ID H6LB08_SAPGL Unreviewed; 356 AA.
AC H6LB08;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Phenylacetate-CoA oxygenase, PaaK subunit {ECO:0000313|EMBL:AFC26973.1};
GN Name=paaE {ECO:0000313|EMBL:AFC26973.1};
GN ORFNames=SGRA_p0033 {ECO:0000313|EMBL:AFC26973.1};
OS Saprospira grandis (strain Lewin).
OG Plasmid SGRA01 {ECO:0000313|Proteomes:UP000007519}.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26973.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC26973.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC26973.1,
RC ECO:0000313|Proteomes:UP000007519};
RC PLASMID=Plasmid SGRA01 {ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP002832; AFC26973.1; -; Genomic_DNA.
DR RefSeq; WP_015695528.1; NC_016936.1.
DR AlphaFoldDB; H6LB08; -.
DR KEGG; sgn:SGRA_p0033; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_14_1_10; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000007519; Plasmid SGRA01.
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; 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; PR00371; FPNCR.
DR PRINTS; PR00410; PHEHYDRXLASE.
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; 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:AFC26973.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007519}.
FT DOMAIN 2..106
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; 40035 MW; 0DA538C6874BF969 CRC64;
MTELYPLQLS DVRQETEDCR SLAFAIPQNL QEKFKFVQGQ YLTLQAKING EDVRRSYSIC
SSPLDQELRV AVKLLPGGKF STFANETLKV GDELLAMPPM GNFYTDLDPQ QSKHYFCVAA
GSGITPMMSI IKTTLETEPN SQITLLYGNK NTRNIIFHEQ LEGLKNKYLE RFTIIYILSR
EKLDEDILFG RIDAQKFEAI SQTLVDLNTV DECFLCGPET MILALKEGLA NKGIPQKNIH
FELFGTNQKG QKKPEIKKEN QGKAAKVEVR VDGRSFMFDL PFGQDNLLDA SMKEGADLPF
ACKGGVCCTC KARVKKGEVE MMVNYALEPE EVADGLILSC QAYPKSEEIM LDFDDI
//
