(data stored in SCRATCH zone)

SWISSPROT: C8U219_ECO10

ID   C8U219_ECO10            Unreviewed;       349 AA.
AC   C8U219;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   SubName: Full=Predicted oxidoreductase, Zn-dependent and NAD(P)-binding {ECO:0000313|EMBL:BAI29177.1};
GN   Name=yahK {ECO:0000313|EMBL:BAI29177.1};
GN   OrderedLocusNames=ECO103_0307 {ECO:0000313|EMBL:BAI29177.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29177.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29177.1, 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|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; AP010958; BAI29177.1; -; Genomic_DNA.
DR   RefSeq; WP_000692754.1; NC_013353.1.
DR   SMR; C8U219; -.
DR   EnsemblBacteria; BAI29177; BAI29177; ECO103_0307.
DR   KEGG; eoh:ECO103_0307; -.
DR   HOGENOM; HOG000294667; -.
DR   KO; K13979; -.
DR   OMA; YRFSIDM; -.
DR   BioCyc; ECOL585395:ECO103_RS01605-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U219.
DR   SWISS-2DPAGE; C8U219.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN        7    342       PKS_ER. {ECO:0000259|SMART:SM00829}.
SQ   SEQUENCE   349 AA;  37978 MW;  AD0E2DF4D43C9B09 CRC64;
     MKIKAVGAYS AKQPLEPMDI TRREPGPNDV KIEIAYCGVC HSDLHQVRSE WAGTVYPCVP
     GHEIVGRVVA VGDQVEKYAP GDLVGVGCIV DSCKHCEECE DGLENYCDHM TGTYNSPTPD
     EPGHTLGGYS QQIVVHERYV LRIRHPQEQL AAVAPLLCAG ITTYSPLRHW QAGPGKKVGV
     VGIGGLGHMG IKLAHAMGAH VVAFTTSEAK REAAKALGAD EVVNSRNADE MAAHLKSFDF
     ILNTVAAPHN LDDFTTLLKR DGTMTLVGAP ATPHKSPEVF NLIMKRRAIA GSMIGGIPET
     QEMLDFCAEH GIVADIEMIR ADQINEAYER MLRGDVKYRF VIDNRTLTD
//

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