ID R9PCA7_PSEHS Unreviewed; 928 AA.
AC R9PCA7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=5-demethoxyubiquinone hydroxylase, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03194};
DE Short=DMQ hydroxylase {ECO:0000256|HAMAP-Rule:MF_03194};
DE EC=1.14.99.60 {ECO:0000256|HAMAP-Rule:MF_03194};
DE AltName: Full=Ubiquinone biosynthesis monooxygenase COQ7 {ECO:0000256|HAMAP-Rule:MF_03194};
GN Name=COQ7 {ECO:0000256|HAMAP-Rule:MF_03194};
GN ORFNames=PHSY_006437 {ECO:0000313|EMBL:GAC98842.1};
OS Pseudozyma hubeiensis (strain SY62) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1305764 {ECO:0000313|EMBL:GAC98842.1, ECO:0000313|Proteomes:UP000014071};
RN [1] {ECO:0000313|Proteomes:UP000014071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY62 {ECO:0000313|Proteomes:UP000014071};
RX PubMed=23814110; DOI=10.1128/genomea.00409-13;
RA Konishi M., Hatada Y., Horiuchi J.;
RT "Draft genome sequence of the basidiomycetous yeast-like fungus Pseudozyma
RT hubeiensis SY62, which produces an abundant amount of the biosurfactant
RT mannosylerythritol lipids.";
RL Genome Announc. 1:E0040913-E0040913(2013).
CC -!- FUNCTION: Catalyzes the hydroxylation of 2-polyprenyl-3-methyl-6-
CC methoxy-1,4-benzoquinol (DMQH2) during ubiquinone biosynthesis. Has
CC also a structural role in the COQ enzyme complex, stabilizing other COQ
CC polypeptides. {ECO:0000256|HAMAP-Rule:MF_03194}.
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:0000256|HAMAP-Rule:MF_03194};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03194};
CC Note=Binds 2 iron ions per subunit. {ECO:0000256|HAMAP-Rule:MF_03194};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03194}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000256|HAMAP-
CC Rule:MF_03194}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03194}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03194}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03194}.
CC -!- SIMILARITY: Belongs to the COQ7 family. {ECO:0000256|HAMAP-
CC Rule:MF_03194}.
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DR EMBL; DF238821; GAC98842.1; -; Genomic_DNA.
DR RefSeq; XP_012192429.1; XM_012337039.1.
DR AlphaFoldDB; R9PCA7; -.
DR STRING; 1305764.R9PCA7; -.
DR GeneID; 24111708; -.
DR eggNOG; KOG3855; Eukaryota.
DR eggNOG; KOG4061; Eukaryota.
DR HOGENOM; CLU_009665_8_0_1; -.
DR OrthoDB; 5473786at2759; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000014071; Unassembled WGS sequence.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:UniProtKB-UniRule.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01042; DMQH; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR HAMAP; MF_01658; COQ7; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR018168; Ubi_Hdrlase_CS.
DR InterPro; IPR011566; Ubq_synth_Coq7.
DR PANTHER; PTHR43876; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43876:SF7; UBIQUINONE BIOSYNTHESIS MONOOXYGENASE COQ6, MITOCHONDRIAL; 1.
DR Pfam; PF03232; COQ7; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF47240; Ferritin-like; 1.
DR PROSITE; PS01304; UBIH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Iron {ECO:0000256|HAMAP-Rule:MF_03194};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03194};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03194};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03194};
KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03194};
KW Monooxygenase {ECO:0000256|HAMAP-Rule:MF_03194};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03194}; Reference proteome {ECO:0000313|Proteomes:UP000014071};
KW Ubiquinone biosynthesis {ECO:0000256|HAMAP-Rule:MF_03194}.
FT DOMAIN 515..558
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT REGION 12..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 755
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 788
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 788
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 791
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 840
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 889
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 889
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
FT BINDING 892
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03194"
SQ SEQUENCE 928 AA; 99260 MW; BC3F29446344A1A2 CRC64;
MTRLARTTVA ASSLSRATAT RHSLQRTLAT SSSHHLQSNS RAGPSRPFLH PNVAAPPQIL
AAISSTSRKL ATAATSTHNI ESDIVVVGGG VVGLGLACDL VASQAVSSTS QSGDQPITLI
EASNLDRLRS WTADRAHHLS QSHASSSSST DGLDWENRVI SLTSENLDWL KRMGVYPFLV
EHRLRPISSM RVWDGLSGAL LDFDSAHLSD AVGSSSQISV MVEISNLQQA MLQFLEQGPG
KGICTIKDGA KVDSIVGGSK VEVGSTSIEQ DPWPIVQLSA GDAIQARLLV GADGPNSPVR
KYAGIGDYGW PYDRRGLVGT LRCRGVEHGE PAVGHTAYQR FLPSGTIAFL PLSDSTGSMV
WTLEPEVASA LAVLHHETAE STDEPLAKLV DAAFRLPWSH IERLFARVVA FTKYPQPEGA
QRDWRWLTAE IPTEAEWVER GLDEPLPESG SGEVPPKVHS LDVKSVASFP LNLKHADAYL
GASLNSSPVL PSGLLAGAMA AVGLAPEGAG QGAGRGRTVL VGDAAHTIHP LAGQGLNLGI
ADVRSLSRTL RSALGAGADI GSYNALKGYA RDRYWENQKM LSAVDHLHWL YAGTPVPLSQ
QADGGKQQRE RDGLFRTAAK EVVGRGTVWA RSTGLEVINE LDFVKNAFMR QAGSTTSSVR
SGPWPSSRRT FSTLRGQGLH LTSRPRASPL TRGNGSLIRH HSSEYSGPLA SDVYTGVDAS
DPSNAATTST PSLASLTPSQ RRALRDMLRV DHSGEIAANT IYQGQADMFG ALGDVKNRDL
SIEMWQTEKK HLEVMRALLR QHNVRPSLLL PVWSTAGRVL GGVTALLGPR SAMACTEAVE
SVIGEHYDDQ LKELKTILEK EQVGGEVAED VHPSLPLLSD IIKEFRDDEL EHLDTAVENE
SQQAAGHALL SAVIAAGCRG AIWVASRV
//
