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