ID A0A0J7J1K1_9FLAO Unreviewed; 362 AA.
AC A0A0J7J1K1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Phenylacetate-CoA oxygenase {ECO:0000313|EMBL:KMQ72298.1};
GN ORFNames=ACM44_02310 {ECO:0000313|EMBL:KMQ72298.1};
OS Chryseobacterium koreense CCUG 49689.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1304281 {ECO:0000313|EMBL:KMQ72298.1, ECO:0000313|Proteomes:UP000035900};
RN [1] {ECO:0000313|EMBL:KMQ72298.1, ECO:0000313|Proteomes:UP000035900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 49689 {ECO:0000313|EMBL:KMQ72298.1,
RC ECO:0000313|Proteomes:UP000035900};
RX PubMed=15545478; DOI=10.1099/ijs.0.02998-0;
RA Kim M.K., Im W.T., Shin Y.K., Lim J.H., Kim S.H., Lee B.C., Park M.Y.,
RA Lee K.Y., Lee S.T.;
RT "Kaistella koreensis gen. nov., sp. nov., a novel member of the
RT Chryseobacterium-Bergeyella-Riemerella branch.";
RL Int. J. Syst. Evol. Microbiol. 54:2319-2324(2004).
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:KMQ72298.1}.
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DR EMBL; LFNG01000003; KMQ72298.1; -; Genomic_DNA.
DR RefSeq; WP_048498495.1; NZ_LFNG01000003.1.
DR AlphaFoldDB; A0A0J7J1K1; -.
DR STRING; 1304281.ACM44_02310; -.
DR PATRIC; fig|1304281.5.peg.501; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000035900; 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; 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; 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:UP000035900}.
FT DOMAIN 2..108
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 272..362
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 362 AA; 41193 MW; 75A98E41B7FBB220 CRC64;
MHHFYPLKAI KVRKETNDSI NIAFEIPPNL KNEFSFKQGQ YLNLRFVFGD EDLRRSYSIV
NAPTEGNAEL EILVKHLDGG KVSTYLNNEL KAGDFIEVMA PMGHFYTNYH PSNEKTYVGL
AAGSGISPVL SNLKEALYLE PKSKAYLFFS NKSFDQIIFR KEIDELAEKF NGRLKVVYIL
SREKHFEDEL FEGRITAGKL ELLFARFEEI PIQGATYFIC GPTEMIKGIS DYLKNDKKVP
SLQIMYEYYA APDDEENAEM SDEFKAIPNL ESMVTVIIDD DEYSFHLNSK KNSILDQAIK
EKLPVPFACK GGVCCTCKAQ VLEGEVFMEK NFALTDDEVA KGYVLTCQCH PTTNVVMLNY
DV
//