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Database: UniProt
Entry: D2SEM0_GEOOG
LinkDB: D2SEM0_GEOOG
Original site: D2SEM0_GEOOG 
ID   D2SEM0_GEOOG            Unreviewed;       320 AA.
AC   D2SEM0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=Electron transfer flavoprotein alpha subunit {ECO:0000313|EMBL:ADB76656.1};
GN   OrderedLocusNames=Gobs_4091 {ECO:0000313|EMBL:ADB76656.1};
OS   Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS   A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB76656.1, ECO:0000313|Proteomes:UP000001382};
RN   [1] {ECO:0000313|EMBL:ADB76656.1, ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX   PubMed=21304698;
RA   Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA   Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA   Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA   Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT   "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT   20).";
RL   Stand. Genomic Sci. 2:158-167(2010).
RN   [2] {ECO:0000313|Proteomes:UP000001382}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC   NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA   Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL   Submitted (JAN-2010) 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}.
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DR   EMBL; CP001867; ADB76656.1; -; Genomic_DNA.
DR   RefSeq; WP_012950081.1; NC_013757.1.
DR   AlphaFoldDB; D2SEM0; -.
DR   STRING; 526225.Gobs_4091; -.
DR   KEGG; gob:Gobs_4091; -.
DR   eggNOG; COG2025; Bacteria.
DR   HOGENOM; CLU_034178_0_1_11; -.
DR   OrthoDB; 9770286at2; -.
DR   Proteomes; UP000001382; 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; 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:UP000001382};
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         209
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         234..235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         248..252
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         265..272
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT   BINDING         286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ   SEQUENCE   320 AA;  32636 MW;  9F4126D12959417D CRC64;
     MAEVLVLVEL NPTGEGVRKT TLEALTAARA LGEPAAVVVG GPGTAAAAKA QLAEYGAQKV
     YVAESEEVDQ FLVAPKAEVL AQLVAEKSPA AVVIPSSPEG KEIAGRLAIK TGSGFLTDVT
     EIAPDGTATQ VAFAGATIVH SKVTVGTPIY TVRGNSVTPE PAPGAAEEEQ VALQLSDAAK
     ATRVVDRVVE QKSSRPELTE ASIVVSGGRG VASAENFSVI EALADSLGAA VGASRAAVDS
     GYYPHTFQVG QTGKTVSPQL YIAVGISGAI QHRAGMQTSK TIVAVNKDPE APIFELADFG
     VVGDLNTVVP QATEAINSRK
//
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