ID A5I3W5_CLOBH Unreviewed; 349 AA.
AC A5I3W5; A7G5B8;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE SubName: Full=Electron transfer flavoprotein alpha-subunit {ECO:0000313|EMBL:CAL83735.1};
GN Name=etfA1 {ECO:0000313|EMBL:CAL83735.1};
GN OrderedLocusNames=CBO2194 {ECO:0000313|EMBL:CAL83735.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL83735.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL83735.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000089-1};
CC Note=Binds 1 FAD per dimer. {ECO:0000256|PIRSR:PIRSR000089-1};
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000256|ARBA:ARBA00005817}.
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DR EMBL; AM412317; CAL83735.1; -; Genomic_DNA.
DR RefSeq; WP_011986692.1; NC_009698.1.
DR RefSeq; YP_001254689.1; NC_009495.1.
DR RefSeq; YP_001387983.1; NC_009698.1.
DR AlphaFoldDB; A5I3W5; -.
DR GeneID; 5186449; -.
DR KEGG; cbh:CLC_2137; -.
DR KEGG; cbo:CBO2194; -.
DR PATRIC; fig|413999.7.peg.2162; -.
DR HOGENOM; CLU_034178_1_1_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 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; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR43153; ELECTRON TRANSFER FLAVOPROTEIN ALPHA; 1.
DR PANTHER; PTHR43153:SF1; ELECTRON TRANSFER FLAVOPROTEIN SUBUNIT ALPHA, MITOCHONDRIAL; 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; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000089-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000089-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 13..202
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 251..252
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 265..269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 282..289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 303
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 349 AA; 37872 MW; 70F7F698B69F9999 CRC64;
MDIKKDLSSY KNVWVIAEQR QGKITPVVIE LLGEGRKIAN DIGVELCAVL LGYNVDNLAD
ELIKFGADKV YYANDPLLEK YTTDGYAKVI VDAVNDIKPE IVLIGATHIG RDLAPRIASN
LDTGLTADCT KLEVDPEDKK LKQTRPAFGG NIMATIICPD NRPQMSTVRP GVMDKAVKDE
SRKGQILKLS ADLIKDDIRT EVIEIVKSKK ELVSLTDANF IVSGGLGLGN PDGFKLLKQL
ADRLGGVVGS SRAAVDAGWI ENSHQVGQTG TTVKPTVYIA CGISGAIQHL AGMQESDVII
AINKNESAPI FEVADYGIVG DLYDVVPKLL ELLDDDDRIN RLFEESKIV
//
