ID YDJA_ECOLI Reviewed; 183 AA. AC P0ACY1; P24250; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 22-NOV-2005, sequence version 1. DT 02-SEP-2026, entry version 127. DE RecName: Full=Putative NAD(P)H nitroreductase YdjA; DE EC=1.-.-.-; GN Name=ydjA; OrderedLocusNames=b1765, JW1754; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1650339; DOI=10.1128/jb.173.16.4983-4993.1991; RA Sawers G., Heider J., Zehelein E., Boeck A.; RT "Expression and operon structure of the sel genes of Escherichia coli and RT identification of a third selenium-containing formate dehydrogenase RT isoenzyme."; RL J. Bacteriol. 173:4983-4993(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., RA Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [3] 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 [4] 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 [5] 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FMN, COFACTOR, AND RP SUBUNIT. RX PubMed=18241886; DOI=10.1016/j.jmb.2008.01.004; RA Choi J.-W., Lee J., Nishi K., Kim Y.-S., Jung C.-H., Kim J.-S.; RT "Crystal structure of a minimal nitroreductase, ydjA, from Escherichia coli RT K12 with and without FMN cofactor."; RL J. Mol. Biol. 377:258-267(2008). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:18241886}; CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:18241886}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18241886}. CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M68961; AAA24245.1; -; Genomic_DNA. DR EMBL; U00096; AAC74835.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15556.1; -; Genomic_DNA. DR PIR; A40360; A40360. DR RefSeq; NP_416279.1; NC_000913.3. DR RefSeq; WP_000339283.1; NZ_CP009789.1. DR PDB; 3BM1; X-ray; 2.00 A; A/B=1-183. DR PDB; 3BM2; X-ray; 2.10 A; A/B=1-183. DR AlphaFoldDB; P0ACY1; -. DR SMR; P0ACY1; -. DR BioGRID; 4259139; 171. DR DIP; DIP-31841N; -. DR FunCoup; P0ACY1; 186. DR IntAct; P0ACY1; 11. DR STRING; 511145.b1765; -. DR jPOST; P0ACY1; -. DR PaxDb; 511145-b1765; -. DR EnsemblBacteria; AAC74835; AAC74835; b1765. DR GeneID; 93775982; -. DR GeneID; 945964; -. DR KEGG; ecj:JW1754; -. DR KEGG; eco:b1765; -. DR KEGG; ecoc:C3026_10075; -. DR PATRIC; fig|1411691.4.peg.489; -. DR EchoBASE; EB1124; -. DR eggNOG; COG0778; Bacteria. DR HOGENOM; CLU_070764_5_0_6; -. DR InParanoid; P0ACY1; -. DR OMA; LTEWFAY; -. DR OrthoDB; 9804207at2; -. DR PhylomeDB; P0ACY1; -. DR BioCyc; EcoCyc:EG11134-MONOMER; -. DR EvolutionaryTrace; P0ACY1; -. DR PRO; PR:P0ACY1; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR CDD; cd02135; YdjA-like; 1. DR FunFam; 3.40.109.10:FF:000005; NAD(P)H nitroreductase; 1. DR Gene3D; 3.40.109.10; NADH Oxidase; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR InterPro; IPR026021; YdjA-like. DR NCBIfam; NF008088; PRK10828.1; 1. DR PANTHER; PTHR43821; NAD(P)H NITROREDUCTASE YDJA-RELATED; 1. DR PANTHER; PTHR43821:SF1; NAD(P)H NITROREDUCTASE YDJA-RELATED; 1. DR Pfam; PF00881; Nitroreductase; 1. DR PIRSF; PIRSF000232; YdjA; 1. DR SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1. DR PDBsum; 3BM1; -. DR PDBsum; 3BM2; -. PE 1: Evidence at protein level; KW 3D-structure; Flavoprotein; FMN; NAD; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1..183 FT /note="Putative NAD(P)H nitroreductase YdjA" FT /id="PRO_0000169002" FT BINDING 10..12 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:18241886" FT BINDING 35 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000269|PubMed:18241886" FT BINDING 39 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000269|PubMed:18241886" FT BINDING 121..126 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255" FT BINDING 131..133 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000269|PubMed:18241886" FT HELIX 3..9 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 16..18 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 19..21 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 23..33 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 46..51 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 53..69 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 73..81 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 86..94 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 104..123 FT /evidence="ECO:0007829|PDB:3BM1" FT TURN 124..126 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 128..132 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 135..138 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 140..145 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 153..163 FT /evidence="ECO:0007829|PDB:3BM1" FT HELIX 177..179 FT /evidence="ECO:0007829|PDB:3BM1" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:3BM1" SQ SEQUENCE 183 AA; 20059 MW; A69809EE378847CB CRC64; MDALELLINR RSASRLAEPA PTGEQLQNIL RAGMRAPDHK SMQPWHFFVI EGEGRERFSA VLEQGAIAAG SDDKAIDKAR NAPFRAPLII TVVAKCEENH KVPRWEQEMS AGCAVMAMQM AAVAQGFGGI WRSGALTESP VVREAFGCRE QDKIVGFLYL GTPQLKASTS INVPDPTPFV TYF //