ID A0A094G091_9PEZI Unreviewed; 1655 AA.
AC A0A094G091;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03193};
DE EC=1.14.13.- {ECO:0000256|HAMAP-Rule:MF_03193};
GN Name=COQ6 {ECO:0000256|HAMAP-Rule:MF_03193};
GN ORFNames=V498_02689 {ECO:0000313|EMBL:KFY96456.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY96456.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY96456.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: FAD-dependent monooxygenase required for the C5-ring
CC hydroxylation during ubiquinone biosynthesis. Catalyzes the
CC hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-
CC polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the
CC hydroxylation reaction may be funneled indirectly from NADPH via a
CC ferredoxin/ferredoxin reductase system to COQ6. {ECO:0000256|HAMAP-
CC Rule:MF_03193}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxy-3-all-trans-hexaprenylbenzoate + 2 H(+) + O2 + 2
CC reduced [2Fe-2S]-[ferredoxin] = 3,4-dihydroxy-5-all-trans-
CC hexaprenylbenzoate + H2O + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:20361, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:58373,
CC ChEBI:CHEBI:84492; Evidence={ECO:0000256|HAMAP-Rule:MF_03193};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|HAMAP-Rule:MF_03193};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_03193}.
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_03193}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_03193}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_03193}; Matrix side {ECO:0000256|HAMAP-Rule:MF_03193}.
CC -!- SIMILARITY: Belongs to the UbiH/COQ6 family.
CC {ECO:0000256|ARBA:ARBA00005349, ECO:0000256|HAMAP-Rule:MF_03193}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFY96456.1}.
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DR EMBL; JPKA01000431; KFY96456.1; -; Genomic_DNA.
DR HOGENOM; CLU_001412_0_0_1; -.
DR UniPathway; UPA00232; -.
DR Proteomes; UP000029270; Unassembled WGS sequence.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008681; F:2-octaprenyl-6-methoxyphenol hydroxylase activity; IEA:InterPro.
DR GO; GO:0106364; F:4-hydroxy-3-all-trans-hexaprenylbenzoate oxygenase activity; IEA:RHEA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13118; POLO_box_1; 1.
DR CDD; cd14099; STKc_PLK; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.30.1120.30; POLO box domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR HAMAP; MF_03193; COQ6_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033701; POLO_box_1.
DR InterPro; IPR036947; POLO_box_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR018168; Ubi_Hdrlase_CS.
DR InterPro; IPR010971; UbiH/COQ6.
DR InterPro; IPR000689; UbQ_mOase_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 Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF82615; Polo-box domain; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS01304; UBIH; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_03193};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_03193}; Membrane {ECO:0000256|HAMAP-Rule:MF_03193};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03193};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW ECO:0000256|HAMAP-Rule:MF_03193};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_03193};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03193};
KW Ubiquinone biosynthesis {ECO:0000256|ARBA:ARBA00022688, ECO:0000256|HAMAP-
KW Rule:MF_03193}.
FT DOMAIN 149..411
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 105..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1655 AA; 183766 MW; B62D9CAFB0C4BD49 CRC64;
MLHCRCRGPT FVVGARHIRG NSANLIYCAH DSNEKHLLDN LAYLDFEYHD REEGGLLEEG
ETYETTTKEA FVTVKPYLAW ECLYPEGIDM AALSPLDINA NLRPRQAAHK ERTKAPPAKV
SPREKDHPPP PPADVHEPPS SDRPNGATYK TGKLLGKGGF AICYDGVLAG TREKYALKIV
KSIMPQKKME QKFQTELQIH SKMRHANIVQ FHRAFAYQES TYIVLELCPN GSLMDMVKKR
RFVTEPEVRF YTIQIAGAIK YMHSKGIIHR DLKMGNIFLD KDMNVKVGDF GLAALLMSGK
DMTACRRTTL CGTPNYIAPE ILEKGKGGHD HAVDIWSLGI IIFAMLTGRP PFQSTTQDEI
YRKAREREYD WPSLDKTNNY ISQEAKDLVS LLLQSPEERP DCDTIVQHPF FSSGWVPQEE
EMTPSLRENS PDPNQFATLS LRGGRASLYA RNLKALCVKS DVGPWSTTQK VHSSTYREVA
AEEKAGLTPA VPLAGNVVYR PFDEVVREHK ATLAREESTV AAKSTEYDQK PLTHRPVTVA
STSKTVPRSF AAQQRAQNQP PTISATARRP RAQVESAPST RRANPSDQAS EEEQVSTETR
TRSRREPSRS QSKVKAVSES VVSAEARLGA DMVQQLGRSN SETTIPPVKT SSRDPTFASI
FSPSENAEFL HRSKPRHVTK NLQILYAEIE RALNSRSVGP AREAPDSEPT IVVKWVDYTN
KFGLGYILND GGVGCIFKSL PVSGDANTLV PPTCVVVRNA EKHLQNRRNP NYPDRHQLVP
VSGADIEFFE NNGDEGISCV KVNPRAFAAS EEYGAAGKLG RGKDEWEDRK REKIVLWRKF
ANYMTVFGRD QDHPYDDALN RTSMDGESDS SDPNKSNVVT FYQRFGDVGC WGFRNGSFQF
NFPDHTKILL SADGTWCDFY HLPLEAARDL ALTGNLPSAA LDDRQHLSFP TQAFLNFMTK
PSTRNGMASR RRAIQVDPMI QGIPAANDFR RKIEFIKAIV GEWITNGGIG RSAMEPESRL
RWLGNRELVN VKVPFKHVWV TVGAYGGDDR RVAWFDPREP KIRREVARHI ATNELSSLVS
NVGAVKVAST SKLQYERLAP RLNTIIPINP AQLNSTSHIP NVSMKQLATR TTTRSFGRYI
CRSCSRQAPR QRRAYATESS PELYDVVCVG GGPAGLSVLA ALRATAATSG LKVALIESQD
LSRTRSWSLP SSQYSNRCSS LTPTSVEFLD KIGAWKNVRR DRVQPYEEMQ VWDGVTGTRI
EFDWPQGSQG KTIAYMNENL NLTSGLLKRI DELSGVSIFD NTKVENIELG QETETADLRS
WPIVQLSGGR QIAARLLVGA DGANSPVRAF AGINSSGWDY NRHGVVATVE LEGDGWGGED
RKVAYQRFLP TGPAAMLPLP GRFSTLVWST TPERAALLKT LSTEDFTAMV NAAFRLSPVD
LTYMHTLTSG QADEYNWRSQ HTSSDSNRIP QRVLSVQEGT VASFPLKMRH ADTYIGERVA
LIGDAAHTVH PLAGQGLNQG QGDVESLVKT IEYSVTHGLD IGVSMSLESY NADRYAKNHV
MMGVVDKLHK LYAFESGPIV PLRSIGLSAV NALGPLKHFF MGQAAGTGAK IFTPANSRLE
LVIAMQQDVN ALSEVNKVVK QAIKHYIQIP NICQA
//
