ID A0A0U2X2Q9_9ACTN Unreviewed; 393 AA.
AC A0A0U2X2Q9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Phenylacetate-CoA oxygenase {ECO:0000313|EMBL:ALV38090.1};
GN ORFNames=AS200_43180 {ECO:0000313|EMBL:ALV38090.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV38090.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV38090.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV38090.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP013743; ALV38090.1; -; Genomic_DNA.
DR RefSeq; WP_058927666.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U2X2Q9; -.
DR STRING; 1725411.AS200_43180; -.
DR KEGG; scx:AS200_43180; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd06214; PA_degradation_oxidoreductase_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 27..131
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 303..393
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 393 AA; 41827 MW; F9446E5F90BA2D70 CRC64;
MNTPATSPTV LRPETSAEQP VPGGQSPRWH SATVGEVCRL TPDAVAVTLE VPARLREVFA
HRPGQHVIVR YRRADGELRR AYSLCPPPHD PTALRLVIKR GAPDGFGAHA ARLSPGDRLE
LSSPTGHFTL PDVHGAHHVL IAGGSGITPL AALAADALLR DTTCRVSLVH SVPTAAHALL
SDELAALKDT FLDRFSVLYV LTREEQAPGG GPFRGRIDAD MLSRLLTALD AEPAEDTSFA
LCGPPEMIAT IRRCLDAWGA PPSLVRWELF TAGPTTTTPA ADPSPTRPPA DSTSATSPAP
GTSHITALLG GHRRHTTVGP HDTVILDALL RAHPDVPYAC REGVCGSCRA KILSGRVRAD
HQHALDDRDR AAGYTLVCRA RPDTAEVVLD FDA
//
