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ETFD_ACIAD
ID   ETFD_ACIAD              Reviewed;         570 AA.
AC   P94132;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable 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   Name=etfD; OrderedLocusNames=ACIAD1680;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9294455; DOI=10.1128/jb.179.18.5935-5942.1997;
RA   Williams P.A., Shaw L.E.;
RT   "mucK, a gene in Acinetobacter calcoaceticus ADP1 (BD413), encodes the
RT   ability to grow on exogenous cis,cis-muconate as the sole carbon source.";
RL   J. Bacteriol. 179:5935-5942(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
CC   -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster.;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
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DR   EMBL; U87258; AAC27118.1; -; Genomic_DNA.
DR   EMBL; CR543861; CAG68525.1; -; Genomic_DNA.
DR   RefSeq; WP_004926550.1; NC_005966.1.
DR   AlphaFoldDB; P94132; -.
DR   SMR; P94132; -.
DR   STRING; 62977.ACIAD1680; -.
DR   EnsemblBacteria; CAG68525; CAG68525; ACIAD1680.
DR   GeneID; 45234070; -.
DR   KEGG; aci:ACIAD1680; -.
DR   eggNOG; COG0644; Bacteria.
DR   eggNOG; COG2440; Bacteria.
DR   HOGENOM; CLU_009667_4_1_6; -.
DR   OMA; APSWHIV; -.
DR   OrthoDB; 1770293at2; -.
DR   BioCyc; ASP62977:ACIAD_RS07745-MON; -.
DR   Proteomes; UP000000430; 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; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   4: Predicted;
KW   4Fe-4S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Oxidoreductase; Reference proteome; Transport; Ubiquinone.
FT   CHAIN           1..570
FT                   /note="Probable electron transfer flavoprotein-ubiquinone
FT                   oxidoreductase"
FT                   /id="PRO_0000200681"
FT   DOMAIN          530..559
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT   BINDING         13..27
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   BINDING         515
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         539
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         542
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         545
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   570 AA;  62996 MW;  0107DD88E78A7DE5 CRC64;
     MITIEREAME FDVVIVGAGP AGLSAAIKIR QLAIENNLPD LSVCVVEKGS EVGAHILSGA
     VLEPRAINEL FPNWKEEGAP LNVPVTEDKT YFLMSDEKSQ EAPHWMVPKT MHNDGNYVIS
     LGNVVRWLGQ KAEELEVSIF PGFAAAEILY HADGTVKGIQ TGDMGIGKDG EPTHNFAPGY
     ELHAKYTLFA EGCRGHLGKR LINKFNLDQD ADPQHYGIGI KELWEIDPAK HKPGLVMHGS
     GWPLSETGSS GGWWLYHAEN NQVTLGMIVD LSYENPHMFP FMEMQRWKTH PLIKQYLEGG
     KRISYGARAV VKGGLNSLPK LTFPGGCLIG DDAGFLNFAK IKGSHTAMKS GMLCGEAVFE
     AIARGVDKGG DLAIARVVEG EDLFDKELTT YTQKFDKSWL KEELHRSRNF GPAMHKFGLW
     IGGAFNFVDQ NIFKVPFTLH DLQPDYSALK TQDQATFKPN YPKPDGKLTF DRLSSVFVSN
     TVHEENQPSH LKLTDASIPV AVNLPRWDEP AQRYCPAGVY EIVDEGEGNK RFQINAANCV
     HCKTCDIKDP SQNITWVTPE GGGGPNYPNM
 
 
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