位置:首页 > 蛋白库 > ETFA_CLOAB
ETFA_CLOAB
ID   ETFA_CLOAB              Reviewed;         336 AA.
AC   P52039;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Electron transfer flavoprotein subunit alpha;
DE            Short=Alpha-ETF;
DE   AltName: Full=Electron transfer flavoprotein large subunit;
DE            Short=ETFLS;
GN   Name=etfA; OrderedLocusNames=CA_C2709;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=8655474; DOI=10.1128/jb.178.11.3015-3024.1996;
RA   Boynton Z.L., Bennett G.N., Rudolph F.B.;
RT   "Cloning, sequencing, and expression of clustered genes encoding beta-
RT   hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA
RT   dehydrogenase from Clostridium acetobutylicum ATCC 824.";
RL   J. Bacteriol. 178:3015-3024(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC       electron acceptor for other dehydrogenases. It transfers the electrons
CC       to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF
CC       dehydrogenase) (By similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per dimer. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U17110; AAA95970.1; -; Genomic_DNA.
DR   EMBL; AE001437; AAK80655.1; -; Genomic_DNA.
DR   PIR; D97233; D97233.
DR   PIR; T47264; T47264.
DR   RefSeq; NP_349315.1; NC_003030.1.
DR   RefSeq; WP_010965996.1; NC_003030.1.
DR   AlphaFoldDB; P52039; -.
DR   SMR; P52039; -.
DR   STRING; 272562.CA_C2709; -.
DR   PRIDE; P52039; -.
DR   DNASU; 1118892; -.
DR   EnsemblBacteria; AAK80655; AAK80655; CA_C2709.
DR   GeneID; 44999198; -.
DR   KEGG; cac:CA_C2709; -.
DR   PATRIC; fig|272562.8.peg.2899; -.
DR   eggNOG; COG2025; Bacteria.
DR   HOGENOM; CLU_034178_1_1_9; -.
DR   OMA; YKHVWVF; -.
DR   OrthoDB; 1400253at2; -.
DR   BioCyc; MetaCyc:MON-21349; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   CDD; cd01715; ETF_alpha; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR014730; ETF_a/b_N.
DR   InterPro; IPR001308; ETF_a/FixB.
DR   InterPro; IPR033947; ETF_alpha_N.
DR   InterPro; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR43153; PTHR43153; 1.
DR   Pfam; PF01012; ETF; 1.
DR   Pfam; PF00766; ETF_alpha; 1.
DR   PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR   SMART; SM00893; ETF; 1.
DR   SUPFAM; SSF52467; SSF52467; 1.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   Electron transport; FAD; Flavoprotein; Reference proteome; Transport.
FT   CHAIN           1..336
FT                   /note="Electron transfer flavoprotein subunit alpha"
FT                   /id="PRO_0000167847"
FT   BINDING         275..303
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        169
FT                   /note="F -> FF (in Ref. 1; AAA95970)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   336 AA;  35964 MW;  B8AA0538330A730B CRC64;
     MNKADYKGVW VFAEQRDGEL QKVSLELLGK GKEMAEKLGV ELTAVLLGHN TEKMSKDLLS
     HGADKVLAAD NELLAHFSTD GYAKVICDLV NERKPEILFI GATFIGRDLG PRIAARLSTG
     LTADCTSLDI DVENRDLLAT RPAFGGNLIA TIVCSDHRPQ MATVRPGVFE KLPVNDANVS
     DDKIEKVAIK LTASDIRTKV SKVVKLAKDI ADIGEAKVLV AGGRGVGSKE NFEKLEELAS
     LLGGTIAASR AAIEKEWVDK DLQVGQTGKT VRPTLYIACG ISGAIQHLAG MQDSDYIIAI
     NKDVEAPIMK VADLAIVGDV NKVVPELIAQ VKAANN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024