ID ETFB_SYNWW Reviewed; 252 AA. AC Q0AZ34; DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 1. DT 11-DEC-2019, entry version 70. DE RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000303|PubMed:23468890}; GN Name=etfB {ECO:0000303|PubMed:23468890}; GN OrderedLocusNames=Swol_0696 {ECO:0000312|EMBL:ABI68020.1}; OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae; OC Syntrophomonas. OX NCBI_TaxID=335541; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2245B / Goettingen; RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x; RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L., RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.; RT "The genome of Syntrophomonas wolfei: new insights into syntrophic RT metabolism and biohydrogen production."; RL Environ. Microbiol. 12:2289-2301(2010). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION, AND PATHWAY. RX PubMed=19648244; DOI=10.1128/jb.01605-08; RA Mueller N., Schleheck D., Schink B.; RT "Involvement of NADH:acceptor oxidoreductase and butyryl coenzyme A RT dehydrogenase in reversed electron transport during syntrophic butyrate RT oxidation by Syntrophomonas wolfei."; RL J. Bacteriol. 191:6167-6177(2009). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, SUBCELLULAR LOCATION, RP FUNCTION, AND PATHWAY. RX PubMed=23468890; DOI=10.1371/journal.pone.0056905; RA Schmidt A., Mueller N., Schink B., Schleheck D.; RT "A proteomic view at the biochemistry of syntrophic butyrate oxidation in RT Syntrophomonas wolfei."; RL PLoS ONE 8:E56905-E56905(2013). CC -!- FUNCTION: Part of an electron transfer flavoprotein involved in CC syntrophic growth of S.wolfei with butyrate. Probably receives CC electrons from butyryl-CoA dehydrogenases, and transfers them to the CC membrane-bound quinone oxidoreductase Swol_0698. CC {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}. CC -!- COFACTOR: CC Name=AMP; Xref=ChEBI:CHEBI:456215; CC Evidence={ECO:0000250|UniProtKB:P13804}; CC Note=Binds 1 AMP per subunit. {ECO:0000250|UniProtKB:P13804}; CC -!- PATHWAY: Lipid metabolism; butanoate metabolism. CC {ECO:0000305|PubMed:19648244, ECO:0000305|PubMed:23468890}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. CC {ECO:0000250|UniProtKB:P13804}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23468890}. CC -!- INDUCTION: Highly expressed during syntrophic growth with butyrate (at CC protein level) (PubMed:19648244, PubMed:23468890). Seems to be CC constitutively expressed (PubMed:23468890). CC {ECO:0000269|PubMed:19648244, ECO:0000269|PubMed:23468890}. CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {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; CP000448; ABI68020.1; -; Genomic_DNA. DR SMR; Q0AZ34; -. DR STRING; 335541.Swol_0696; -. DR EnsemblBacteria; ABI68020; ABI68020; Swol_0696. DR KEGG; swo:Swol_0696; -. DR eggNOG; ENOG4105BZJ; Bacteria. DR eggNOG; COG2086; LUCA. DR HOGENOM; HOG000247879; -. DR KO; K03521; -. DR OMA; YNGGMVP; -. DR BioCyc; SWOL335541:G1G78-709-MONOMER; -. DR UniPathway; UPA00863; -. DR Proteomes; UP000001968; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0019605; P:butyrate metabolic process; IEA:UniProtKB-UniPathway. DR CDD; cd01714; ETF_beta; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014730; ETF_a/b_N. DR InterPro; IPR012255; ETF_b. DR InterPro; IPR033948; ETF_beta_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR21294; PTHR21294; 1. DR Pfam; PF01012; ETF; 1. DR PIRSF; PIRSF000090; Beta-ETF; 1. DR SMART; SM00893; ETF; 1. PE 1: Evidence at protein level; KW Cytoplasm; Electron transport; Fatty acid metabolism; Lipid metabolism; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1..252 FT /note="Electron transfer flavoprotein subunit beta" FT /id="PRO_0000442218" SQ SEQUENCE 252 AA; 26280 MW; 93D8CE68B7862732 CRC64; MNLKVLVCVK QTFDTEAKIE LKDGKIADAG INLIINPYDE VAVEGAIQLK EKGVAKEIVV VAAGSDKAMD AIRTALAMGA DRGILVQQDT AADEFARAVA LAEAIKGENP DIILAGHVAA DDGSSQVPTR VAEILGLPHV NVITAVEIAG GKATCTSEAD GGTQVTEVSL PAVISSQVSW NEPRYPSMKG IMAAKKKPVA TAAAAAAESK VKILEFSLPP AKAAGIKIED EPEVCATKLA EWMKNTVKVE VK //