ID H6SHR0_CLOTT Unreviewed; 334 AA.
AC H6SHR0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 28-JUN-2023, entry version 22.
DE SubName: Full=Electron transfer flavoprotein alpha-subunit {ECO:0000313|EMBL:CCF78541.1};
DE SubName: Full=Electron transfer flavoprotein subunit alpha/FixB family protein {ECO:0000313|EMBL:MBC2400195.1};
GN Name=etfA {ECO:0000313|EMBL:CCF78541.1};
GN ORFNames=HGG79_20960 {ECO:0000313|EMBL:MBC2400195.1};
OS Clostridium tetanomorphum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1553 {ECO:0000313|EMBL:CCF78541.1};
RN [1] {ECO:0000313|EMBL:CCF78541.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GT6 {ECO:0000313|EMBL:CCF78541.1};
RX PubMed=24331236; DOI=10.1016/j.syapm.2013.10.004;
RA Panitz J.C., Zverlov V.V., Pham V.T., Sturzl S., Schieder D., Schwarz W.H.;
RT "Isolation of a solventogenic Clostridium sp. strain: fermentation of
RT glycerol to n-butanol, analysis of the bcs operon region and its potential
RT regulatory elements.";
RL Syst. Appl. Microbiol. 37:1-9(2014).
RN [2] {ECO:0000313|EMBL:MBC2400195.1, ECO:0000313|Proteomes:UP000563151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ011 {ECO:0000313|EMBL:MBC2400195.1,
RC ECO:0000313|Proteomes:UP000563151};
RA Brown S.;
RT "Genomic insights into acetone-butanol-ethanol (ABE) fermentation by
RT sequencing solventogenic clostridia strains.";
RL Submitted (APR-2020) 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; HE660044; CCF78541.1; -; Genomic_DNA.
DR EMBL; JAAZWO010000060; MBC2400195.1; -; Genomic_DNA.
DR AlphaFoldDB; H6SHR0; -.
DR Proteomes; UP000563151; 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 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:UP000563151}.
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 334 AA; 36229 MW; 9AF00AAE529D4B30 CRC64;
MNIADYRGVW VFAEQRDGQL QKVALELLGK GREIADKIGV ELTAVLLGDE IDGVANELVA
YGADRVLYAH NPLLKHFTTD AYTKVICDLV NERKPEIILV GASYIGRDLG PRVAARLDTG
LTADCTSLDI EEGTNHLLMT RPAFGGNLMA TIMCTDHRPQ MSTVRPGVFE KLKKDENRKG
EVEKIAAKVE MSHIRTKVED VVKIAKNVMD IGEAEVLVSG GRGVGAKENF ELLKELADLF
GGSLAGSRAA IDNAWLDKAY QVGQTGKTVR PKVYIAVGIS GAIQHLAGMQ DSDYIIAINK
DESAPIMQVA DLGIVGDFKK VIPELIAEIK ATMN
//
