ETFA_METME
ID ETFA_METME Reviewed; 321 AA.
AC P53571;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
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;
OS Methylophilus methylotrophus (Bacterium W3A1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=17;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33, MASS
RP SPECTROMETRY, FUNCTION, AND COFACTOR.
RX PubMed=7798207; DOI=10.1016/s0021-9258(18)31609-0;
RA Chen D., Swenson R.P.;
RT "Cloning, sequence analysis, and expression of the genes encoding the two
RT subunits of the methylotrophic bacterium W3A1 electron transfer
RT flavoprotein.";
RL J. Biol. Chem. 269:32120-32130(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FAD AND TMADH.
RX PubMed=12567183; DOI=10.1038/nsb894;
RA Leys D., Basran J., Talfournier F., Sutcliffe M.J., Scrutton N.S.;
RT "Extensive conformational sampling in a ternary electron transfer
RT complex.";
RL Nat. Struct. Biol. 10:219-225(2003).
CC -!- FUNCTION: Heterodimeric electron transfer flavoprotein that accepts
CC electrons from trimethylamine dehydrogenase (PubMed:7798207). It
CC transfers the electrons to the main respiratory chain via ETF-
CC ubiquinone oxidoreductase (ETF dehydrogenase) (Probable).
CC {ECO:0000269|PubMed:7798207, ECO:0000305}.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:12567183, ECO:0000269|PubMed:7798207};
CC Note=Binds 1 FAD per dimer. {ECO:0000269|PubMed:12567183};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC {ECO:0000269|PubMed:12567183, ECO:0000269|PubMed:7798207}.
CC -!- MASS SPECTROMETRY: Mass=33672; Mass_error=34; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:7798207};
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; U17242; AAA64953.1; -; Genomic_DNA.
DR PIR; T47206; T47206.
DR PDB; 1O94; X-ray; 2.00 A; D/F=2-321.
DR PDB; 1O95; X-ray; 3.70 A; D/F=2-321.
DR PDB; 1O96; X-ray; 3.10 A; B/D/F/Z=2-321.
DR PDB; 1O97; X-ray; 1.60 A; D=2-321.
DR PDB; 3CLR; X-ray; 1.90 A; D=1-321.
DR PDB; 3CLS; X-ray; 1.65 A; D=1-321.
DR PDB; 3CLT; X-ray; 2.00 A; D=1-321.
DR PDB; 3CLU; X-ray; 1.80 A; D=1-321.
DR PDBsum; 1O94; -.
DR PDBsum; 1O95; -.
DR PDBsum; 1O96; -.
DR PDBsum; 1O97; -.
DR PDBsum; 3CLR; -.
DR PDBsum; 3CLS; -.
DR PDBsum; 3CLT; -.
DR PDBsum; 3CLU; -.
DR AlphaFoldDB; P53571; -.
DR SMR; P53571; -.
DR MINT; P53571; -.
DR STRING; 1122236.KB905144_gene2340; -.
DR EvolutionaryTrace; P53571; -.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; FAD;
KW Flavoprotein; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7798207"
FT CHAIN 2..321
FT /note="Electron transfer flavoprotein subunit alpha"
FT /id="PRO_0000167851"
FT BINDING 211
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 236..237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 250..254
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 268..275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT BINDING 307..308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:12567183,
FT ECO:0007744|PDB:1O96, ECO:0007744|PDB:3CLR,
FT ECO:0007744|PDB:3CLS, ECO:0007744|PDB:3CLU"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:1O97"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1O96"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3CLU"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:1O97"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1O97"
FT HELIX 308..318
FT /evidence="ECO:0007829|PDB:1O97"
SQ SEQUENCE 321 AA; 33723 MW; 25A566407E7F42E9 CRC64;
MSKILVIAEH RRNDLRPVSL ELIGAANGLK KSGEDKVVVA VIGSQADAFV PALSVNGVDE
LVVVKGSSID FDPDVFEASV SALIAAHNPS VVLLPHSVDS LGYASSLASK TGYGFATDVY
IVEYQGDELV ATRGGYNQKV NVEVDFPGKS TVVLTIRPSV FKPLEGAGSP VVSNVDAPSV
QSRSQNKDYV EVGGGNDIDI TTVDFIMSIG RGIGEETNVE QFRELADEAG ATLCCSRPIA
DAGWLPKSRQ VGQSGKVVGS CKLYVAMGIS GSIQHMAGMK HVPTIIAVNT DPGASIFTIA
KYGIVADIFD IEEELKAQLA A
