ETFA_PARDE
ID ETFA_PARDE Reviewed; 308 AA.
AC P38974;
DT 01-FEB-1995, 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 Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-8.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=8376381; DOI=10.1016/s0021-9258(20)80716-9;
RA Bedzyk L.A., Escudero K.W., Gill R.E., Griffin K.J., Frerman F.E.;
RT "Cloning, sequencing, and expression of the genes encoding subunits of
RT Paracoccus denitrificans electron transfer flavoprotein.";
RL J. Biol. Chem. 268:20211-20217(1993).
RN [2]
RP PROTEIN SEQUENCE OF 2-22; 215-250; 252-270 AND 274-287.
RC STRAIN=ATCC 13543 / NRRL B-3784 / NRC 449;
RX PubMed=1576992; DOI=10.1111/j.1432-1033.1992.tb16877.x;
RA Watmough N.J., Kiss J., Frerman F.E.;
RT "Structural and redox relationships between Paracoccus denitrificans,
RT porcine and human electron-transferring flavoproteins.";
RL Eur. J. Biochem. 205:1089-1097(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=10026281; DOI=10.1021/bi9820917;
RA Roberts D.L., Salazar D., Fulmer J.P., Frerman F.E., Kim J.-J.P.;
RT "Crystal structure of Paracoccus denitrificans electron transfer
RT flavoprotein: structural and electrostatic analysis of a conserved flavin
RT binding domain.";
RL Biochemistry 38:1977-1989(1999).
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).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per dimer.;
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; L14864; AAA03072.1; -; Unassigned_DNA.
DR PIR; B48008; B48008.
DR RefSeq; WP_011748831.1; NZ_FOYK01000007.1.
DR PDB; 1EFP; X-ray; 2.60 A; A/C=2-308.
DR PDBsum; 1EFP; -.
DR AlphaFoldDB; P38974; -.
DR SMR; P38974; -.
DR DIP; DIP-6157N; -.
DR IntAct; P38974; 1.
DR OMA; WRPYAEQ; -.
DR EvolutionaryTrace; P38974; -.
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:1576992,
FT ECO:0000269|PubMed:8376381"
FT CHAIN 2..308
FT /note="Electron transfer flavoprotein subunit alpha"
FT /id="PRO_0000167854"
FT BINDING 252..280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT CONFLICT 220
FT /note="G -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 42..49
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:1EFP"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:1EFP"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 210..218
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 227..231
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1EFP"
FT TURN 266..270
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:1EFP"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:1EFP"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:1EFP"
SQ SEQUENCE 308 AA; 31294 MW; 445B57680098BFA1 CRC64;
MAVLLLGEVT NGALNRDATA KAVAAVKALG DVTVLCAGAS AKAAAEEAAK IAGVAKVLVA
EDALYGHRLA EPTAALIVGL AGDYSHIAAP ATTDAKNVMP RVAALLDVMV LSDVSAILDA
DTFERPIYAG NAIQVVKSKD AKKVFTIRTA SFDAAGEGGT APVTETAAAA DPGLSSWVAD
EVAESDRPEL TSARRVVSGG RGLGSKESFA IIEELADKLG AAVGASRAAV DSGYAPNDWQ
VGQTGKVVAP ELYVAVGISG AIQHLAGMKD SKVIVAINKD EEAPIFQIAD YGLVGDLFSV
VPELTGKL
