(data stored in ACNUC7421 zone)

SWISSPROT: B7UKP3_ECO27

ID   B7UKP3_ECO27            Unreviewed;       362 AA.
AC   B7UKP3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   SubName: Full=Predicted oxidoreductase {ECO:0000313|EMBL:CAS08050.1};
GN   Name=ybdH {ECO:0000313|EMBL:CAS08050.1};
GN   OrderedLocusNames=E2348C_0502 {ECO:0000313|EMBL:CAS08050.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08050.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08050.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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};
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DR   EMBL; FM180568; CAS08050.1; -; Genomic_DNA.
DR   RefSeq; WP_001120448.1; NC_011601.1.
DR   EnsemblBacteria; CAS08050; CAS08050; E2348C_0502.
DR   KEGG; ecg:E2348C_0502; -.
DR   HOGENOM; HOG000031783; -.
DR   KO; K08317; -.
DR   OMA; GHCSERD; -.
DR   BioCyc; ECOL574521:E2348C_RS02640-MONOMER; -.
DR   Proteomes; UP000008205; 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; B7UKP3.
DR   SWISS-2DPAGE; B7UKP3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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    347       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;  39310 MW;  FF00BB380CFC44FF CRC64;
     MPHNPIRVVV GPANYFSHPG SFNHLHDFFT DEQLSRTVWI YGERAIAAAQ TKLPPAFELP
     RVKHILFRGH CSESDVQQLA AESGDDRSVV IGVGGGALLD TAKALARRLG LPFVAVPTIA
     ATCAAWTPLS VWYNDAGQAL HYEIFDDANF MVLVEPEIIL NAPQEYLLAG IGDTLAKWYE
     AVVLAPQPET LPLTVRLGIN NAQAIRDVLL NSSEQALADQ QNQQLTQSFC DVVDAIIAGG
     GMVGGLGDRF TRVAAAHAVH NGLTVLPQTE KFLHGTKVAY GILVQSALLG QDDVLAQLTG
     AYQRFHLPTT LAELEVDINN QVEIDKMIAH TLRPVESIHY LPVTLTPGTL RAAFEKVESF
     KA
//

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