YGIN_ECOLI
ID YGIN_ECOLI Reviewed; 104 AA.
AC P0ADU2; P40718; Q2M9H1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Probable quinol monooxygenase YgiN;
DE Short=QuMo;
DE EC=1.-.-.-;
GN Name=ygiN; OrderedLocusNames=b3029, JW2997;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7568050; DOI=10.1073/pnas.92.19.8950;
RA Chatterjee P.K., Sternberg N.L.;
RT "A general genetic approach in Escherichia coli for determining the
RT mechanism(s) of action of tumoricidal agents: application to DMP 840, a
RT tumoricidal agent.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8950-8954(1995).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP PROTEIN SEQUENCE OF 1-4.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9600841; DOI=10.1006/jmbi.1998.1726;
RA Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C.,
RA Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L.,
RA Hochstrasser D.F.;
RT "Protein identification with N and C-terminal sequence tags in proteome
RT projects.";
RL J. Mol. Biol. 278:599-608(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MENADIONE, FUNCTION,
RP AND SUBUNIT.
RX PubMed=15613473; DOI=10.1074/jbc.m412637200;
RA Adams M.A., Jia Z.;
RT "Structural and biochemical evidence for an enzymatic quinone redox cycle
RT in Escherichia coli: identification of a novel quinol monooxygenase.";
RL J. Biol. Chem. 280:8358-8363(2005).
CC -!- FUNCTION: Can oxidize menadiol to menadione.
CC {ECO:0000269|PubMed:15613473}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15613473}.
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DR EMBL; U18656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U28377; AAA69197.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76065.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77085.1; -; Genomic_DNA.
DR PIR; C65090; C65090.
DR RefSeq; NP_417501.1; NC_000913.3.
DR RefSeq; WP_000958598.1; NZ_STEB01000001.1.
DR PDB; 1R6Y; X-ray; 2.20 A; A=1-104.
DR PDB; 1TUV; X-ray; 1.70 A; A=1-104.
DR PDBsum; 1R6Y; -.
DR PDBsum; 1TUV; -.
DR AlphaFoldDB; P0ADU2; -.
DR SMR; P0ADU2; -.
DR BioGRID; 4262392; 5.
DR IntAct; P0ADU2; 2.
DR STRING; 511145.b3029; -.
DR SWISS-2DPAGE; P0ADU2; -.
DR jPOST; P0ADU2; -.
DR PaxDb; P0ADU2; -.
DR PRIDE; P0ADU2; -.
DR EnsemblBacteria; AAC76065; AAC76065; b3029.
DR EnsemblBacteria; BAE77085; BAE77085; BAE77085.
DR GeneID; 66673080; -.
DR GeneID; 947506; -.
DR KEGG; ecj:JW2997; -.
DR KEGG; eco:b3029; -.
DR PATRIC; fig|1411691.4.peg.3702; -.
DR EchoBASE; EB2525; -.
DR eggNOG; COG1359; Bacteria.
DR HOGENOM; CLU_131496_13_1_6; -.
DR InParanoid; P0ADU2; -.
DR OMA; HLQTAHM; -.
DR PhylomeDB; P0ADU2; -.
DR BioCyc; EcoCyc:EG12657-MON; -.
DR BioCyc; MetaCyc:EG12657-MON; -.
DR EvolutionaryTrace; P0ADU2; -.
DR PRO; PR:P0ADU2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0003824; F:catalytic activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0010447; P:response to acidic pH; IEP:EcoCyc.
DR InterPro; IPR007138; ABM_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR Pfam; PF03992; ABM; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS51725; ABM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..104
FT /note="Probable quinol monooxygenase YgiN"
FT /id="PRO_0000169408"
FT DOMAIN 2..100
FT /note="ABM"
FT CONFLICT 4
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1TUV"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1R6Y"
FT HELIX 16..33
FT /evidence="ECO:0007829|PDB:1TUV"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1TUV"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:1TUV"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:1TUV"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1TUV"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1TUV"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:1TUV"
SQ SEQUENCE 104 AA; 11532 MW; 46E7B5A11ADED1EA CRC64;
MLTVIAEIRT RPGQHHRQAV LDQFAKIVPT VLKEEGCHGY APMVDCAAGV SFQSMAPDSI
VMIEQWESIA HLEAHLQTPH MKAYSEAVKG DVLEMNIRIL QPGI
