ID A0A2W2CB32_9ACTN Unreviewed; 319 AA.
AC A0A2W2CB32;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000313|EMBL:PZF89098.1};
GN ORFNames=C1I93_24315 {ECO:0000313|EMBL:PZF89098.1};
OS Micromonospora endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=515350 {ECO:0000313|EMBL:PZF89098.1, ECO:0000313|Proteomes:UP000248627};
RN [1] {ECO:0000313|EMBL:PZF89098.1, ECO:0000313|Proteomes:UP000248627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45430 {ECO:0000313|EMBL:PZF89098.1,
RC ECO:0000313|Proteomes:UP000248627};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella endophytica.";
RL Submitted (JAN-2018) 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:PZF89098.1}.
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DR EMBL; POTX01000221; PZF89098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2CB32; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000248627; 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 GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; 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; IPR012131; Hstdl_DH.
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 PRINTS; PR00083; HOLDHDRGNASE.
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 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 319 AA; 32792 MW; EF707FD15C3EC790 CRC64;
MSEVLVVVEA TREFGVKKVT LEMLTLAREL GTPSAVVLGG AGAADALAGK LGEYGAEKIY
AAEGAEIDGY LVAPKATVVA ELVQRVQPAA VLLASSQEGK EIAARLAVKL DNGILTDVVG
LAADGTATQV VFAGSAIVKS KVTRGLPLVT VRPNSVNPTP AAASPAVEQL TVTTTDADKL
AKVVERVAEQ KGSRPELTEA GVVVSGGRGV GNADNFKLVE ELADLLGGAV GASRAAVDSG
FYPHQFQVGQ TGKTVSPQLY VALGISGAIQ HRAGMQTSKT IVAVNKDGEA PIFELADFGV
VGDLFKIVPQ AAEEIRKRK
//
