ID   ETFA_MYCTO              Reviewed;         318 AA.
AC   P9WNG8; L0TBC1; O53275;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
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; Synonyms=fixB; OrderedLocusNames=MT3112;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47442.1; -; Genomic_DNA.
DR   PIR; G70858; G70858.
DR   RefSeq; WP_003899889.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNG8; -.
DR   SMR; P9WNG8; -.
DR   EnsemblBacteria; AAK47442; AAK47442; MT3112.
DR   KEGG; mtc:MT3112; -.
DR   PATRIC; fig|83331.31.peg.3354; -.
DR   HOGENOM; CLU_034178_0_1_11; -.
DR   Proteomes; UP000001020; 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; Transport.
FT   CHAIN           1..318
FT                   /note="Electron transfer flavoprotein subunit alpha"
FT                   /id="PRO_0000427129"
FT   BINDING         257..285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  31691 MW;  3C155E4CF5B0FE2D CRC64;
     MAEVLVLVEH AEGALKKVSA ELITAARALG EPAAVVVGVP GTAAPLVDGL KAAGAAKIYV
     AESDLVDKYL ITPAVDVLAG LAESSAPAGV LIAATADGKE IAGRLAARIG SGLLVDVVDV
     REGGVGVHSI FGGAFTVEAQ ANGDTPVITV RAGAVEAEPA AGAGEQVSVE VPAAAENAAR
     ITAREPAVAG DRPELTEATI VVAGGRGVGS AENFSVVEAL ADSLGAAVGA SRAAVDSGYY
     PGQFQVGQTG KTVSPQLYIA LGISGAIQHR AGMQTSKTIV AVNKDEEAPI FEIADYGVVG
     DLFKVAPQLT EAIKARKG