ID   YGHA_ECO57              Reviewed;         294 AA.
AC   P0AG85; P25887; Q46852;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Uncharacterized oxidoreductase YghA;
DE            EC=1.-.-.-;
GN   Name=yghA; OrderedLocusNames=Z4356, ECs3887;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
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., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG58139.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37310.1; -; Genomic_DNA.
DR   PIR; G85959; G85959.
DR   PIR; G91114; G91114.
DR   RefSeq; NP_311914.1; NC_002695.1.
DR   RefSeq; WP_000018760.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AG85; -.
DR   SMR; P0AG85; -.
DR   STRING; 155864.EDL933_4225; -.
DR   EnsemblBacteria; AAG58139; AAG58139; Z4356.
DR   EnsemblBacteria; BAB37310; BAB37310; ECs_3887.
DR   GeneID; 66673100; -.
DR   GeneID; 916290; -.
DR   KEGG; ece:Z4356; -.
DR   KEGG; ecs:ECs_3887; -.
DR   PATRIC; fig|386585.9.peg.4055; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_4_0_6; -.
DR   OMA; WEVANVI; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Acetylation; Oxidoreductase; Reference proteome.
FT   CHAIN           1..294
FT                   /note="Uncharacterized oxidoreductase YghA"
FT                   /id="PRO_0000054838"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        199
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         53..77
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         39
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   294 AA;  31488 MW;  34B8742A16278811 CRC64;
     MSHLKDPTTQ YYTGEYPKQK QPTPGIQAKM TPVPDCGEKT YVGSGRLKDR KALVTGGDSG
     IGRAAAIAYA REGADVAISY LPVEEEDAQD VKKIIEECGR KAVLLPGDLS DEKFARSLVH
     EAHKALGGLD IMALVAGKQV AIPDIADLTS EQFQKTFAIN VFALFWLTQE AIPLLPKGAS
     IITTSSIQAY QPSPHLLDYA ATKAAILNYS RGLAKQVAEK GIRVNIVAPG PIWTALQISG
     GQTQDKIPQF GQQTPMKRAG QPAELAPVYV YLASQESSYV TAEVHGVCGG EHLG