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Aniline dioxygenase reductase component

 Q44253_9GAMM            Unreviewed;       336 AA.
Q44253; Q7DL05;
01-NOV-1996, integrated into UniProtKB/TrEMBL.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 100.
SubName: Full=Aniline dioxygenase reductase component {ECO:0000313|EMBL:BAA13014.1};
Name=atdA5 {ECO:0000313|EMBL:BAA23552.1};
Acinetobacter sp. YAA.
Plasmid pYA1 {ECO:0000313|EMBL:BAA13014.1}.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Moraxellaceae; Acinetobacter.
NCBI_TaxID=278934 {ECO:0000313|EMBL:BAA13014.1};
[1] {ECO:0000313|EMBL:BAA13014.1}
NUCLEOTIDE SEQUENCE.
STRAIN=YAA {ECO:0000313|EMBL:BAA13014.1};
PLASMID=pYA1 {ECO:0000313|EMBL:BAA13014.1};
Fujii T., Takeo M., Maeda Y.;
"Plasmid-encoded genes specifying aniline oxidation from Acinetobacter
sp. strain YAA.";
Microbiology (Mosc.) 143:93-99(1997).
[2] {ECO:0000313|EMBL:BAA13014.1}
NUCLEOTIDE SEQUENCE.
STRAIN=YAA {ECO:0000313|EMBL:BAA13014.1};
PLASMID=pYA1 {ECO:0000313|EMBL:BAA13014.1};
Takeo M., Fujii T., Maeda Y.;
"Sequence analysis of the genes encoding a multicomponent dioxygenase
involved in oxidation of aniline and o-toluidine in Acinetobacter sp.
strain YAA.";
J. Ferment. Bioeng. 85:17-24(1998).
[3] {ECO:0000313|EMBL:BAA23552.1}
NUCLEOTIDE SEQUENCE.
STRAIN=YAA {ECO:0000313|EMBL:BAA23552.1};
Takeo M., Fujii T., Takenaka K., Maeda Y.;
"Cloning and sequencing of a gene cluster for the meta-cleavage
pathway of aniline degradation in Acinetobacter sp. strain YAA.";
J. Ferment. Bioeng. 85:514-517(1998).
[4] {ECO:0000313|EMBL:BAA23552.1}
NUCLEOTIDE SEQUENCE.
STRAIN=YAA {ECO:0000313|EMBL:BAA23552.1};
PubMed=17617714; DOI=10.1271/bbb.70079;
Takeo M., Nishimura M., Shirai M., Takahashi H., Negoro S.;
"Purification and characterization of catechol 2,3-dioxygenase from
the aniline degradation pathway of Acinetobacter sp. YAA and its
mutant enzyme, which resists substrate inhibition.";
Biosci. Biotechnol. Biochem. 71:1668-1675(2007).
[5] {ECO:0000313|EMBL:BAA13014.1}
NUCLEOTIDE SEQUENCE.
STRAIN=YAA {ECO:0000313|EMBL:BAA13014.1};
PLASMID=pYA1 {ECO:0000313|EMBL:BAA13014.1};
PubMed=23893114; DOI=10.1128/JB.00397-13;
Takeo M., Ohara A., Sakae S., Okamoto Y., Kitamura C., Kato D.,
Negoro S.;
"Function of a glutamine synthetase-like protein in bacterial aniline
oxidation via gamma-glutamylanilide.";
J. Bacteriol. 195:4406-4414(2013).
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EMBL; D86080; BAA13014.1; -; Genomic_DNA.
EMBL; AB008831; BAA23552.1; -; Genomic_DNA.
ProteinModelPortal; Q44253; -.
BioCyc; MetaCyc:MONOMER-15721; -.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd00207; fer2; 1.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR012675; Beta-grasp_dom.
InterPro; IPR017927; Fd_Rdtase_FAD-bd.
InterPro; IPR008333; OxRdtase_FAD-bd_dom.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR001221; Phe_hydroxylase.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00970; FAD_binding_6; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF00175; NAD_binding_1; 1.
PRINTS; PR00410; PHEHYDRXLASE.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51384; FAD_FR; 1.
4: Predicted;
2Fe-2S {ECO:0000256|SAAS:SAAS00660781};
Dioxygenase {ECO:0000313|EMBL:BAA13014.1};
FAD {ECO:0000256|SAAS:SAAS00486465};
Flavoprotein {ECO:0000256|SAAS:SAAS00486465};
Iron {ECO:0000256|SAAS:SAAS00660781};
Iron-sulfur {ECO:0000256|SAAS:SAAS00660781};
Metal-binding {ECO:0000256|SAAS:SAAS00660781};
Oxidoreductase {ECO:0000313|EMBL:BAA13014.1};
Plasmid {ECO:0000313|EMBL:BAA13014.1}.
DOMAIN 1 104 FAD-binding FR-type.
{ECO:0000259|PROSITE:PS51384}.
DOMAIN 247 336 2Fe-2S ferredoxin-type.
{ECO:0000259|PROSITE:PS51085}.
SEQUENCE 336 AA; 37160 MW; C8F535524AD8C22A CRC64;
MNTLKFRVID KIAETKESFS FVLKPLDGVL AEHSPGKYLP IKIRTEKGLL FRSYSLSSSA
SANEDFKITV KRERGGRGSN WLCDNVKVGD FIETLPPAGS FHPQNWDRDF VFFAGGSGIT
PVISIIKTAL NRHKNRIKLF YANSSESSII FHKELKDLCL QFPDRLDIQF WLDDEKGIPT
SIAFEQYIDD ALEVEYFLCG PAPFMGGVEN FLIESKVPPG LITKESFAGS VSDDNGDTVE
SSAEKDVTVN FMLNGIKNSV MCSEDDFILN EIIKAGINVP SSCCAGNCGS CMCLLVSGDV
ILESNTVLDA SDEEDGWILA CRSKPRSKNI EISFDQ


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