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Database: UniProt
Entry: D4MUW2_ANAHA
LinkDB: D4MUW2_ANAHA
Original site: D4MUW2_ANAHA 
ID   D4MUW2_ANAHA            Unreviewed;       325 AA.
AC   D4MUW2;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Electron transfer flavoprotein large subunit {ECO:0000313|EMBL:CUN77000.1};
DE   SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:AQP38938.1};
DE   SubName: Full=Electron transfer flavoprotein, alpha subunit {ECO:0000313|EMBL:CBL39178.1};
GN   Name=etfA_2 {ECO:0000313|EMBL:CUP08687.1};
GN   Synonyms=etfA_3 {ECO:0000313|EMBL:CUN77000.1};
GN   ORFNames=CL2_23190 {ECO:0000313|EMBL:CBL39178.1}, DO83_04570
GN   {ECO:0000313|EMBL:AQP38938.1}, ERS852475_00761
GN   {ECO:0000313|EMBL:CUN77000.1}, ERS852520_00576
GN   {ECO:0000313|EMBL:CUP08687.1};
OS   Anaerostipes hadrus.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL39178.1, ECO:0000313|Proteomes:UP000008960};
RN   [1] {ECO:0000313|EMBL:CBL39178.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL39178.1,
RC   ECO:0000313|Proteomes:UP000008960};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SSC/2.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL39178.1, ECO:0000313|Proteomes:UP000008960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SSC/2 {ECO:0000313|EMBL:CBL39178.1,
RC   ECO:0000313|Proteomes:UP000008960};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000095564, ECO:0000313|Proteomes:UP000095611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5834860 {ECO:0000313|EMBL:CUN77000.1,
RC   ECO:0000313|Proteomes:UP000095611}, and 2789STDY5834908
RC   {ECO:0000313|EMBL:CUP08687.1, ECO:0000313|Proteomes:UP000095564};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AQP38938.1, ECO:0000313|Proteomes:UP000188159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPB5 {ECO:0000313|EMBL:AQP38938.1,
RC   ECO:0000313|Proteomes:UP000188159};
RX   PubMed=27264309; DOI=10.1038/srep27572;
RA   Zhang Q., Wu Y., Wang J., Wu G., Long W., Xue Z., Wang L., Zhang X.,
RA   Pang X., Zhao Y., Zhao L., Zhang C.;
RT   "Accelerated dysbiosis of gut microbiota during aggravation of DSS-induced
RT   colitis by a butyrate-producing bacterium.";
RL   Sci. Rep. 6:27572-27572(2016).
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}.
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DR   EMBL; CP012098; AQP38938.1; -; Genomic_DNA.
DR   EMBL; FP929061; CBL39178.1; -; Genomic_DNA.
DR   EMBL; CYZM01000002; CUN77000.1; -; Genomic_DNA.
DR   EMBL; CZAU01000003; CUP08687.1; -; Genomic_DNA.
DR   RefSeq; WP_008394110.1; NZ_WQRB01000005.1.
DR   AlphaFoldDB; D4MUW2; -.
DR   STRING; 649756.ERS852387_00118; -.
DR   GeneID; 15232269; -.
DR   KEGG; bprl:CL2_23190; -.
DR   PATRIC; fig|245018.3.peg.2607; -.
DR   OrthoDB; 9770286at2; -.
DR   Proteomes; UP000008960; Chromosome.
DR   Proteomes; UP000095564; Unassembled WGS sequence.
DR   Proteomes; UP000095611; Unassembled WGS sequence.
DR   Proteomes; UP000188159; Chromosome.
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}.
FT   DOMAIN          7..194
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         211
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         236..237
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         250..254
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         267..274
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         288
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   325 AA;  34147 MW;  88352ECE941558E6 CRC64;
     MAECKNIMVY VETAEGNPVK VGLEMLSPAK KLADKVTAVV IGGGVADAAK EVAKAGADQV
     ICVDSEDYKE FNLDAYAQVL VELVKEENPE AVFVGGTQDG KDIAPVVAAK CNTGCASDVL
     DIKAEDGEVI YTCPLYGGTV LEDVKIKTTP QIATLRSGAF QKVEDPTEGE VVAKEVKVAD
     DVIKAKITES VKEIAETINL EEAEVIVSGG RGMGSKENFA LVDDLAKLLG GVVGATRPAI
     EDGWVSKIHQ VGQSGKIVAP KLYIACGISG ATQHVSGIMN SGYIVAINKD EDAPIFDVAN
     VGIVGDVMKV LPVMIEEIKK IKDAQ
//
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