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YGHA_ECOLI
ID   YGHA_ECOLI              Reviewed;         294 AA.
AC   P0AG84; P25887; Q2M9J4; Q46852;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Uncharacterized oxidoreductase YghA;
DE            EC=1.-.-.-;
GN   Name=yghA; OrderedLocusNames=b3003, JW2972;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-294.
RC   STRAIN=K12;
RX   PubMed=2670903; DOI=10.1128/jb.171.9.5117-5126.1989;
RA   Eick-Helmerich K., Braun V.;
RT   "Import of biopolymers into Escherichia coli: nucleotide sequences of the
RT   exbB and exbD genes are homologous to those of the tolQ and tolR genes,
RT   respectively.";
RL   J. Bacteriol. 171:5117-5126(1989).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; U28377; AAA69170.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76039.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77062.1; -; Genomic_DNA.
DR   EMBL; M28819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A65087; A65087.
DR   RefSeq; NP_417476.1; NC_000913.3.
DR   RefSeq; WP_000018760.1; NZ_STEB01000001.1.
DR   AlphaFoldDB; P0AG84; -.
DR   SMR; P0AG84; -.
DR   BioGRID; 4261414; 24.
DR   DIP; DIP-36027N; -.
DR   IntAct; P0AG84; 6.
DR   STRING; 511145.b3003; -.
DR   iPTMnet; P0AG84; -.
DR   jPOST; P0AG84; -.
DR   PaxDb; P0AG84; -.
DR   PRIDE; P0AG84; -.
DR   EnsemblBacteria; AAC76039; AAC76039; b3003.
DR   EnsemblBacteria; BAE77062; BAE77062; BAE77062.
DR   GeneID; 66673100; -.
DR   GeneID; 947478; -.
DR   KEGG; ecj:JW2972; -.
DR   KEGG; eco:b3003; -.
DR   PATRIC; fig|1411691.4.peg.3725; -.
DR   EchoBASE; EB1269; -.
DR   eggNOG; COG1028; Bacteria.
DR   HOGENOM; CLU_010194_4_0_6; -.
DR   InParanoid; P0AG84; -.
DR   OMA; WEVANVI; -.
DR   PhylomeDB; P0AG84; -.
DR   BioCyc; EcoCyc:EG11292-MON; -.
DR   BioCyc; MetaCyc:EG11292-MON; -.
DR   PRO; PR:P0AG84; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acetylation; Oxidoreductase; Reference proteome.
FT   CHAIN           1..294
FT                   /note="Uncharacterized oxidoreductase YghA"
FT                   /id="PRO_0000054837"
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:0000269|PubMed:18723842"
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
 
 
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