(data stored in ACNUC7421 zone)

SWISSPROT: B2TF57_PARPJ

ID   B2TF57_PARPJ            Unreviewed;       224 AA.
AC   B2TF57;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=FMN-dependent NADH-azoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE            EC=1.7.-.- {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=Azo-dye reductase {ECO:0000256|HAMAP-Rule:MF_01216};
DE   AltName: Full=FMN-dependent NADH-azo compound oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216};
GN   Name=azoR {ECO:0000256|HAMAP-Rule:MF_01216};
GN   OrderedLocusNames=Bphyt_4351 {ECO:0000313|EMBL:ACD18728.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18728.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18728.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
CC   -!- FUNCTION: Catalyzes the reductive cleavage of azo bond in aromatic
CC       azo compounds to the corresponding amines. Requires NADH, but not
CC       NADPH, as an electron donor for its activity. {ECO:0000256|HAMAP-
CC       Rule:MF_01216, ECO:0000256|SAAS:SAAS00016147}.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01216};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01216};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01216,
CC       ECO:0000256|SAAS:SAAS00016163}.
CC   -!- SIMILARITY: Belongs to the azoreductase type 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01216, ECO:0000256|SAAS:SAAS00540904}.
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DR   EMBL; CP001053; ACD18728.1; -; Genomic_DNA.
DR   RefSeq; WP_012426244.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4351; -.
DR   EnsemblBacteria; ACD18728; ACD18728; Bphyt_4351.
DR   KEGG; bpy:Bphyt_4351; -.
DR   eggNOG; ENOG4105SB3; Bacteria.
DR   eggNOG; COG1182; LUCA.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; PPIGRDY; -.
DR   OrthoDB; 1402654at2; -.
DR   Proteomes; UP000001739; Chromosome 2.
DR   GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IEA:InterPro.
DR   Gene3D; 3.40.50.360; -; 1.
DR   HAMAP; MF_01216; Azoreductase_type1; 1.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR023048; NADH-azoreductase_FMN-depdnt.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2TF57.
DR   SWISS-2DPAGE; B2TF57.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001739};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01216,
KW   ECO:0000256|SAAS:SAAS00016150};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_01216, ECO:0000256|SAAS:SAAS00016179};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01216, ECO:0000256|SAAS:SAAS00016149};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01216,
KW   ECO:0000256|SAAS:SAAS00016167}.
FT   DOMAIN        1    195       Flavodoxin_2. {ECO:0000259|Pfam:PF02525}.
SQ   SEQUENCE   224 AA;  23817 MW;  37FDC558D5ADB7E1 CRC64;
     MRILLINASP HGEASHGYRF ADEIVGMLHG HAAPAASAIT VVERDLAAAP LPPIARDYAR
     AVTSRAPDTA HFDVSEQLIG EIETTDALII NTPMHNFTVP AALKLWIDYT LRIHRTFAST
     PEGKVGLMRD RPTIVIVGSG GVHSGERARQ TDFLTPYLRY ALGSIGIHSV QFLLLQGLVM
     GEATVAKALD AARVQLTGDA VFVSLAAQAS RCARTAAGST ARSA
//

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