ID A0A0F0HX55_9PSEU Unreviewed; 356 AA.
AC A0A0F0HX55;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:KJK60055.1};
GN ORFNames=UK12_01125 {ECO:0000313|EMBL:KJK60055.1};
OS Saccharothrix sp. ST-888.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK60055.1, ECO:0000313|Proteomes:UP000033409};
RN [1] {ECO:0000313|EMBL:KJK60055.1, ECO:0000313|Proteomes:UP000033409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-888 {ECO:0000313|EMBL:KJK60055.1,
RC ECO:0000313|Proteomes:UP000033409};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJK60055.1}.
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DR EMBL; JYJF01000001; KJK60055.1; -; Genomic_DNA.
DR RefSeq; WP_045298338.1; NZ_JYJF01000001.1.
DR AlphaFoldDB; A0A0F0HX55; -.
DR PATRIC; fig|1427391.3.peg.246; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000033409; 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; PaaE.
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; PR00371; FPNCR.
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:UP000033409}.
FT DOMAIN 6..109
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 267..356
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT REGION 247..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 38494 MW; D46DB7FCBE6ACA5D CRC64;
MSVRRPAFHE LSIGTVEPLC EDAVAVTFEV PPELAAEFTF RPGQTLTLRR MVDGADERRS
YSICSPVGGP LRIAVREVPG GLFSRWLVRA AAAGDRVEVL PPSGLFSPEL GVSARHVLLA
AGSGITPMVS IAGSVLAADE GSEVTLLYGN RRSDTVMFAD ELADLKDRHL GRFQLLHVLS
RETRDAELLS GRLDPERVRA LVEALVDVEQ TDHWWLCGPY GMVEGAKELL AGLGVPAERV
HQELFHAEDE PVAERPEEGG AADGASSEVT VVLDGRSGTL TLPRDRSILD GAQRARPDLP
FACKGGVCGT CRALVTEGEV TMRRNFALEE KEVAAGYVLT CQARPVSDRV TVDYDR
//