ID A0A095XYU2_9CORY Unreviewed; 316 AA.
AC A0A095XYU2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:KGF15330.1};
GN ORFNames=HMPREF1650_11575 {ECO:0000313|EMBL:KGF15330.1};
OS Corynebacterium freneyi DNF00450.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1287475 {ECO:0000313|EMBL:KGF15330.1, ECO:0000313|Proteomes:UP000029548};
RN [1] {ECO:0000313|EMBL:KGF15330.1, ECO:0000313|Proteomes:UP000029548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00450 {ECO:0000313|EMBL:KGF15330.1,
RC ECO:0000313|Proteomes:UP000029548};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF15330.1}.
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DR EMBL; JRNE01000079; KGF15330.1; -; Genomic_DNA.
DR RefSeq; WP_035123421.1; NZ_JRNE01000079.1.
DR AlphaFoldDB; A0A095XYU2; -.
DR eggNOG; COG2025; Bacteria.
DR Proteomes; UP000029548; 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:UP000029548};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..192
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 205
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 316 AA; 31976 MW; F3BAF483F85A42D3 CRC64;
MTDVLVLVDH NDGELKNTTA ELLTAARAFG TPAAVVVGKP GTAENFAETL GKYGAGEILA
AESDEAGKHL ITPEVGVLVG LASERQVPVL VASSAAGKEI AGRVAALTGS GVLSDVVEIK
DDRSAVYSIF GGEFIVEGAG YGASPAYALR PGSVDPVEAA ASPSVTAVEY PAADDTAVEI
VSFTPAEGGD RPELTEAKIV VSGGRGVASA EGFADVVEPL ADALGAAVGA SRAAVDADYY
PGQFQVGQTG KTVSPDLYIA LGISGAIQHK AGMQTSKTVV AVNKDEEAPI FEIADFGVIG
DLFNVAPQAT EEIKMA
//
