ID Q897M1_CLOTE Unreviewed; 336 AA.
AC Q897M1;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Electron transfer flavoprotein alpha-subunit fixB {ECO:0000313|EMBL:AAO35315.1};
GN Name=fixB {ECO:0000313|EMBL:AAO35315.1};
GN OrderedLocusNames=CTC_00712 {ECO:0000313|EMBL:AAO35315.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO35315.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO35315.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO35315.1; -; Genomic_DNA.
DR RefSeq; WP_011098981.1; NC_004557.1.
DR AlphaFoldDB; Q897M1; -.
DR STRING; 212717.CTC_00712; -.
DR GeneID; 24253497; -.
DR KEGG; ctc:CTC_00712; -.
DR HOGENOM; CLU_034178_1_1_9; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 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:UP000001412}.
FT DOMAIN 9..198
FT /note="Electron transfer flavoprotein alpha/beta-subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM00893"
FT BINDING 222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 247..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 261..265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 278..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000089-1"
SQ SEQUENCE 336 AA; 36507 MW; 5096E7F0D8EEF4E4 CRC64;
MNIADYKGVW VFAEQRDGEL QKVSLELLGK GREIADKLGV ELTALLLGNK IDSIAEELVA
YGADKVIYAQ NPLLSHYTTD GYTKVICDLV AEEKPEIILV GATYIGRDLG PRVAARLRTG
LTADCTALDV EEGTNNLLMT RPAFGGNLMA TIVCGEHRPQ MSTVRPGVFE KLKKDAGRKG
EIKKIEAKLE MSDIRTKVED VVKITKNVMD IGEAEFLVAG GRGIGSKENF KMLEELAELL
GGNVAGSRAA IDNGWIDKDY QVGQTGKTVR PMVYIAVGIS GAIQHLAGMQ DSDYIIAINK
DEAAPIMQIA DLGLVGDYNK IVPELIAKLK EEKEEN
//