UniProt: A0A2S2FAI0

Database: UniProt
Entry: A0A2S2FAI0_9GAMM

LinkDB:  A0A2S2FAI0_9GAMM 
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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (5)   
   Pfam (3)   
   PROSITE (1)   
All databases (16)   

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ID   A0A2S2FAI0_9GAMM        Unreviewed;       570 AA.
AC   A0A2S2FAI0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=DJ533_04625 {ECO:0000313|EMBL:AWL27920.1};
OS   Acinetobacter defluvii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1871111 {ECO:0000313|EMBL:AWL27920.1, ECO:0000313|Proteomes:UP000245977};
RN   [1] {ECO:0000313|Proteomes:UP000245977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHA30 {ECO:0000313|Proteomes:UP000245977};
RA   Hu Y., Qin J., Feng Y., Zong Z.;
RT   "The complete genome of Acinetobacter defluvii strain WCHAD010030.";
RL   Submitted (MAY-2018) 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};
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DR   EMBL; CP029397; AWL27920.1; -; Genomic_DNA.
DR   RefSeq; WP_065994037.1; NZ_CP029397.2.
DR   AlphaFoldDB; A0A2S2FAI0; -.
DR   STRING; 1871111.GCA_001704615_03378; -.
DR   KEGG; adv:DJ533_04625; -.
DR   OrthoDB; 9766632at2; -.
DR   Proteomes; UP000245977; 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:UP000245977};
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;  62880 MW;  912A9BF1BB2DB77D CRC64;
     MEHIERESME FDVVIVGAGP AGLSAAIKIR QLAIENNLPD LSVCVVEKGS EVGAHILSGA
     VLEPRAINEL FPNWKEEGAP LNVPVTEDHT FFTLSATTSK QAPHWMVPKT MHNEGNYIVS
     LGNVVRWLGT KAEELEVSIF PGFAASEILY HEDGSVKGIQ TGDMGIGKDG EPTHNFTPGY
     ELHAKYTIFA EGCRGHLGKR LIAKYNLDQD ADPQHYGIGI KELWEIDPAK HKPGLVMHGT
     GWPLNETGSS GGWWLYHAEN NQVTLGLIVD LSYQNPHMYP FAEMQRWKTH PLIKQYLEGG
     KRISYGARAI TKGGINALPK LTFPGGCLVG DDAGFLNFAK IKGSHTAMKS GMLCGEAVFE
     AIQAGVAKGG EVGYARVVEG EDFFIKELTS YTDKFNNSWL KEELHRSRNF GPAMHKFGQW
     IGGAFNFIDQ NIFQVPFTLH DLVPDFSALK TVDAATFKPD YPKPDGKLTF DRLSSVFVSN
     TVHEENQPAH LKLTDPTIPV NVNLPKWDEP AQRYCPAGVY EIMENDDGSK RFQINAANCV
     HCKTCDIKDP SQNITWVTPE GGGGPNYPNM
//

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