ETFD_PSEAE
ID ETFD_PSEAE Reviewed; 551 AA.
AC Q9HZP5;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase;
DE Short=ETF-QO;
DE Short=ETF-ubiquinone oxidoreductase;
DE EC=1.5.5.1;
DE AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE Short=ETF dehydrogenase;
GN OrderedLocusNames=PA2953;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 62-90 AND 363-376.
RC STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
CC -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
CC {ECO:0000250|UniProtKB:Q16134}.
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:0000250|UniProtKB:Q16134};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q16134};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q16134};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q16134};
CC -!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06341.1; -; Genomic_DNA.
DR PIR; D83277; D83277.
DR RefSeq; NP_251643.1; NC_002516.2.
DR RefSeq; WP_003102932.1; NZ_QZGE01000009.1.
DR AlphaFoldDB; Q9HZP5; -.
DR SMR; Q9HZP5; -.
DR STRING; 287.DR97_4986; -.
DR PaxDb; Q9HZP5; -.
DR PRIDE; Q9HZP5; -.
DR EnsemblBacteria; AAG06341; AAG06341; PA2953.
DR GeneID; 880159; -.
DR KEGG; pae:PA2953; -.
DR PATRIC; fig|208964.12.peg.3099; -.
DR PseudoCAP; PA2953; -.
DR HOGENOM; CLU_009667_4_1_6; -.
DR InParanoid; Q9HZP5; -.
DR OMA; GGGWMYH; -.
DR PhylomeDB; Q9HZP5; -.
DR BioCyc; PAER208964:G1FZ6-3004-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR040156; ETF-QO.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR10617; PTHR10617; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Direct protein sequencing; Electron transport; FAD; Flavoprotein;
KW Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Reference proteome;
KW Transport; Ubiquinone.
FT CHAIN 1..551
FT /note="Electron transfer flavoprotein-ubiquinone
FT oxidoreductase"
FT /id="PRO_0000200683"
FT DOMAIN 511..540
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 10..24
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 496
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q16134, ECO:0000255"
FT BINDING 520
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q16134, ECO:0000255"
FT BINDING 523
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q16134, ECO:0000255"
FT BINDING 526
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q16134, ECO:0000255"
SQ SEQUENCE 551 AA; 59929 MW; D7EA049B8992893F CRC64;
MEREYMEFDV VIVGAGPAGL SAACRLKQKA AEAGQEISVC VVEKGSEVGA HILSGAVFEP
RALNELFPDW KELGAPLNTP VTGDDIYVLK SAESATKVPN FFVPKTMHNE GNYIISLGNL
CRWLAQQAEG LGVEIYPGFA AQEALIDENG VVRGIVTGDL GVDREGNPKE GYYTPGMELR
AKYTLFAEGC RGHIGKQLIK KYNLDSEADA QHYGIGIKEI WDIDPSKHKP GLVVHTAGWP
LNDENTGGSF LYHLENNQVF VGLIIDLSYS NPHLSPFDEF QRYKHHPVVK QYLEGGKRVA
YGARAICKGG LNSLPKMVFP GGALIGCDLG TLNFAKIKGS HTAMKSGMLA ADAIAEALAA
GREGGDELSS YVDAFKASWL YDELFRSRNF GAAIHKFGAI GGGAFNFIDQ NIFGGKIPVT
LHDDKPDYAC LKKASEAPKI DYPKPDGKLS FDKLSSVFLS NTNHEEDQPI HLKLADASIP
IEKNLPLYDE PAQRYCPAGV YEVVANDDGS KRFQINAQNC VHCKTCDIKD PAQNITWVAP
EGTGGPNYPN M
