ID A8LS35_DINSH Unreviewed; 399 AA.
AC A8LS35;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000313|EMBL:ABV94128.1};
GN OrderedLocusNames=Dshi_2392 {ECO:0000313|EMBL:ABV94128.1};
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV94128.1, ECO:0000313|Proteomes:UP000006833};
RN [1] {ECO:0000313|Proteomes:UP000006833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC {ECO:0000313|Proteomes:UP000006833};
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC {ECO:0000256|ARBA:ARBA00005349}.
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DR EMBL; CP000830; ABV94128.1; -; Genomic_DNA.
DR RefSeq; WP_012179059.1; NC_009952.1.
DR AlphaFoldDB; A8LS35; -.
DR STRING; 398580.Dshi_2392; -.
DR KEGG; dsh:Dshi_2392; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_1_5; -.
DR OrthoDB; 9796623at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000006833; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010971; UbiH/COQ6.
DR NCBIfam; TIGR01988; Ubi-OHases; 1.
DR PANTHER; PTHR43876; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43876:SF7; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006833}.
FT DOMAIN 6..349
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 399 AA; 42652 MW; E4A2B5815B6ED5BF CRC64;
MQTEQTDILI SGGGVAGLSA AAAFGSAGFQ VIVVDPAPPV TEGAADGADM RTTAFLQPSR
EVLEKAGLWA RLAPFAAPLQ VMQIIDAGGT EPVARVQKAF NARDISDDPF GWNLQNWLLR
REMVARLEEL PNVTFRPGVG TADVLARERE ARVRLTDGTM VSARLLIAAD GRNSPVRNAL
GIGVRTTRYG QKALAFAVTH PIPHDNVSTE IHRSGGPFTL VPLPDLEGQP RSAIVWMERG
PEALRLASCD VAEFEAEMTA RSTGLLGPLK LVSRRSVWPI ISQMAERLTG PRTALIAEAA
HVVPPIGAQG LNMSLADVRV LLELAEAAPD TLGSPEMLQA YARKRAPDVR TRITGIDLLN
RASMAGAQPL RDARAQGLKA LYGLAPVRKS LMQLGLGVR
//
