29472.1};
GN   Name=ybdH {ECO:0000313|EMBL:BAI29472.1};
GN   OrderedLocusNames=ECO103_0608 {ECO:0000313|EMBL:BAI29472.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29472.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29472.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-
CC       1};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010958; BAI29472.1; -; Genomic_DNA.
DR   RefSeq; WP_001120470.1; NC_013353.1.
DR   EnsemblBacteria; BAI29472; BAI29472; ECO103_0608.
DR   KEGG; eoh:ECO103_0608; -.
DR   HOGENOM; HOG000031783; -.
DR   KO; K08317; -.
DR   OMA; GHCSERD; -.
DR   BioCyc; ECOL585395:ECO103_RS03170-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR016205; Glycerol_DH.
DR   PANTHER; PTHR43616; PTHR43616; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
PE   4: Predicted;
DR   PRODOM; C8U2W4.
DR   SWISS-2DPAGE; C8U2W4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000112-1};
KW   NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT   DOMAIN       12    348       Fe-ADH. {ECO:0000259|Pfam:PF00465}.
FT   NP_BIND      96    100       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   METAL       173    173       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR000112-1}.
FT   METAL       257    257       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR000112-1}.
FT   METAL       274    274       Zinc; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR000112-1}.
FT   BINDING     127    127       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   BINDING     129    129       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000112-3}.
FT   BINDING     133    133       NAD. {ECO:0000256|PIRSR:PIRSR000112-3}.
SQ   SEQUENCE   362 AA;  39052 MW;  08660FEA5A058DFD CRC64;
     MPHNPIRVVV GPANYFSHPG SFNYLNDFFT DEQLSRAVWI YGKRAIAAAQ TKLPPAFGLP
     GAKHILFRGH CSESDVQQLA AESGDDRSVV IGVGGGALLD TAKALARRLG LPFVAAPTIA
     ATCAAWTPLS VWYNDAGQAL HYEIFDDANF MVLVEPEIIL NAPQQYLLAG IGDTLAKWYE
     AVVLAPQPET LPLTVRLGIN NAQAIRDVLL NSSEQALADQ QNQQLTQSFC DVVDAIIAGG
     GMVGGLGDRF TRVAAAHAVH NGLTVLPQTE KFLHGTKVAY GILVQSALLG QDDVLAQLTG
     AYQRFHLPTT LAELEVDINN QAEIDKVIAH TLRPVESIHY LPVTLTPDTL RAAFEKVESF
     KA
//