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Database: UniProt
Entry: A0A418ZTK6_9RHOB
LinkDB: A0A418ZTK6_9RHOB
Original site: A0A418ZTK6_9RHOB 
ID   A0A418ZTK6_9RHOB        Unreviewed;       354 AA.
AC   A0A418ZTK6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   03-MAY-2023, entry version 13.
DE   SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:RJL01473.1};
GN   ORFNames=D3P06_12320 {ECO:0000313|EMBL:RJL01473.1};
OS   Paracoccus aestuarii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=453842 {ECO:0000313|EMBL:RJL01473.1, ECO:0000313|Proteomes:UP000285530};
RN   [1] {ECO:0000313|EMBL:RJL01473.1, ECO:0000313|Proteomes:UP000285530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19484 {ECO:0000313|EMBL:RJL01473.1,
RC   ECO:0000313|Proteomes:UP000285530};
RA   Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Laiz L.,
RA   Saiz-Jimenez C.;
RT   "Paracoccus onubensis nov. sp. a moderate halophilic bacterium isolated
RT   from Gruta de las Maravillas (Aracena, Spain).";
RL   Submitted (SEP-2018) 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:RJL01473.1}.
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DR   EMBL; QZEV01000066; RJL01473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418ZTK6; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000285530; 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   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:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285530}.
FT   DOMAIN          2..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          265..354
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   354 AA;  38217 MW;  BD6A6F9DD1378349 CRC64;
     MACFLPLTVT AIRRETRDAV VLTLTPRPKD MAAFAFVQGQ YLTFRRDFDG TELRRSYSIC
     AGLDDGCLQV AVKRVEGGAF SSWVNTDLAP GDILEAMPPA GRFFAPVEGA RHYLAFAAGS
     GITPILSIIR TALAREPDAR VTLVYANRGA ASIMFREDLE DLKNLHLGRL SVIHVLEQEG
     QEIELFTGRL EADRLARLFR LWIDPAGADM AFICGPEPMM LAVAASLRDH GMADDRIRFE
     LFSAGQQGRA ATPPRPVAAP TDQGVEAAVT LDGTTRRIAV APGQTLLEAA LAAQMDAPWS
     CRAGVCSTCR CKVTEGAVEM AVNHALEDDE VRAGYVLSCQ AVPLTAAVTM TYDA
//
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