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Entry: A6UH26_SINMW
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ID   A6UH26_SINMW            Unreviewed;       358 AA.
AC   A6UH26;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Phenylacetate-CoA oxygenase/reductase, PaaK subunit {ECO:0000313|EMBL:ABR62956.1};
GN   OrderedLocusNames=Smed_4151 {ECO:0000313|EMBL:ABR62956.1};
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG   Plasmid pSMED01 {ECO:0000313|EMBL:ABR62956.1,
OG   ECO:0000313|Proteomes:UP000001108}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394 {ECO:0000313|EMBL:ABR62956.1, ECO:0000313|Proteomes:UP000001108};
RN   [1] {ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|Proteomes:UP000001108};
RC   PLASMID=Plasmid pSMED01 {ECO:0000313|Proteomes:UP000001108};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABR62956.1, ECO:0000313|Proteomes:UP000001108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419 {ECO:0000313|EMBL:ABR62956.1,
RC   ECO:0000313|Proteomes:UP000001108};
RC   PLASMID=Plasmid pSMED01 {ECO:0000313|Proteomes:UP000001108};
RX   PubMed=21304680; DOI=10.4056/sigs.43526;
RA   Reeve W., Chain P., O'Hara G., Ardley J., Nandesena K., Brau L., Tiwari R.,
RA   Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA   Hauser L., Chang Y.J., Ivanova N., Mavromatis K., Markowitz V.,
RA   Kyrpides N., Gollagher M., Yates R., Dilworth M., Howieson J.;
RT   "Complete genome sequence of the Medicago microsymbiont Ensifer
RT   (Sinorhizobium) medicae strain WSM419.";
RL   Stand. Genomic Sci. 2:77-86(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000739; ABR62956.1; -; Genomic_DNA.
DR   RefSeq; WP_011969778.1; NC_009620.1.
DR   RefSeq; YP_001312889.1; NC_009620.1.
DR   AlphaFoldDB; A6UH26; -.
DR   KEGG; smd:Smed_4151; -.
DR   PATRIC; fig|366394.8.peg.607; -.
DR   HOGENOM; CLU_003827_14_1_5; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000001108; Plasmid pSMED01.
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};
KW   Plasmid {ECO:0000313|EMBL:ABR62956.1}.
FT   DOMAIN          2..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          268..358
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   REGION          248..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   358 AA;  39747 MW;  3087CFE4BB3D14A7 CRC64;
     MARFHPLQVT EVRRETRDAV VVTLEPRDED RAAFDFTQGQ YLTFRRIFDG EELRRSYSIC
     SGLGEGALRV GIKRVDGGCF SNWANEVLKP GDTLEAMPPM GTFFVPVEPE VSRHYLGFAG
     GSGITPVLSL VKTVLAREPR SAFTLVYANR HFSSIMFREE LDDLKNLYLG RLSVLHILES
     EAQDIDLFSG RLDLEKCTAL FRHWIDVKSA DIAFICGPEP MMQAVAATLR AHGVSDSRIR
     FELFGSSQPG RARRRTASPA GTDGGSRCEA TVTLDGATRS FTLPKRGQSL LEAALENRMD
     APYACKAGVC SSCRAKVLEG EVEMESNNAL EDYEVEQGYV LMCQSYPLSD RVVVSYDE
//
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