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Database: UniProt
Entry: A0A0X3TX47_9RHOB
LinkDB: A0A0X3TX47_9RHOB
Original site: A0A0X3TX47_9RHOB 
ID   A0A0X3TX47_9RHOB        Unreviewed;       357 AA.
AC   A0A0X3TX47;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Phenylacetic acid degradation protein {ECO:0000313|EMBL:KUJ80303.1};
GN   ORFNames=AVO45_04385 {ECO:0000313|EMBL:KUJ80303.1};
OS   Ruegeria marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ80303.1, ECO:0000313|Proteomes:UP000053791};
RN   [1] {ECO:0000313|EMBL:KUJ80303.1, ECO:0000313|Proteomes:UP000053791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ80303.1,
RC   ECO:0000313|Proteomes:UP000053791};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KUJ80303.1}.
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DR   EMBL; LQBQ01000012; KUJ80303.1; -; Genomic_DNA.
DR   RefSeq; WP_068345420.1; NZ_LQBQ01000012.1.
DR   AlphaFoldDB; A0A0X3TX47; -.
DR   STRING; 1685379.AVO45_04385; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000053791; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053791}.
FT   DOMAIN          2..106
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   DOMAIN          268..357
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
SQ   SEQUENCE   357 AA;  39300 MW;  BF3DF64959136F3A CRC64;
     MARFHDLEVT DIHKTIRDAV VVTLKPVNGS AEEFDFTQGQ YLTFRRDFDG EELRRSYSIC
     AGKDDGVLQV GIKKVDGGAF STWANEELKV GDTLQAMPPM GGFFTPLDPE AEKQYLGFAG
     GSGITPVLSI LKTTLAREPK SHFTLVYANK GVNTIMFREE LEDLKNLYMG RLNVLHILET
     DAQEIDLFTG LVTKEKCAEL FKHWIDIENV DAAFICGPEP MMLGIAEALR EHGLDDSQIK
     FELFASAQPG RAKRKVTSAE ATTSANQTKA AITLDGATQT ITMPKDQSIL DAALENAMDA
     PYACKAGVCS TCRCKVLEGE VEMVANHALE DYEVEKGYVL SCQAFPLTDT VVVDYDQ
//
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