ID Q5QZ12_IDILO Unreviewed; 188 AA.
AC Q5QZ12;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Putative NAD(P)H nitroreductase {ECO:0000256|PIRNR:PIRNR000232};
DE EC=1.-.-.- {ECO:0000256|PIRNR:PIRNR000232};
GN OrderedLocusNames=IL1328 {ECO:0000313|EMBL:AAV82168.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82168.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82168.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRSR:PIRSR000232-1};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|PIRSR:PIRSR000232-1};
CC -!- SIMILARITY: Belongs to the nitroreductase family.
CC {ECO:0000256|ARBA:ARBA00007118, ECO:0000256|PIRNR:PIRNR000232}.
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DR EMBL; AE017340; AAV82168.1; -; Genomic_DNA.
DR RefSeq; WP_011234574.1; NC_006512.1.
DR AlphaFoldDB; Q5QZ12; -.
DR STRING; 283942.IL1328; -.
DR KEGG; ilo:IL1328; -.
DR eggNOG; COG0778; Bacteria.
DR HOGENOM; CLU_070764_5_0_6; -.
DR OrthoDB; 9804207at2; -.
DR Proteomes; UP000001171; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02135; YdjA-like; 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 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.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000232};
KW FMN {ECO:0000256|PIRNR:PIRNR000232, ECO:0000256|PIRSR:PIRSR000232-1};
KW NAD {ECO:0000256|PIRNR:PIRNR000232}; NADP {ECO:0000256|PIRNR:PIRNR000232};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000232};
KW Reference proteome {ECO:0000313|Proteomes:UP000001171}.
FT DOMAIN 18..161
FT /note="Nitroreductase"
FT /evidence="ECO:0000259|Pfam:PF00881"
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:0000256|PIRSR:PIRSR000232-1"
FT BINDING 35
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000232-1"
FT BINDING 39
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR000232-1"
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:0000256|PIRSR:PIRSR000232-1"
SQ SEQUENCE 188 AA; 20778 MW; AFAEBE5A1D18721D CRC64;
MNAEELLTSR SSMPRLSEPG PTIEQLELIK AAAVRAPDHM GLTPYQFIQF QGKERQVLAD
IYQQAARLSD FSETVIEQAG QLPFRAPTII VSCLRFQEHP KVPRDEQLCT VACATHGMQQ
AAFAQGIGAI WRTGWMAEDD FIKEQLGLSV DDAIVGFLYV GTPAVPTPIK PQKDSSPFFM
NGNDLVLD
//
