ID   O84985_PSEPU            Unreviewed;       358 AA.
AC   O84985;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 2.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=PaaK {ECO:0000313|EMBL:AAC24337.2};
GN   Name=paaK {ECO:0000313|EMBL:AAC24337.2};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303 {ECO:0000313|EMBL:AAC24337.2};
RN   [1] {ECO:0000313|EMBL:AAC24337.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=U {ECO:0000313|EMBL:AAC24337.2};
RX   PubMed=9600981; DOI=10.1073/pnas.95.11.6419;
RA   Olivera E.R., Minambres B., Garcia B., Muniz C., Moreno M.A., Ferrandez A.,
RA   Diaz E., Garcia J.L., Luengo J.M.;
RT   "Molecular characterization of the phenylacetic acid catabolic pathway in
RT   Pseudomonas putida U: the phenylacetyl-CoA catabolon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:6419-6424(1998).
RN   [2] {ECO:0000313|EMBL:AAC24337.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=U {ECO:0000313|EMBL:AAC24337.2};
RA   Olivera E.R., Minambres B.M., Garcia B., Muniz C., Luengo J.M.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF029714; AAC24337.2; -; Genomic_DNA.
DR   AlphaFoldDB; O84985; -.
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; 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   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          2..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          267..358
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   358 AA;  39433 MW;  DD14E667B805506B CRC64;
     MSQFHSLTIK QVRNETRDAV SIAFDVPEHL QAQFRFTQGQ YLVMRTQLDN EEVRRSYSIC
     SAVQDGELRV AVKRVPGGRF SAFANEVLKA GQQLEVMPPA GSFFVPLDAA RQGNYLGVAA
     GSGITPILSI IGTTLDSEPH SCFTLLYGNR SSSGALFRDK LEDLKNRYLD RLNLIFVFSR
     EQQDVDLYNG RVDADKCGQL FSRWLDVPGL DAAFICGPQA MTETVRDSLQ ANGLGKERIH
     FELFAAAGSE TRREAREAAH QVDSALSHIT VISDGRALTF DLPRNTQNVL DAGNAIGAEL
     PYSCKAGVCS TCKCRVIEGE VEMDSNHALE DYEVAAGYVL SCQTYPVSDK VVLDFDQL
//