ID F2RC00_STRVP Unreviewed; 318 AA.
AC F2RC00;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Electron transfer flavoprotein, alpha subunit {ECO:0000313|EMBL:CCA59251.1};
GN OrderedLocusNames=SVEN_5965 {ECO:0000313|EMBL:CCA59251.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59251.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA59251.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA59251.1};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
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; FR845719; CCA59251.1; -; Genomic_DNA.
DR RefSeq; WP_015037146.1; NZ_JABVZO010000178.1.
DR AlphaFoldDB; F2RC00; -.
DR STRING; 953739.SVEN_5965; -.
DR GeneID; 69868007; -.
DR KEGG; sve:SVEN_5965; -.
DR PATRIC; fig|953739.5.peg.1175; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_0_1_11; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000006854; Chromosome.
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:UP000006854};
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 233..234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 247..251
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 264..271
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 318 AA; 32056 MW; 0193F0E78BB89E72 CRC64;
MAEILVLVDH ADGAVRKPAL ELLTLARRIG EPTAVVLGAG EAAASIAATA GEYGAATVYV
ADGAEFTEQL VVPKVDALTQ LAKEKGAAAV LVTSSGEGKE IAARVALRLG SGLITDAVEL
EAGENAPVAT QSVFAASYQV KSTVTHGVPV ITVKPNSAAP EAAPAAGTVE NVTVAFTGNA
AKVVSRTARV STGRPELTES AIVVSGGRGV GAAEGFAVVE KLADSLGAAV GASRAAVDAG
WYPHSNQVGQ TGKQVSPQLY VAAGISGAIQ HRAGMQTSKT IVAVNKDPEA PIFDLVDYGV
VGDLFEVLPQ LTDEIGAR
//
