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Database: UniProt
Entry: A0A0M3DMI7_9CLOT
LinkDB: A0A0M3DMI7_9CLOT
Original site: A0A0M3DMI7_9CLOT 
ID   A0A0M3DMI7_9CLOT        Unreviewed;       329 AA.
AC   A0A0M3DMI7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:KKY02617.1};
GN   ORFNames=VN21_02205 {ECO:0000313|EMBL:KKY02617.1};
OS   Paraclostridium benzoelyticum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Paraclostridium.
OX   NCBI_TaxID=1629550 {ECO:0000313|EMBL:KKY02617.1, ECO:0000313|Proteomes:UP000034407};
RN   [1] {ECO:0000313|EMBL:KKY02617.1, ECO:0000313|Proteomes:UP000034407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC272 {ECO:0000313|EMBL:KKY02617.1,
RC   ECO:0000313|Proteomes:UP000034407};
RA   Jyothsna T., Sasikala C., Ramana C.;
RT   "Microcin producing Clostridium sp. JC272T.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKY02617.1}.
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DR   EMBL; LBBT01000041; KKY02617.1; -; Genomic_DNA.
DR   RefSeq; WP_046821841.1; NZ_LBBT01000041.1.
DR   AlphaFoldDB; A0A0M3DMI7; -.
DR   PATRIC; fig|1629550.3.peg.3139; -.
DR   OrthoDB; 9770286at2; -.
DR   Proteomes; UP000034407; Unassembled WGS sequence.
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; 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:UP000034407}.
FT   DOMAIN          8..197
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         221
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         246..247
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         260..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         277..284
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         298
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   329 AA;  35825 MW;  DB3EA14E4B879E09 CRC64;
     MGGKTMSVMV FVEQRSGEIQ NVSLELLGKG RELADKINNK LSAVLLGHNI EKLSEELIQY
     GADEVVYVED KNLDVYLTGT YTKALTEVIN KKNPEIVLVG ATTIGRDLAP RVSATIGTGL
     TADCTSLEID EENQGLLMTR PAFGGNIMAT IICPNHRPQM STVRPGVMKK LEKNMARKGN
     VEKIEVKFLE DYENVQVLKY VKENIKKVNI EDAKVLISAG RGIGCKENMD ALYELADLLG
     AEVSASRAVV DAGWIDKSRQ VGQTGKTVRP DVYIACGISG AIQHLAGMEE SEYIIAINNN
     SDAAIFEVAD LSLVGDVNRV IKNLIQELA
//
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