(data stored in ACNUC7421 zone)

SWISSPROT: Q8XBU7_ECO57

ID   Q8XBU7_ECO57            Unreviewed;       362 AA.
AC   Q8XBU7; A0A0H3JCJ1; Q7AGR0;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAY-2019, entry version 122.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:BAB34061.1};
GN   Name=ybdH {ECO:0000313|EMBL:BAB34061.1};
GN   ORFNames=ECs_0638 {ECO:0000313|EMBL:BAB34061.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34061.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34061.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 /
RC   EHEC {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; BA000007; BAB34061.1; -; Genomic_DNA.
DR   RefSeq; NP_308665.1; NC_002695.1.
DR   RefSeq; WP_001120445.1; NZ_SDVX01000001.1.
DR   STRING; 155864.EDL933_0671; -.
DR   EnsemblBacteria; AAG54934; AAG54934; Z0742.
DR   EnsemblBacteria; BAB34061; BAB34061; BAB34061.
DR   GeneID; 916997; -.
DR   KEGG; ecs:ECs0638; -.
DR   PATRIC; fig|386585.9.peg.749; -.
DR   eggNOG; ENOG4107SCQ; Bacteria.
DR   eggNOG; COG0371; LUCA.
DR   KO; K08317; -.
DR   BioCyc; ECOO157:YBDH-MONOMER; -.
DR   Proteomes; UP000000558; 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; Q8XBU7.
DR   SWISS-2DPAGE; Q8XBU7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000112-1};
KW   NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558};
KW   Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
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;  39019 MW;  26814B7BA7CD690A CRC64;
     MPHNPIRVVV GPANYFSHPG SFNHLHDFFT DEQLSRAVWI YGVRAIAAAQ 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
//

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