ID   FIXB_CLOSA              Reviewed;         334 AA.
AC   P53578; Q9R5W1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Protein FixB;
GN   Name=fixB;
OS   Clostridium saccharobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=169679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-117 / DSM 13864 / NCP 262;
RA   Lin F.-P., Reid S.J., Woods D.R.;
RT   "Independent transcription of the linked Clostridium acetobutylicum fixB,
RT   a-hbd and adh1 genes in C. acetobutylicum P262 and Escherichia coli.";
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-117 / DSM 13864 / NCP 262;
RX   PubMed=7875566; DOI=10.1111/j.1574-6968.1995.tb07356.x;
RA   Youngleson J.S., Lin F.-P., Reid S.J., Woods D.R.;
RT   "Structure and transcription of genes within the beta-hbd-adh1 region of
RT   Clostridium acetobutylicum P262.";
RL   FEMS Microbiol. Lett. 125:185-191(1995).
CC   -!- FUNCTION: May play a role in a redox process.
CC   -!- SUBUNIT: FixA and FixB form a heterodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from C.acetobutylicum.
CC       {ECO:0000305}.
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DR   EMBL; M91817; AAA23237.1; -; Genomic_DNA.
DR   AlphaFoldDB; P53578; -.
DR   SMR; P53578; -.
DR   STRING; 169679.CSACC_03530; -.
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..334
FT                   /note="Protein FixB"
FT                   /id="PRO_0000167860"
FT   BINDING         271..299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        15
FT                   /note="Q -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  35680 MW;  69919D07A35D6604 CRC64;
     MNIADYKGVW VFAEQREGEL QKVSLELLGE GRRVADKLGV KLTALLLGSN VEGIKDLAEH
     GADEVLVADN KDLQHYTTDA YTKVICDLAN ERKPGILFVG ATFIGRDLGP RVAARLNTGL
     TADCTSIDVE VENGDLLATR PAFGGNLMAT IACPEHRPQM ATVRPGVFEK VNTDGANCKV
     EKVEVKLTNN DLRTKVLEII KSKKDIVDIS EAKIIVAGGR GVGSKENFEL LGELAKVLGG
     TVAGSRAAVE KGWIENAYQV GQTGKTVKPS IYIACGISGA IQHVAGMQDS DMIIAINKDE
     TAPIMKVADY GIVGDVKNVL PELIAQAKEI ISAE