ID   ETFA_ANAPI              Reviewed;         367 AA.
AC   G3KIM6;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Acryloyl-CoA reductase electron transfer subunit beta;
DE   AltName: Full=Electron transfer flavoprotein large subunit;
DE            Short=ETFLS;
DE   AltName: Full=Electron transfer flavoprotein subunit beta;
DE            Short=Beta-ETF;
GN   Name=acrA;
OS   Anaerotignum propionicum (Clostridium propionicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerotignum.
OX   NCBI_TaxID=28446;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RA   Poehlein A., Schlien K., Daniel R., Gottschalk G., Buckel W.;
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RX   PubMed=22810300; DOI=10.1007/s00253-012-4274-y;
RA   Kandasamy V., Vaidyanathan H., Djurdjevic I., Jayamani E.,
RA   Ramachandran K.B., Buckel W., Jayaraman G., Ramalingam S.;
RT   "Engineering Escherichia coli with acrylate pathway genes for propionic
RT   acid synthesis and its impact on mixed-acid fermentation.";
RL   Appl. Microbiol. Biotechnol. 97:1191-1200(2013).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND SUBUNIT.
RC   STRAIN=ATCC 25522 / DSM 1682 / JCM 1430 / NCIMB 10656 / VPI 5303 / X2;
RX   PubMed=12603323; DOI=10.1046/j.1432-1033.2003.03450.x;
RA   Hetzel M., Brock M., Selmer T., Pierik A.J., Golding B.T., Buckel W.;
RT   "Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of
RT   propionyl-CoA dehydrogenase and electron-transferring flavoprotein.";
RL   Eur. J. Biochem. 270:902-910(2003).
CC   -!- FUNCTION: Part of the ETF-acryloyl-CoA reductase complex involved in
CC       the pathway of L-alanine fermentation. The electron transfer
CC       flavoprotein (ETF) serves as a specific electron acceptor for acryloyl-
CC       CoA reductase. {ECO:0000269|PubMed:12603323}.
CC   -!- SUBUNIT: Heterohexadecamer; tetramer of tetramers. Each tetramer is
CC       composed of 2 alpha (AcrC), a beta (AcrA) and a gamma (AcrB) subunit.
CC       {ECO:0000269|PubMed:12603323}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12603323}.
CC   -!- MASS SPECTROMETRY: Mass=37650; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12603323};
CC   -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JN244654; AEM62996.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3KIM6; -.
DR   SMR; G3KIM6; -.
DR   BioCyc; MetaCyc:MON-12758; -.
DR   BRENDA; 1.3.1.95; 1504.
DR   SABIO-RK; G3KIM6; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
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; 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.
PE   1: Evidence at protein level;
KW   Cytoplasm; Electron transport; Transport.
FT   CHAIN           1..367
FT                   /note="Acryloyl-CoA reductase electron transfer subunit
FT                   beta"
FT                   /id="PRO_0000424268"
FT   BINDING         305..333
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  39863 MW;  22CF738C18E3093D CRC64;
     MAFNSADINS FRDIWVFCEQ REGKLINTDF ELISEGRKLA DERGSKLVGI LLGHEVEEIA
     KELGGYGADK VIVCDHPELK FYTTDAYAKV LCDVVMEEKP EVILIGATNI GRDLGPRCAA
     RLHTGLTADC THLDIDMNKY VDFLSTSSTL DISSMTFPME DTNLKMTRPA FGGHLMATII
     CPRFRPCMST VRPGVMKKAE FSQEMAQACQ VVTRHVNLSD EDLKTKVINI VKETKKIVDL
     IGAEIIVSVG RGISKDVQGG IALAEKLADA FGNGVVGGSR AVIDSGWLPA DHQVGQTGKT
     VHPKVYVALG ISGAIQHKAG MQDSELIIAV NKDETAPIFD CADYGITGDL FKIVPMMIDA
     IKEGKNA