ID A0A1V1W0Z6_9ACTN Unreviewed; 328 AA.
AC A0A1V1W0Z6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:GAW53874.1};
GN Name=etfA {ECO:0000313|EMBL:GAW53874.1};
GN ORFNames=PD653_1278 {ECO:0000313|EMBL:GAW53874.1};
OS Nocardioides sp. PD653.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=393303 {ECO:0000313|EMBL:GAW53874.1, ECO:0000313|Proteomes:UP000194147};
RN [1] {ECO:0000313|Proteomes:UP000194147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD653 {ECO:0000313|Proteomes:UP000194147};
RA Ito K., Takagi K., Tanaka N., Kanesaki Y., Iwasaki A.;
RT "Nocardioides sp. PD653 draft genome sequence.";
RL Submitted (NOV-2016) 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:GAW53874.1}.
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DR EMBL; BDJG01000011; GAW53874.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1W0Z6; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000194147; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000194147}.
FT DOMAIN 2..189
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 239..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 253..257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 270..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 328 AA; 33257 MW; 1B6EC3CF84D72B4B CRC64;
MILVLVETSP SREAVEVSRE AVTFARSLSD SGGGVPVDAV VVGAASEALV ATLASYGVRQ
VHVLEGDAFA AFSGAAWASG ILAVRASAGS VVVMAAGTPR GNEVMAHVAA RAGVAMAANV
LSFSGLSPFV VTRQVVGGSA LEEMRLSDRP AVFTVAGHAV EASPAAAPGP GEVVTHTPDV
DAADLVARVV SSEEPEPDLS GTLTSARVVV GAGRGAGSSD GFADLLELTE LVGGSLGVSR
VVTSLGWRPH HEQVGQTGSR ISPDLYIPCG ISGAIQHWAG CSTAKNILAI NTDPDAPMVT
KATYAVIGDL HEVVPAINEE IRRRRSAG
//
