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Database: UniProt
Entry: K2S5E5_MACPH
LinkDB: K2S5E5_MACPH
Original site: K2S5E5_MACPH 
ID   K2S5E5_MACPH            Unreviewed;       628 AA.
AC   K2S5E5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=MPH_02470 {ECO:0000313|EMBL:EKG20237.1};
OS   Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Macrophomina.
OX   NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG20237.1, ECO:0000313|Proteomes:UP000007129};
RN   [1] {ECO:0000313|EMBL:EKG20237.1, ECO:0000313|Proteomes:UP000007129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS6 {ECO:0000313|EMBL:EKG20237.1,
RC   ECO:0000313|Proteomes:UP000007129};
RX   PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA   Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA   Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA   Saito J.A., Alam M.;
RT   "Tools to kill: Genome of one of the most destructive plant pathogenic
RT   fungi Macrophomina phaseolina.";
RL   BMC Genomics 13:493-493(2012).
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};
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:EKG20237.1}.
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DR   EMBL; AHHD01000091; EKG20237.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2S5E5; -.
DR   STRING; 1126212.K2S5E5; -.
DR   VEuPathDB; FungiDB:MPH_02470; -.
DR   eggNOG; KOG2415; Eukaryota.
DR   HOGENOM; CLU_009667_4_0_1; -.
DR   InParanoid; K2S5E5; -.
DR   OrthoDB; 275372at2759; -.
DR   Proteomes; UP000007129; 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   Gene3D; 3.30.70.20; -; 1.
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; 1.
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:UP000007129};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT   DOMAIN          286..379
FT                   /note="ETF-QO/FixC ubiquinone-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21162"
FT   DOMAIN          522..625
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
SQ   SEQUENCE   628 AA;  69833 MW;  5712CF2246FA65E1 CRC64;
     MASRIVAPNA LRRALVVRPR PAHFSTRTFI TAARRSPLDS YRPALRIAGQ RRSLSNTART
     RLADVDESFD PSQIEREADE VDVCIVGGGP AGLAAAIRLK QLANEQGNED FRVLLLEKAG
     EIGDHIVSGN VIEPSALNEL LPDWNSEENP NRFEHATPAK TEKMRFLTPN KSFWLPMPPQ
     MNNHGNYIIS LNQLVKWLGE RAEEVGVEIY PGFSASEILY TPDGSVKGVA TNDQGISRDG
     TPKDSFERGM EFHARCTLLA EGCHGSLTKQ VVKKFDLRRD SDHQTYGLGI KEVWEIDPAK
     FESGLVAHSL GYPLSKDTYG GGWMYHWNDN LVSIGLVVGL DYPNPWTSPY GEFQKMKQHP
     FYRQYLEGGK CISYAARTLN EGGFQSIPKC AFPGGALIGD TAGFLNLPKI KGTHTAMQSG
     MLAAEAAYTA LSGKSDQGTI FLYDYEDKLR NSSIWSELKE VRNMRPSFHN PLGLYGGILY
     SGITAFLLRG KEPWTFKHGT PDHAATKKAD ECKKIEYPKP DGKISFDILT SVSRSGTNHE
     EDQPVHLQVK DCDAHAAKEW PRFKGVENRF CPAGVYEYVE DESKDLGVRF QINSQNCVHC
     KTCDIKAPSQ DINWVCPTGG DGPKYYMT
//
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