ID A0A1Q3T6S3_9SPHI Unreviewed; 360 AA.
AC A0A1Q3T6S3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:OJV97884.1};
GN ORFNames=BGO52_10535 {ECO:0000313|EMBL:OJV97884.1};
OS Sphingobacteriales bacterium 44-61.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895838 {ECO:0000313|EMBL:OJV97884.1, ECO:0000313|Proteomes:UP000186208};
RN [1] {ECO:0000313|EMBL:OJV97884.1, ECO:0000313|Proteomes:UP000186208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44-61 {ECO:0000313|EMBL:OJV97884.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJV97884.1}.
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DR EMBL; MKTW01000018; OJV97884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3T6S3; -.
DR STRING; 1895838.BGO52_10535; -.
DR Proteomes; UP000186208; 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; 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; 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; 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}.
FT DOMAIN 3..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 268..360
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 360 AA; 40633 MW; 6F9F90D310FE8BEA CRC64;
MSLHFHKLRV KDIRKETDDC VSISFDIPNA LKDVFLFEQG QNITLRRDLN GEETRRSYSI
CTSPFENELR VAVKKVEGGL FSCFAHAELH AGDEIEVLPP TGKFNTKLDP LNAKKYLAFA
AGSGITPVIS IIKTTLQTEP GSSFTLVYGN RSRHSIIFFE ELEALKNKYL QRFNLIYILS
REGTDTPVNA GRIDINKLSE LSRLVNYQSM DEIFICGPEE MIFTVKGFME KEKIDADKIH
FELFTTPGQK KNMFPDPFSK KEKGSDKSLI TIKQDGRTMD FELAPDSEDT ILDAALKLGA
DLPYSCRGGV CCTCKAKLLE GKVEMDTNWG LEKEEVEQGY ILTCQSHPRT PKVVVDFDVK
//