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Database: UniProt
Entry: A0A1T4XM70_9GAMM
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Original site: A0A1T4XM70_9GAMM 
ID   A0A1T4XM70_9GAMM        Unreviewed;       365 AA.
AC   A0A1T4XM70;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0000313|EMBL:SKA90637.1};
GN   ORFNames=SAMN02745130_03167 {ECO:0000313|EMBL:SKA90637.1};
OS   Thiothrix eikelboomii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA90637.1, ECO:0000313|Proteomes:UP000190460};
RN   [1] {ECO:0000313|EMBL:SKA90637.1, ECO:0000313|Proteomes:UP000190460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA90637.1,
RC   ECO:0000313|Proteomes:UP000190460};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
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DR   EMBL; FUYB01000019; SKA90637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4XM70; -.
DR   STRING; 92487.SAMN02745130_03167; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000190460; 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:UP000190460}.
FT   DOMAIN          4..108
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          274..365
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   365 AA;  40424 MW;  8730E86322051F41 CRC64;
     MADTRFYPLR ISEIKPETDT AVCISFQVPP ELTNNFKFVQ GQFLTLKADI EGEDVRRSYS
     ICSGVHDGHL RVGIKRVRGG KFSNYANDQF KVGDTVEVMP PQGSFNSPLN PEQAKNYMCL
     AGGSGITPIL SIMKTILIEE PQSKVTLIYG NRRSNSVMFK DELSFLKNRY MNRFQWINIM
     SQEDQGADLL NGQIDNQKGA ALHKSRLINI KTTDEVFICG PEAMMSEVSR GFRASGLSEE
     QIHYELFANS SADAATLLEK AQQRIDTYGE EKTSKVTVIA DGRSLQFDLA TVGQNILDAG
     IHNGLDLPYA CKAGVCSTCK AKLVKGQVDM DIHHGLEAHE IAAGYILTCQ AHPVSDEVVV
     DFDQR
//
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