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Database: UniProt
Entry: W6JYK9_9MICO
LinkDB: W6JYK9_9MICO
Original site: W6JYK9_9MICO 
ID   W6JYK9_9MICO            Unreviewed;       318 AA.
AC   W6JYK9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:CCH73745.1};
GN   Name=etfA {ECO:0000313|EMBL:CCH73745.1};
GN   ORFNames=BN11_3200004 {ECO:0000313|EMBL:CCH73745.1};
OS   Tetrasphaera australiensis Ben110.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Tetrasphaera.
OX   NCBI_TaxID=1193182 {ECO:0000313|EMBL:CCH73745.1, ECO:0000313|Proteomes:UP000035763};
RN   [1] {ECO:0000313|EMBL:CCH73745.1, ECO:0000313|Proteomes:UP000035763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ben110 {ECO:0000313|EMBL:CCH73745.1,
RC   ECO:0000313|Proteomes:UP000035763};
RX   PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA   Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA   Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA   Nielsen K.L., Nielsen P.H.;
RT   "A metabolic model for members of the genus Tetrasphaera involved in
RT   enhanced biological phosphorus removal.";
RL   ISME J. 7:543-554(2013).
CC   -!- FUNCTION: The electron transfer flavoprotein serves as a specific
CC       electron acceptor for other dehydrogenases. It transfers the electrons
CC       to the main respiratory chain via ETF-ubiquinone oxidoreductase (ETF
CC       dehydrogenase). {ECO:0000256|ARBA:ARBA00025649}.
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   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000256|ARBA:ARBA00011355}.
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:CCH73745.1}.
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DR   EMBL; CAJA01000247; CCH73745.1; -; Genomic_DNA.
DR   RefSeq; WP_048699379.1; NZ_HG764815.1.
DR   AlphaFoldDB; W6JYK9; -.
DR   STRING; 1193182.BN11_3200004; -.
DR   OrthoDB; 9770286at2; -.
DR   Proteomes; UP000035763; 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   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; IPR014731; ETF_asu_C.
DR   InterPro; IPR018206; ETF_asu_C_CS.
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.
DR   PROSITE; PS00696; ETF_ALPHA; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000089-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035763};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          4..187
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         208
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         231..232
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         245..249
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         262..269
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         283
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   318 AA;  32296 MW;  2D802743DAFE6E54 CRC64;
     MAEIFVLVDH ANGQVRKTTA EMLTIAARLG EPSAVYLGPG AAEAAATLGK FGAGRVYAMD
     SADLTGYLVV PQAEFLAALV GKLKPGAVLI PSNPAGKEIA ARVAVKTGSG LVTDAIDVQP
     GDGGIETTKS VFAGSYTVKA KVTKGTPIIC VKPNSAAPQE KPAAGQVVPV NLTISDAAKT
     AQITEAKEKQ ASGRPELTEA AIVVSGGRGT GGDFSPVETF ADSLGAAVGA SRAAVDAGWY
     PHTSQVGQTG KQVSPQLYVA CGISGAIQHR AGMQTSKTIV AINKDPEAPI FELVDFGVVG
     DLFTVLPQAT EKVQASKG
//
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