ID F0KLF6_ACICP Unreviewed; 570 AA.
AC F0KLF6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=etfD {ECO:0000313|EMBL:ADY83873.1};
GN OrderedLocusNames=BDGL_003287 {ECO:0000313|EMBL:ADY83873.1};
OS Acinetobacter calcoaceticus (strain PHEA-2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=871585 {ECO:0000313|EMBL:ADY83873.1, ECO:0000313|Proteomes:UP000007477};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PHEA-2;
RA Zhan Y., Yan Y., Zhang W., Chen M., Ping S., Lu W., Lin M.;
RT "The genome sequence of a nonpathogenic wastewater-adapted bacterium
RT Acinetobacter calcoaceticus PHEA-2 and comparative genomics insights into
RT environmental adaptation.";
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADY83873.1, ECO:0000313|Proteomes:UP000007477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHEA-2 {ECO:0000313|EMBL:ADY83873.1,
RC ECO:0000313|Proteomes:UP000007477};
RX PubMed=21441526; DOI=10.1128/JB.00261-11;
RA Zhan Y., Yan Y., Zhang W., Yu H., Chen M., Lu W., Ping S., Peng Z.,
RA Yuan M., Zhou Z., Elmerich C., Lin M.;
RT "Genome sequence of Acinetobacter calcoaceticus PHEA-2, isolated from
RT industry wastewater.";
RL J. Bacteriol. 193:2672-2673(2011).
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};
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DR EMBL; CP002177; ADY83873.1; -; Genomic_DNA.
DR RefSeq; WP_005065953.1; NC_016603.1.
DR RefSeq; YP_004997555.1; NC_016603.1.
DR AlphaFoldDB; F0KLF6; -.
DR STRING; 871585.BDGL_003287; -.
DR GeneID; 11637950; -.
DR KEGG; acc:BDGL_003287; -.
DR PATRIC; fig|871585.3.peg.3282; -.
DR eggNOG; COG0644; Bacteria.
DR eggNOG; COG2440; Bacteria.
DR HOGENOM; CLU_009667_4_1_6; -.
DR OrthoDB; 9766632at2; -.
DR Proteomes; UP000007477; 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; 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000007477};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU366068};
KW Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU366068}.
FT DOMAIN 530..559
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 570 AA; 63018 MW; 02006A492976673C CRC64;
MEHIERESME FDVVIVGAGP AGLSAAIKIR QLAIEKNLPD LSVCVVEKGS EVGAHILSGA
VLEPRAINEL FPNWKEEGAP LNVPVTEDKT FFLLSDTTSK EVPHWMVPKT MHNDGNYVIS
LGNVVRWLGQ KAEELEVSIF PGFAASEVLY HEDGTVKGIQ TGDMGIGKDG EPTHNFTPGY
ELHAKYTLFA EGCRGHLGKR LIAKYNLDKD ADPQHYGIGI KELWEIDPAK HKPGLVMHGA
GWPLAETASS GGWWLYHAEN NQVTLGMIVD LSYENPHMYP FMEMQRWKTH PLIKQYLEGG
KRISYGARAV VKGGFNSLPK LTFPGGCLIG DDAGFLNFAK IKGSHTAMKS GMLCGEAVFE
AIAAGVEKGG DLAIARVTEG EDLFVKELTS YTDKFNNSWL KEELYNSRNF GPAMHKFGQW
MGGAFNFIDQ NVFKVPFTLH DLKQDFAALK TVDATSFKPN YPKPDGKLTF DRLSSVFISN
TVHEENQPAH LKLTDPSIPV NVNLPKWDEP AQRYCPAGVY EIMENDDGSK RFQINAANCV
HCKTCDIKDP SQNITWVTPE GGGGPNYPNM
//
