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Database: UniProt
Entry: A0A067STH6_GALM3
LinkDB: A0A067STH6_GALM3
Original site: A0A067STH6_GALM3 
ID   A0A067STH6_GALM3        Unreviewed;       693 AA.
AC   A0A067STH6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase {ECO:0000256|RuleBase:RU366068};
DE            Short=ETF-QO {ECO:0000256|RuleBase:RU366068};
DE            EC=1.5.5.1 {ECO:0000256|RuleBase:RU366068};
GN   ORFNames=GALMADRAFT_71140 {ECO:0000313|EMBL:KDR74250.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR74250.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC       {ECO:0000256|RuleBase:RU366068}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + reduced [electron-transfer flavoprotein] = a
CC         ubiquinol + H(+) + oxidized [electron-transfer flavoprotein];
CC         Xref=Rhea:RHEA:24052, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566,
CC         Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57692,
CC         ChEBI:CHEBI:58307; EC=1.5.5.1;
CC         Evidence={ECO:0000256|RuleBase:RU366068};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU366068};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU366068};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|RuleBase:RU366068};
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DR   EMBL; KL142383; KDR74250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067STH6; -.
DR   STRING; 685588.A0A067STH6; -.
DR   HOGENOM; CLU_009667_4_0_1; -.
DR   OrthoDB; 275372at2759; -.
DR   Proteomes; UP000027222; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.30.70.20; -; 2.
DR   Gene3D; 3.30.9.90; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR040156; ETF-QO.
DR   InterPro; IPR049398; ETF-QO/FixC_UQ-bd.
DR   InterPro; IPR007859; ETF-QO/FixX_C.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR10617; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR10617:SF107; ELECTRON TRANSFER FLAVOPROTEIN-UBIQUINONE OXIDOREDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF05187; ETF_QO; 3.
DR   Pfam; PF21162; ETFQO_UQ-bd; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU366068};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU366068};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU366068};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU366068};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU366068};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU366068};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027222};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT   DOMAIN          255..350
FT                   /note="ETF-QO/FixC ubiquinone-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21162"
FT   DOMAIN          509..549
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
FT   DOMAIN          576..640
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
FT   DOMAIN          650..687
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
FT   REGION          468..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..497
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   693 AA;  75549 MW;  7A6B7F183F54B1E0 CRC64;
     MLRCRKPLFI PKLTRIRTFR TSAVRKNAIF NPATVERAED EVDVCIVGGG PAGLSAAIRL
     KQLEREKGNE IRVVVLEKGS EIGSHIVSGA VIEPRALNEL LPDWSSMSDH PLTQPTTSSR
     MLFLTPKHAV PIPHPPQMGN KGNYVVSLSQ FTRWLAGVAE NEFGVEVYPG FAGAQLLLSE
     DADALDPWGN KVRSVQGVVT NEVGLTRKFH MKPSFEPGMA FRAKVTLLAE GAHGSLSKQA
     IGLYDLRKES QPQTYGIGLK EVWRVDPEKH KPGEVVHTIG WPLDMQTYGG GWVYHMNGGL
     VSLGLVIGLD YKNPWISPYR ELQKMKHHPY FRSLLSSPKA ERLSYAARVL NEGGLQSVPK
     LNFPGGALIG CSAGFVNIAK IKGTHNAMKS GMLAAEAAWD VVHPESESAS DMSAYDSALH
     KSWIHTDLHE VRNLRASFGT RLGMLGGVLY SGIDSLFLKG RVPWTFKHHK PASSSGKESD
     FPTSSLDASL TQPASSHNPP VYPAFEAPLS TDLLTSVALT GTNHAEDQPV HLRVVRTARY
     VEEVVDKAKE GKGNVAVGAG LDAVRAEAEV LGCEKEAEAE EVREEVERRQ AHVRVNVGEY
     AGLLGRACPA GVYEYVPDEE GGAKEGWDGK KLVINSQVCA FTLLLPISIS FRCSSQNCIH
     CKLCDVKVPT QDITWTVPEG GGGPKYSEFF LTV
//
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