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Database: UniProt
Entry: X7FCE7_9RHOB
LinkDB: X7FCE7_9RHOB
Original site: X7FCE7_9RHOB 
ID   X7FCE7_9RHOB            Unreviewed;       358 AA.
AC   X7FCE7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:ETX29781.1};
GN   ORFNames=RISW2_21250 {ECO:0000313|EMBL:ETX29781.1};
OS   Roseivivax isoporae LMG 25204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX29781.1, ECO:0000313|Proteomes:UP000023430};
RN   [1] {ECO:0000313|EMBL:ETX29781.1, ECO:0000313|Proteomes:UP000023430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX29781.1,
RC   ECO:0000313|Proteomes:UP000023430};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:ETX29781.1}.
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DR   EMBL; JAME01000007; ETX29781.1; -; Genomic_DNA.
DR   RefSeq; WP_043768137.1; NZ_JAME01000007.1.
DR   AlphaFoldDB; X7FCE7; -.
DR   STRING; 1449351.RISW2_21250; -.
DR   PATRIC; fig|1449351.3.peg.1285; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000023430; 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   GO; GO:0010124; P:phenylacetate catabolic process; 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; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR011884; PA_CoA_Oase5.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   NCBIfam; TIGR02160; PA_CoA_Oxy5; 1.
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; PR00406; CYTB5RDTASE.
DR   PRINTS; PR00371; FPNCR.
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:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023430}.
FT   DOMAIN          2..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          270..358
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   358 AA;  39329 MW;  8CFFC49ECAF4279B CRC64;
     MPRFHPLTVT EVRKTTRDAV VVTLAPRPED TASFAFTQGQ YLTFRREFDG EELRRSYSIC
     AGADEGVLRV GIKRVEGGAF STWANEGLRA GDTLEAMPPM GRFFTPLDPH AARHYLAFAG
     GSGITPVLSL VRTMLDREPQ ARVTLVYANR QVGSIMFREE LEDLKNVHLG RLSVIHVLES
     EAQEIDLFSG RIDAAKMDAL FAHWIEPSDV DTAFICGPEP MMLTIAESLR AHGLTDAQIK
     FELFASAQPG RARTRAVSQA ADRAGAMCEA EVTLDGATRT FRFPKDGTAL LDAALENAMD
     VPYSCKAGVC STCRAKVLEG EVEMETNHAL EDYEVRAGYV LTCQCVPLSD RLVVSYDA
//
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