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Database: UniProt
Entry: A0A0M2HDJ1_9MICO
LinkDB: A0A0M2HDJ1_9MICO
Original site: A0A0M2HDJ1_9MICO 
ID   A0A0M2HDJ1_9MICO        Unreviewed;       313 AA.
AC   A0A0M2HDJ1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:KJL42301.1};
GN   Name=etfA_1 {ECO:0000313|EMBL:KJL42301.1};
GN   ORFNames=RS82_02317 {ECO:0000313|EMBL:KJL42301.1};
OS   Microbacterium trichothecenolyticum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL42301.1, ECO:0000313|Proteomes:UP000034098};
RN   [1] {ECO:0000313|EMBL:KJL42301.1, ECO:0000313|Proteomes:UP000034098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL42301.1,
RC   ECO:0000313|Proteomes:UP000034098};
RA   Corretto E.;
RT   "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT   metal contaminated environments.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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:KJL42301.1}.
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DR   EMBL; JYJA01000035; KJL42301.1; -; Genomic_DNA.
DR   RefSeq; WP_045299477.1; NZ_JYJA01000035.1.
DR   AlphaFoldDB; A0A0M2HDJ1; -.
DR   PATRIC; fig|69370.6.peg.2355; -.
DR   OrthoDB; 9770286at2; -.
DR   Proteomes; UP000034098; 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:UP000034098};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          6..179
FT                   /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM00893"
FT   BINDING         201
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         226..227
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         240..244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         257..264
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         278
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         296..297
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   313 AA;  31174 MW;  968B12A3CA94DC48 CRC64;
     MTAQQILVLL DATPSGELAT SAAGLLGAAA GVGTPVALVV GADSAAQRAG ELGAATVLTA
     AGDAVDALVA AVDKIQPDAV IVSHSVEGRE FAARFATRTR SALAVDVVAI SRDDEGIVAH
     HSVYGGSYLV QAAATFGAPV ITVRQGAVDV RAEAVATPVV EALAVEPSRR AAATFGEVEA
     AVASSTRPEL RGASKVVSGG RGLGSGEKFA LVEELADALG AAVGASRAAV DAGYVPQSYQ
     VGQTGVSVSP QLYVALGISG AIQHKAGMQT AKTIVAINKD ADAPIFEIAD FGVVGDIFTV
     VPQLIAALEA KKA
//
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