ID A1S968_SHEAM Unreviewed; 393 AA.
AC A1S968;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase {ECO:0000313|EMBL:ABM00925.1};
DE EC=1.14.13.- {ECO:0000313|EMBL:ABM00925.1};
GN OrderedLocusNames=Sama_2722 {ECO:0000313|EMBL:ABM00925.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABM00925.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABM00925.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000507; ABM00925.1; -; Genomic_DNA.
DR RefSeq; WP_011760830.1; NC_008700.1.
DR AlphaFoldDB; A1S968; -.
DR STRING; 326297.Sama_2722; -.
DR KEGG; saz:Sama_2722; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_8_3_6; -.
DR OrthoDB; 9769565at2; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000009175; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of 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; IPR018168; Ubi_Hdrlase_CS.
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.
DR PROSITE; PS01304; UBIH; 1.
PE 3: Inferred from homology;
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ABM00925.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175}.
FT DOMAIN 7..348
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
SQ SEQUENCE 393 AA; 42657 MW; 0317BE6644B67B88 CRC64;
MMTTQSCDVA IVGGGMVGLA TAIGLAEAGL KVTVLDAGSQ SAVAGEPRLR VSAINRASED
LLKSLGAWPL MDSQRTASYG RMQVWDKDGM GKIGFDANEL GESSLGTIIE NDNIAAALAK
RAGEFDNLDY REGVRLSRLA FGEKEAWLTL EEGDMLSAAL VIAADGANSW VRSQCNIPLT
FWDYGHTAIV ATIETAEPHE SCARQVFLPD GPLAFLPLFQ ANLCSIVWSV TEPRAQELLA
MDDENFSKSL TAAFDARLGL CHVKSERIGF NLRMRYARHF ARHRLLLAGD AAHTIHPLAG
QGVNLGFQDA AAIIETIGRL KAEGKDIGDY RLLRPLERER KAAAQEMIAT MEGFKRLFEG
SNPIKQAVRD LGLNLVDKLP GLKTVFIKQA MGR
//
