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Database: UniProt
Entry: Q1GKX1_RUEST
LinkDB: Q1GKX1_RUEST
Original site: Q1GKX1_RUEST 
ID   Q1GKX1_RUEST            Unreviewed;       356 AA.
AC   Q1GKX1;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   SubName: Full=Phenylacetic acid degradation oxidoreductase PaaK {ECO:0000313|EMBL:ABF62695.1};
GN   Name=paaK {ECO:0000313|EMBL:ABF62695.1};
GN   OrderedLocusNames=TM1040_3728 {ECO:0000313|EMBL:ABF62695.1};
OS   Ruegeria sp. (strain TM1040) (Silicibacter sp.).
OG   Plasmid megaplasmid TM1040 {ECO:0000313|Proteomes:UP000000636}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=292414 {ECO:0000313|EMBL:ABF62695.1, ECO:0000313|Proteomes:UP000000636};
RN   [1] {ECO:0000313|Proteomes:UP000000636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040 {ECO:0000313|Proteomes:UP000000636};
RC   PLASMID=megaplasmid TM1040 {ECO:0000313|Proteomes:UP000000636};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Goodwin L., Thompson L.S.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Belas R., Moran M.A., Buchan A., Gonzalez J.M., Schell M.A., Sun F.,
RA   Richardson P.;
RT   "Complete sequence of megaplasmid of Silicibacter sp. TM1040.";
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABF62695.1, ECO:0000313|Proteomes:UP000000636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM1040 {ECO:0000313|EMBL:ABF62695.1,
RC   ECO:0000313|Proteomes:UP000000636};
RC   PLASMID=megaplasmid TM1040 {ECO:0000313|Proteomes:UP000000636};
RX   PubMed=17526795; DOI=10.1128/AEM.02580-06;
RA   Moran M.A., Belas R., Schell M.A., Gonzalez J.M., Sun F., Sun S.,
RA   Binder B.J., Edmonds J., Ye W., Orcutt B., Howard E.C., Meile C.,
RA   Palefsky W., Goesmann A., Ren Q., Paulsen I., Ulrich L.E., Thompson L.S.,
RA   Saunders E., Buchan A.;
RT   "Ecological genomics of marine Roseobacters.";
RL   Appl. Environ. Microbiol. 73:4559-4569(2007).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP000376; ABF62695.1; -; Genomic_DNA.
DR   RefSeq; WP_011537333.1; NC_008043.1.
DR   AlphaFoldDB; Q1GKX1; -.
DR   KEGG; sit:TM1040_3728; -.
DR   HOGENOM; CLU_003827_14_1_5; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000000636; Plasmid megaplasmid TM1040.
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   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; IPR017938; Riboflavin_synthase-like_b-brl.
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:ABF62695.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000636}.
FT   DOMAIN          2..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          267..356
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   356 AA;  38683 MW;  3152DDA657211E28 CRC64;
     MARFHPLEVT DIKKTIRDAV VVTLKPLNGA AAEFDFTQGQ YLTFRRDFDG TELRRSYSIC
     AGKDEGILQV GIKRVDGGAF STWANTVLKV GDTVEAMPPQ GRFFTDLDAA AEKHYLGFAG
     GSGITPVLSI LKTTLQAEPQ SRFTLVYANK GINSIMFREE IEDLKNRYMG RLSVIHVLET
     DAQEVDLFTG LVTQEKCAEL FERWIPIQSV DTAFICGPEP MMLGIAEALR TAGLSDEQIK
     FELFASNQPG RAAKKATSGD AAASAPVTAA ITLDGATRSV TLDRNTSVLE AALENAMDAP
     WSCRAGVCST CRCRVIEGEV EMAANHALED DEVAKGFVLS CQAYPLSDAL VVSYDE
//
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