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Database: UniProt
Entry: M1PDW6_BARAA
LinkDB: M1PDW6_BARAA
Original site: M1PDW6_BARAA 
ID   M1PDW6_BARAA            Unreviewed;       553 AA.
AC   M1PDW6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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   Name=etf {ECO:0000313|EMBL:AGF74796.1};
GN   OrderedLocusNames=BAnh1_09230 {ECO:0000313|EMBL:AGF74796.1};
OS   Bartonella australis (strain Aust/NH1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF74796.1, ECO:0000313|Proteomes:UP000011729};
RN   [1] {ECO:0000313|EMBL:AGF74796.1, ECO:0000313|Proteomes:UP000011729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF74796.1,
RC   ECO:0000313|Proteomes:UP000011729};
RX   PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA   Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA   Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT   "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT   the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL   PLoS Genet. 9:E1003393-E1003393(2013).
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; CP003123; AGF74796.1; -; Genomic_DNA.
DR   RefSeq; WP_015398303.1; NC_020300.1.
DR   AlphaFoldDB; M1PDW6; -.
DR   STRING; 1094489.BAnh1_09230; -.
DR   KEGG; baus:BAnh1_09230; -.
DR   PATRIC; fig|1094489.3.peg.1133; -.
DR   eggNOG; COG0644; Bacteria.
DR   eggNOG; COG2440; Bacteria.
DR   HOGENOM; CLU_009667_4_1_5; -.
DR   OrthoDB; 9766632at2; -.
DR   Proteomes; UP000011729; 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; 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;  61402 MW;  2F3EFEF3AD6D0D4B CRC64;
     MNAKMAHQRE SMEFDIVIVG AGPAGLSAAI RLKQVNPGLS VIVLEKGAEI GAHILSGAII
     DPIGINTLLP GWKNEQNHPF KTLVTNDQFF LLKPKRARLF PNALRPKILS NDGCYIVSLG
     DVCRWLSKKA EALGVEIYPG FAASDVLYND DGAVIGVLTG DMGLKKDETP GKNYMPGMAL
     LAKYTLIAEG ARGSIAKQLI QKFDLSKDRE PQKFGLGLKE LWEVDPQKHK LGLIQHFTGW
     PLDNNTGGGG FLYHQEENLI SVGFVVHLDY KNPYLSPFEE FQRFKTHPKL YEIFKGAKRL
     AYGARAISEG GWQSVPKLTF PGGALIGCSA GFVNVPRIKG SHNAILSGIL AANKIATALA
     QGRAHDEVKE IEDHWRKSLI GKDLYKTRNA KPLWAKYGTN YGIKLAGFDM WWQQLFGFSL
     FKTLPHGKED YACLEPAEKF KPIAYPKPDG IVTFDRLSSI ALSNIHHEEN QPCHLKIASL
     EKQKSSEYTI YRGPSARYCP AAVYEWLDYN NQKNYVINAS NCIHCKTCDI KDPNQNINWI
     CPQGGDGPVY PNM
//
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