(data stored in SCRATCH zone)

SWISSPROT: C6AYB1_RHILS

ID   C6AYB1_RHILS            Unreviewed;       211 AA.
AC   C6AYB1;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 55.
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=Rleg_0023 {ECO:0000313|EMBL:ACS54335.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54335.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54335.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54335.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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:SAAS00096932}.
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:SAAS00345012}.
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; CP001622; ACS54335.1; -; Genomic_DNA.
DR   RefSeq; WP_012755773.1; NC_012850.1.
DR   ProteinModelPortal; C6AYB1; -.
DR   EnsemblBacteria; ACS54335; ACS54335; Rleg_0023.
DR   KEGG; rlg:Rleg_0023; -.
DR   HOGENOM; HOG000247892; -.
DR   KO; K01118; -.
DR   OMA; LRINRTF; -.
DR   OrthoDB; POG091H0DQS; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008752; F:FMN reductase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016652; F:oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor; IEA:UniProtKB-HAMAP.
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_dom.
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; C6AYB1.
DR   SWISS-2DPAGE; C6AYB1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
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    181       Flavodoxin_2. {ECO:0000259|Pfam:PF02525}.
SQ   SEQUENCE   211 AA;  23245 MW;  C379B1FAFE615B5A CRC64;
     MRVLHVSCSP RGEASESYRL SQQIISQLRQ SDPDTTVIDR VIGQGVIPPI DEDYAVSQGS
     SKDVSQLGSM AKSEELILEL ETADVVVIST PMHNLTLPAT LKLWIDHIVR TRRTFNISKF
     GKVGTLQDRP VFVAISSGGR FSGEHPQQPD FLTPYLTAIL GMIGLHNVAI FSVQGTGSHV
     NELASIRRNT DQLVREHFAS FHPDLIAVPT Y
//

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