ID A0A1H3MY37_9CLOT Unreviewed; 396 AA.
AC A0A1H3MY37;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Electron transfer flavoprotein alpha subunit apoprotein {ECO:0000313|EMBL:SDY81135.1};
GN ORFNames=SAMN05192546_104316 {ECO:0000313|EMBL:SDY81135.1};
OS Tindallia californiensis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Tindallia.
OX NCBI_TaxID=159292 {ECO:0000313|EMBL:SDY81135.1, ECO:0000313|Proteomes:UP000199230};
RN [1] {ECO:0000313|EMBL:SDY81135.1, ECO:0000313|Proteomes:UP000199230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APO {ECO:0000313|EMBL:SDY81135.1,
RC ECO:0000313|Proteomes:UP000199230};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the ETF alpha-subunit/FixB family.
CC {ECO:0000256|ARBA:ARBA00005817}.
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DR EMBL; FNPV01000004; SDY81135.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3MY37; -.
DR STRING; 159292.SAMN05192546_104316; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000199230; 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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; 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 Pfam; PF13237; Fer4_10; 1.
DR PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000089-1};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000089-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199230}.
FT DOMAIN 2..30
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 31..60
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 309..310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 323..327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 340..347
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 396 AA; 43332 MW; A43729AAB7AAEC42 CRC64;
MAGLKIDYST CDACGNCINT CPVKALYKRG NKVALEENNC ILCGGCIDSC PYEAISINKK
RTKTINREKT SGIWVYAEHK KGVMHPVVYE LLGKGRELAD KSKHKLTAVL IDGESSHLAK
ELIAYGADRV ILCSHVLLES QQDEYHFDAM TTILEEEIPS IFLFGATSFG RSLAPRMAAR
LQTGLTADCT RLEVDDVSGN LYQTRPAFGG NLMATILCPD QRPQMATVRS GIMHAKEPDY
YREGMIKRVN YKGKIKPNIE IINEIIGEKK ESIGDASVII SAGRGIGSQK NMKLVRKLAD
VLGGQVGVSR PLVDIGWSEY PHQIGQTGAV VRPQLMITCG ISGAIQHLAG IADAKTIIAI
NTDPEAPIFS VANYKIIDDC IEVLKMLIDS MEKKQS
//