ID A0A168DU09_9CLOT Unreviewed; 429 AA.
AC A0A168DU09;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acryloyl-CoA reductase electron transfer subunit beta {ECO:0000313|EMBL:KZL91469.1};
GN Name=acrA_3 {ECO:0000313|EMBL:KZL91469.1};
GN ORFNames=CLMAG_32280 {ECO:0000313|EMBL:KZL91469.1};
OS Clostridium magnum DSM 2767.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL91469.1, ECO:0000313|Proteomes:UP000076603};
RN [1] {ECO:0000313|EMBL:KZL91469.1, ECO:0000313|Proteomes:UP000076603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL91469.1,
RC ECO:0000313|Proteomes:UP000076603};
RA Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT "Genome sequence of Clostridium magnum DSM 2767.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZL91469.1}.
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DR EMBL; LWAE01000003; KZL91469.1; -; Genomic_DNA.
DR RefSeq; WP_066624217.1; NZ_LWAE01000003.1.
DR AlphaFoldDB; A0A168DU09; -.
DR STRING; 1121326.CLMAG_32280; -.
DR PATRIC; fig|1121326.3.peg.3259; -.
DR OrthoDB; 9770286at2; -.
DR Proteomes; UP000076603; 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; PF13187; Fer4_9; 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; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
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:UP000076603}.
FT DOMAIN 1..29
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 30..59
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 429 AA; 46516 MW; A1E2A8E14508AD00 CRC64;
MAVIIADSCN GCELCIPSCP FDALEISGEG KLVASKEKCI ECGKCVSVCP ISSLNILGDK
KKAKGNLGKE TNKNHMDLKI EKPTGDVWVF AEQFEGKLAS VTLELIGEAK KVSLKLDVKV
CAVLLGDKVE SIILELFAHG ADTVYVIDDE VFHFYRSETY NRAFCYLIDK YKPEILLMGA
TTTGRDLAGA VATAMKTGLT ADCTQLDIDL DKGVLLASRP AFGGNIMATI VCEKHRPQMA
TVRPRVMQMP EPEVNKTGSI IRESFKIEEK SLRTWVLEII KEQSENAKLE DAKIIVCGGR
GVQNQEGFKL LEELAKVIGG VVAGSRGAVE KGLVDYKRQV GQTGQTVSPK LYFAIGISGE
IQHTVGVQGA ETIVSINTDP ECEMMKLATY GIQGDVFEVL PKLIISFKEA LGDISSAKPE
DLCAITKEV
//
