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Database: UniProt
Entry: A0A101SX96_9ACTN
LinkDB: A0A101SX96_9ACTN
Original site: A0A101SX96_9ACTN 
ID   A0A101SX96_9ACTN        Unreviewed;       358 AA.
AC   A0A101SX96;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:KUN81846.1};
GN   ORFNames=AQJ64_21925 {ECO:0000313|EMBL:KUN81846.1};
OS   Streptomyces griseoruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN81846.1, ECO:0000313|Proteomes:UP000052982};
RN   [1] {ECO:0000313|EMBL:KUN81846.1, ECO:0000313|Proteomes:UP000052982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN81846.1,
RC   ECO:0000313|Proteomes:UP000052982};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT   for the species Streptomyces griseoruber.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUN81846.1}.
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DR   EMBL; LMWW01000034; KUN81846.1; -; Genomic_DNA.
DR   RefSeq; WP_055636203.1; NZ_LIQS01000345.1.
DR   AlphaFoldDB; A0A101SX96; -.
DR   STRING; 1943.AQJ64_21925; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000052982; Unassembled WGS sequence.
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:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 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}.
FT   DOMAIN          7..117
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          269..358
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   358 AA;  38541 MW;  0F752BBB82195F69 CRC64;
     MARAVTARFH PLPVAAVDRL TDDSVALTLA VPEALREEYR HAAGQHLALR RIADGTEIRR
     TYSICSSAPD PAGEGPRTLR VGVRLVDGGA FSTYALKEIG VGDELEVMTP AGRFTLDPAP
     GLYAAIVGGS GITPVLSIVS TLLAREPDAR FCLIRGDRTA ASTMFLEEVA DLKDRYPERL
     HLVTVLSREE QQAGLPSGRL DRERLTGLLP ALLPVAEVAG WFLCGPFGLV QGAERTLREL
     GVARSRIHEE IFHVDDAAPT TRAAAPAHAT VTARLDGRGG SWPVRDGESV LDTVLRNRPD
     APYACKGGVC GTCRAFLVSG EVRMDRNFAL EPEETEAGYV LACQSHPVTE AVEVDFDR
//
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