GenomeNet

Database: UniProt
Entry: A0A0Q8XRN0_9SPHN
LinkDB: A0A0Q8XRN0_9SPHN
Original site: A0A0Q8XRN0_9SPHN 
ID   A0A0Q8XRN0_9SPHN        Unreviewed;       550 AA.
AC   A0A0Q8XRN0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-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=ASE13_05985 {ECO:0000313|EMBL:KRC81901.1};
OS   Sphingomonas sp. Root241.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736501 {ECO:0000313|EMBL:KRC81901.1, ECO:0000313|Proteomes:UP000051629};
RN   [1] {ECO:0000313|EMBL:KRC81901.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC81901.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC81901.1, ECO:0000313|Proteomes:UP000051629}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root241 {ECO:0000313|EMBL:KRC81901.1,
RC   ECO:0000313|Proteomes:UP000051629};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRC81901.1}.
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; LMIV01000001; KRC81901.1; -; Genomic_DNA.
DR   RefSeq; WP_056612650.1; NZ_LMIV01000001.1.
DR   AlphaFoldDB; A0A0Q8XRN0; -.
DR   STRING; 1736501.ASE13_05985; -.
DR   OrthoDB; 9766632at2; -.
DR   Proteomes; UP000051629; Unassembled WGS sequence.
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   PRINTS; PR00420; RNGMNOXGNASE.
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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT   DOMAIN          212..306
FT                   /note="ETF-QO/FixC ubiquinone-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21162"
FT   DOMAIN          447..547
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
SQ   SEQUENCE   550 AA;  60037 MW;  B7167CBFD2E25D43 CRC64;
     MSERESMPYD VVIVGAGPSG LAAAIRLKQL AAEGEQELSV CILEKGSEVG AHILSGAVVD
     PRALDELLPD WRDDCPLAAT PVTENHHWIL TEKGKASFPE FITPPFLHNK GTYTGSLGNL
     CRWLAGKAEE LGVEIFPGFA AAEILYNDDG SVKGVATGDM GVARDGHHKP DYAPGLELHA
     KYTLFGEGVR GHLSKQLQRQ FDLCRGAQPQ VYGIGIKELW DIDPANHLLG KVIHTQGWPL
     KDGESNGGGF LYHQADGQVA LGFVVWLNYK NPYLSPFHEM QRWKTHPAIA AILKGGKRVS
     YGARAISDGG WQSVPKLVMP GAALIGDTAG FLNVPRIKGT HTAMKSGMMA AEAAFAAVQA
     GRSNDELTAY PEAYKTSWVE KELRGVRNVV PLVKKFGDIW GTILSGAAMW MELIGLRWPF
     TMKHHPDHES LWHASAATPI EYPKPDGVLT FDRLSSVFIS NTNHEEDQPV HLTLKDPDIP
     IGYNLPVYAE PAQRYCPAGV YEVVGEGDDL RFQINAQNCV HCKTCDIKDP TQNINWVVPE
     GGGGPNYPNM
//
DBGET integrated database retrieval system