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Database: UniProt
Entry: J0ZJJ7_BARVI
LinkDB: J0ZJJ7_BARVI
Original site: J0ZJJ7_BARVI 
ID   J0ZJJ7_BARVI            Unreviewed;       553 AA.
AC   J0ZJJ7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=ME1_00629 {ECO:0000313|EMBL:EJF88458.1};
OS   Bartonella vinsonii subsp. arupensis OK-94-513.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094562 {ECO:0000313|EMBL:EJF88458.1, ECO:0000313|Proteomes:UP000002304};
RN   [1] {ECO:0000313|EMBL:EJF88458.1, ECO:0000313|Proteomes:UP000002304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK-94-513 {ECO:0000313|EMBL:EJF88458.1,
RC   ECO:0000313|Proteomes:UP000002304};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Kirby J., Kosoy M., Birtles R., Probert W.S.,
RA   Chiaraviglio L., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Bartonella vinsonii subsp. arupensis OK-94-513.";
RL   Submitted (MAR-2012) 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:EJF88458.1}.
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DR   EMBL; AILZ01000013; EJF88458.1; -; Genomic_DNA.
DR   RefSeq; WP_004863179.1; NZ_JH725037.1.
DR   AlphaFoldDB; J0ZJJ7; -.
DR   STRING; 1094562.ME1_00629; -.
DR   PATRIC; fig|1094562.3.peg.719; -.
DR   HOGENOM; CLU_009667_4_1_5; -.
DR   Proteomes; UP000002304; 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; PF01946; Thi4; 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          214..307
FT                   /note="ETF-QO/FixC ubiquinone-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21162"
FT   DOMAIN          450..550
FT                   /note="ETF-QO/FixX C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05187"
SQ   SEQUENCE   553 AA;  61305 MW;  803F90A475148118 CRC64;
     MNASLHQQRE SMEFDIVIVG AGPAGLSAAI RLKQINPELS VTIVEKGAEV GAHILSGAVV
     DPIGIDTLLP EWRNEHDHPF KTPVTSDQFF FLKPQHATLF PNIFHPKILS NNGCYIVSLG
     DVCRWLSKKA EALGVEIYPG FAISETIQND KGAIIGVLTG DMGINKDGTL GKNYMPGMAL
     LAKYILIAEG ARGSIAKQLI KKFDLSNNRE PQKFGLGFKE LWEIDPQKHK SGLVQHFAGW
     PLDDNTGGGG FLYHQENNLI SVGFVVHLDY KNPYLSPFEE FQRFKTHPKL YEIFKGAKRL
     SYGARVISEG GWQSVPKLTF PGGALIGCSA GFVNVPRIKG SHNAILSGIL AAEKIAIALA
     QGRAHDEVKE IEEHWRKGPI GKDLYKVRNA KPLWAKYGTK YGIKLAGFDI WWQQLFGFSL
     FKTLPHGKAD YACLEPAAKF NPIAYPKPDG IVTFDRLSSV ALSNTHHEEN QPCHLKISSL
     EKQKDSEYAI YAGPSARYCP VAVYEWLNHH DQPTYVINAS NCIHCKTCDI KDPNQNINWT
     CPQGSEGPLY LNM
//
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