ID A0A017HDT5_9RHOB Unreviewed; 356 AA.
AC A0A017HDT5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Phenylacetate-CoA oxygenase/reductase, PaaK subunit {ECO:0000313|EMBL:EYD72323.1};
GN ORFNames=Lokhon_01118 {ECO:0000313|EMBL:EYD72323.1};
OS Limimaricola hongkongensis DSM 17492.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Limimaricola.
OX NCBI_TaxID=1122180 {ECO:0000313|EMBL:EYD72323.1, ECO:0000313|Proteomes:UP000025047};
RN [1] {ECO:0000313|EMBL:EYD72323.1, ECO:0000313|Proteomes:UP000025047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17492 {ECO:0000313|EMBL:EYD72323.1,
RC ECO:0000313|Proteomes:UP000025047};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (MAR-2013) 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:EYD72323.1}.
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DR EMBL; APGJ01000004; EYD72323.1; -; Genomic_DNA.
DR RefSeq; WP_017928260.1; NZ_KK088650.1.
DR AlphaFoldDB; A0A017HDT5; -.
DR STRING; 1122180.Lokhon_01118; -.
DR PATRIC; fig|1122180.6.peg.1109; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_1_5; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000025047; 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; 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 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:UP000025047}.
FT DOMAIN 2..105
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 265..356
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 356 AA; 38932 MW; BE6CD1BE376DA5C2 CRC64;
MQEFYPLTVT GIDHDTRDAV VVSLAPAKGD CETFRFRPGQ YLTFRRDFDG EELRRSYSIC
ATPEEGLRVG IKKVDGGAFS SFAKHELKVG DTLDALPPQG RFHAPEEAGE KHYLGFAAGS
GITPVLSIAK SILQGSRQAR FTLVYGNRQL SSVMFKSELG DLKDRYLDRL NVVHVFSGEA
QEIELFSGRI DAEKCHALFG PWVSPKAEMA FICGPEAMMK DVAGALEEAG MPKEKIKFEL
FGAAQPGRAK MREAAQAARD SGDMVRATVI LDGVSRSFTM PRSGQSVLDA AREHDIDAPF
SCKAGVCSTC IGRVKSGEVE MMQNYALEDN EVADGLVLTC QCLPLSDEIV IEYEGH
//