ID A0A1W6ZE97_9BORD Unreviewed; 362 AA.
AC A0A1W6ZE97;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:ARP95696.1};
GN ORFNames=CAL15_15685 {ECO:0000313|EMBL:ARP95696.1};
OS Bordetella genomosp. 13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463040 {ECO:0000313|EMBL:ARP95696.1, ECO:0000313|Proteomes:UP000194161};
RN [1] {ECO:0000313|EMBL:ARP95696.1, ECO:0000313|Proteomes:UP000194161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU7206 {ECO:0000313|EMBL:ARP95696.1,
RC ECO:0000313|Proteomes:UP000194161};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP021111; ARP95696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ZE97; -.
DR STRING; 463040.CAL15_15685; -.
DR KEGG; bgm:CAL15_15685; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000194161; Chromosome.
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; 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:ARBA00022714}.
FT DOMAIN 4..108
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 270..362
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 362 AA; 40170 MW; BB33413381242FD9 CRC64;
MSQTAFHTLK VASVARNTRD AVVVTFDLPQ DLAGDFAFRP GQYLTLRTQL AGEEIRRSYS
ICSAPDDGVL RVAIKKVDEG VFSSWANHQL QPGQTLEVMP PAGNFTVDFD PAQSRRYVAF
AVGSGITPVL SLVKTALSTE PDSRFTLFFG NRASSSVLFR EEIEDLKNRY MERFSLVYIM
SRETQDIELF NGRLDGEKVD QLLRVWMPPG QIDYAFVCGP QTMIESVVEH LQAQGIPKDR
IKFELFGAPK GPRALRTGRE VAAAPGKGQC EVTVVQDGHS RTFFIDKNKD SVLDSALAQG
IELPYSCKGG VCSTCRCKVI EGEVDMDANF ALEDYEVARG FVLSCQSYPV SDRLVIDYDQ
ET
//
