ID A9WPQ4_RENSM Unreviewed; 317 AA.
AC A9WPQ4;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Electron transfer flavoprotein alpha-subunit {ECO:0000313|EMBL:ABY23012.1};
GN OrderedLocusNames=RSal33209_1275 {ECO:0000313|EMBL:ABY23012.1};
OS Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS NBRC 15589 / NCIMB 2235).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Renibacterium.
OX NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY23012.1, ECO:0000313|Proteomes:UP000002007};
RN [1] {ECO:0000313|Proteomes:UP000002007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC {ECO:0000313|Proteomes:UP000002007};
RX PubMed=18723615; DOI=10.1128/JB.00721-08;
RA Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT reductive evolution away from an environmental Arthrobacter ancestor.";
RL J. Bacteriol. 190:6970-6982(2008).
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; CP000910; ABY23012.1; -; Genomic_DNA.
DR RefSeq; WP_012244697.1; NC_010168.1.
DR AlphaFoldDB; A9WPQ4; -.
DR STRING; 288705.RSal33209_1275; -.
DR KEGG; rsa:RSal33209_1275; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_0_1_11; -.
DR Proteomes; UP000002007; 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; 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:UP000002007}.
FT DOMAIN 4..182
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 207
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 230..231
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 244..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 282
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 317 AA; 32677 MW; 6481F4C3EC646290 CRC64;
MSDIVVFIDQ PGDSLGKAHR ELLTFAHRAG TPVAVVVGVV PAGVLAELGS YGVVQVFSSE
QAELTNYSVV PKAEFLATIA VKVGTRAVLT GNSSEQKDIA ARVAVSLAAG VISDAVGLDE
QLVAEKSVLA GSYSVRAKTT SPVSVIALKS NSTEPEVSPN PQQAVLESVT VDFSTAAWGS
KVLERTDRPA NGRPELSDAR IVVAGGRGVD GDFGPVEALA DALGAAVGAS RAATDAGWID
HAAQVGQTGK TVSPQLYISV GISGAIQQKA GMQTAKLIVA VNKDADSPVF EIADLGIVGD
LFKVLPQAVE EINRRRQ
//
