ID   UBIM_NEIMF              Reviewed;         461 AA.
AC   A1KVW0;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Ubiquinone hydroxylase UbiM {ECO:0000305};
DE            Short=UQ hydroxylase {ECO:0000303|PubMed:30686758};
DE   AltName: Full=2-polyprenyl-6-methoxyphenol hydroxylase {ECO:0000305};
DE            EC=1.14.13.- {ECO:0000305|PubMed:30686758};
DE   AltName: Full=2-polyprenylphenol hydroxylase {ECO:0000305};
DE            EC=1.14.13.240 {ECO:0000305|PubMed:30686758};
DE   AltName: Full=3-demethoxyubiquinol 3-hydroxylase {ECO:0000305};
DE            EC=1.14.99.60 {ECO:0000305|PubMed:30686758};
GN   Name=ubiM {ECO:0000303|PubMed:30686758};
GN   OrderedLocusNames=NMC1849 {ECO:0000312|EMBL:CAM11015.1};
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=30686758; DOI=10.1016/j.chembiol.2018.12.001;
RA   Hajj Chehade M., Pelosi L., Fyfe C.D., Loiseau L., Rascalou B.,
RA   Brugiere S., Kazemzadeh K., Vo C.D., Ciccone L., Aussel L., Coute Y.,
RA   Fontecave M., Barras F., Lombard M., Pierrel F.;
RT   "A soluble metabolon synthesizes the isoprenoid lipid ubiquinone.";
RL   Cell Chem. Biol. 26:482-492(2019).
CC   -!- FUNCTION: Catalyzes the hydroxylation of three positions of the
CC       aromatic ring during ubiquinone biosynthesis.
CC       {ECO:0000269|PubMed:30686758}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-all-trans-polyprenylphenol + H(+) + NADPH + O2 = a 3-(all-
CC         trans-polyprenyl)benzene-1,2-diol + H2O + NADP(+);
CC         Xref=Rhea:RHEA:55892, Rhea:RHEA-COMP:9516, Rhea:RHEA-COMP:9550,
CC         ChEBI:CHEBI:1269, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:62729; EC=1.14.13.240;
CC         Evidence={ECO:0000305|PubMed:30686758};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 6-methoxy-3-methyl-2-all-trans-polyprenyl-1,4-benzoquinol +
CC         AH2 + O2 = A + a 3-demethylubiquinol + H2O; Xref=Rhea:RHEA:50908,
CC         Rhea:RHEA-COMP:10859, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:84167, ChEBI:CHEBI:84422; EC=1.14.99.60;
CC         Evidence={ECO:0000305|PubMed:30686758};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P25535};
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC       {ECO:0000269|PubMed:30686758}.
CC   -!- SIMILARITY: Belongs to the UbiH/COQ6 family. {ECO:0000305}.
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DR   EMBL; AM421808; CAM11015.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1KVW0; -.
DR   SMR; A1KVW0; -.
DR   EnsemblBacteria; CAM11015; CAM11015; NMC1849.
DR   KEGG; nmc:NMC1849; -.
DR   HOGENOM; CLU_009665_8_1_4; -.
DR   OMA; AHGFNFG; -.
DR   UniPathway; UPA00232; -.
DR   Proteomes; UP000002286; Chromosome.
DR   GO; GO:0008682; F:3-demethoxyubiquinol 3-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010971; UbiH/COQ6.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01988; Ubi-OHases; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; Oxidoreductase; Ubiquinone biosynthesis.
FT   CHAIN           1..461
FT                   /note="Ubiquinone hydroxylase UbiM"
FT                   /id="PRO_0000447678"
SQ   SEQUENCE   461 AA;  51325 MW;  77C8406DA049913F CRC64;
     MRLFTYPTPD LIHIKLKVKI RIHPPLHISS TAGFDIIAYL LQIVQTAFKP LQMPSEIIGI
     RLCKGYFMSL HSDILVVGAG PAGLSFAAEL AGSGLKVTLI ERSPLTVLQN PPYDGREIAL
     THFSREIMQR LGMWDKIPEN EIYPLRDAKV LNGRSDYQLH FPQPTEARGE PADCLGYLIS
     NHNIRRAAYE VVSQLDNVSI LTDTVVKEVK TSDNEAQVIL ENGKILTARL LLAADSRFSQ
     TRRQLGISSD MHDYSRTMFV CRMKHTLSNQ HTAYECFHYG RTIALLPLEE HLTNTVITVD
     TDKINSVQNL SPEELAASVK EQLKGRLGDM ELVSSIHHYP LVGMIAKRFY GKRSALIGDA
     AVGMHPVTAH GFNLGLSSAD ILAKLILEAE QRGQDIGASS LLEKYSNKHM LHAHPLYHGT
     NMMLKLFTNE TAPAKLLRGL VLRAGNNFPP LKKLITKQLT G