ID J3VTZ8_9ENTR Unreviewed; 240 AA.
AC J3VTZ8;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=2-polyprenylphenol hydroxylase-like oxidoreductase {ECO:0000313|EMBL:AFP85546.1};
GN ORFNames=A35E_00237 {ECO:0000313|EMBL:AFP85546.1};
OS secondary endosymbiont of Heteropsylla cubana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts.
OX NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85546.1, ECO:0000313|Proteomes:UP000003937};
RN [1] {ECO:0000313|EMBL:AFP85546.1, ECO:0000313|Proteomes:UP000003937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hcub_S {ECO:0000313|EMBL:AFP85546.1};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(2012).
CC -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00038177}.
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DR EMBL; CP003547; AFP85546.1; -; Genomic_DNA.
DR RefSeq; WP_014888843.1; NC_018420.1.
DR AlphaFoldDB; J3VTZ8; -.
DR STRING; 134287.A35E_00237; -.
DR KEGG; sehc:A35E_00237; -.
DR PATRIC; fig|134287.3.peg.228; -.
DR HOGENOM; CLU_003827_7_4_6; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000003937; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd06189; flavin_oxioreductase; 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; 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:SF7; NAD(P)H-FLAVIN REDUCTASE; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00410; PHEHYDRXLASE.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Reference proteome {ECO:0000313|Proteomes:UP000003937}.
FT DOMAIN 1..99
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 240 AA; 27700 MW; 080736718C3B2325 CRC64;
MIRLTCKVLS VDAITKTVYR IRLVRAPTYN FRAGQYLMVV MDHNDIRPFS MASTPLEQTF
IELHIDASSL NLYARKLVEA VIKTQEITIE RPRGSAFLRD DTERPILLIA GGTGFSYIRS
ILLTVLSLQP TRKVMIYWGG KKREHLYKLD ELEVLALQYS KLSVVPVVEQ CDDKQWKGRY
GTVIMAVIQD YNYLKPYDIY IGGNFNMARV AQTLLCSECR AVVERIFSDA FSLERNFYFN
//
