ID A0A1Q6A5W5_9SPHI Unreviewed; 339 AA.
AC A0A1Q6A5W5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Ring-1,2-phenylacetyl-CoA epoxidase subunit PaaE {ECO:0008006|Google:ProtNLM};
GN ORFNames=RG47T_4882 {ECO:0000313|EMBL:OKS89398.1};
OS Mucilaginibacter polytrichastri.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1302689 {ECO:0000313|EMBL:OKS89398.1, ECO:0000313|Proteomes:UP000186720};
RN [1] {ECO:0000313|EMBL:OKS89398.1, ECO:0000313|Proteomes:UP000186720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG4-7 {ECO:0000313|EMBL:OKS89398.1,
RC ECO:0000313|Proteomes:UP000186720};
RA Li Y.;
RT "Whole Genome Sequencing of Mucilaginibacter polytrichastri RG4-7(T)
RT isolated from the moss sample.";
RL Submitted (NOV-2016) 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:OKS89398.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MPPL01000001; OKS89398.1; -; Genomic_DNA.
DR RefSeq; WP_074492391.1; NZ_MPPL01000001.1.
DR AlphaFoldDB; A0A1Q6A5W5; -.
DR STRING; 1302689.RG47T_4882; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000186720; 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; NADH OXIDOREDUCTASE HCR; 1.
DR PANTHER; PTHR47354:SF5; PROTEIN RFBI; 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:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000186720}.
FT DOMAIN 1..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT DOMAIN 251..339
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
SQ SEQUENCE 339 AA; 38198 MW; D47D74FD140C187E CRC64;
MNTIQLIVDS IKQETSDTAT FYLRPANGQQ VHYEAGQFIT LIFTHHDEEI TRSYSLSSSP
DEELLSITIK RISNGEISRF MLSHTKPGDE LTAIQPAGRF ILPESGSHRR LIYFAAGSGI
VPVFAQLKHA LLRGLDLQMV LIYSSQSNND IIFKPQLDEL AAAHPGKFLV KYLISDEANR
LNNLMLEKLV KQLTNQHYHD TLFYICGPFP YMRMVQFALH YMGVQSANIR KENFVLETIP
VISNITNFPP RKIRIFFKNE WHDLVAGENQ SILQAALQNN IPLPYSCRSG ACSACFAKCT
SGKVEVVSNE VLTPEDLKNG YVLTCTGHAL TDDVVIEFR
//
