ID A0A127MEP3_9SPHN Unreviewed; 551 AA.
AC A0A127MEP3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=AZE99_07565 {ECO:0000313|EMBL:AMO71724.1};
OS Sphingorhabdus sp. M41.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingorhabdus.
OX NCBI_TaxID=1806885 {ECO:0000313|EMBL:AMO71724.1, ECO:0000313|Proteomes:UP000073959};
RN [1] {ECO:0000313|EMBL:AMO71724.1, ECO:0000313|Proteomes:UP000073959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:AMO71724.1,
RC ECO:0000313|Proteomes:UP000073959};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000256|ARBA:ARBA00002819, 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014545; AMO71724.1; -; Genomic_DNA.
DR RefSeq; WP_067199446.1; NZ_CP014545.1.
DR AlphaFoldDB; A0A127MEP3; -.
DR STRING; 1806885.AZE99_07565; -.
DR KEGG; sphg:AZE99_07565; -.
DR OrthoDB; 9766632at2; -.
DR Proteomes; UP000073959; Chromosome.
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; IPR017896; 4Fe4S_Fe-S-bd.
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.
DR PROSITE; PS51379; 4FE4S_FER_2; 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 Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 511..540
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 551 AA; 60856 MW; 28A3EA5DA885CCCC CRC64;
MSERESMPYD LVIVGGGPAG LSAAIKFKQL ADEAGKDLSV CILEKGSEIG AHILSGAVID
PKGLDELFPA WRDEDCPLAN TPVTENHHWI LTKKKKFSIP HFITPSFMHN KGTYTGSLGN
LCRWLGERAE YMGIEIFPGF AAAEILYNED GSVKGVATGD MGVARDGSHK PDYQPGLELH
AKYTFFAEGA RGHLTKILKN QFALDAESQP QIYGLGVKEL WDIDPAKHKP GRVIHSQGWP
LSEGANGGGF IYHQADNQVA LGFVTWLNYE NPYLSPFEEM QRWKQHPEVR KILEGGKRVS
YGARAINDGG FQAVPKLYFP GGALIGCSAG FVNVPRIKGT HTAMKTGMMA AEAAYEAIVA
ERANDELTAY GTAYENSWVR EELRVVRNVL PAVEKYGDFL GTILSGITMW AEHLKIKMPF
TMKLHPDWSR LRRAEHCVKI EYPKPDGVIS FDRLSSVFLS NTNHEEDQPV HLQLKDPNIP
VDVNLPVFAG PSARYCPAGV YEFVEDEAGN PKFQINAQNC VHCKTCDIKD PSQNINWVVP
EGGGGPNYPN M
//