ID A0A1D3TVP0_9FIRM Unreviewed; 648 AA.
AC A0A1D3TVP0;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=2,4-dienoyl-CoA reductase {ECO:0000313|EMBL:SCP98219.1};
GN ORFNames=SAMN05421730_10189 {ECO:0000313|EMBL:SCP98219.1};
OS Anaerobium acetethylicum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerobium.
OX NCBI_TaxID=1619234 {ECO:0000313|EMBL:SCP98219.1, ECO:0000313|Proteomes:UP000199315};
RN [1] {ECO:0000313|EMBL:SCP98219.1, ECO:0000313|Proteomes:UP000199315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GluBS11 {ECO:0000313|EMBL:SCP98219.1,
RC ECO:0000313|Proteomes:UP000199315};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000256|ARBA:ARBA00011048}.
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DR EMBL; FMKA01000018; SCP98219.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D3TVP0; -.
DR STRING; 1619234.SAMN05421730_10189; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000199315; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023014};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000199315}.
FT DOMAIN 7..331
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 387..613
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 648 AA; 71148 MW; 30C551DD5ED63075 CRC64;
MNFESTFKPM YIGKMLVKNR LVVPAMDSAM CEMDGKIEKM ACDYYGARAK GGFGIVITEI
AAVDDKATGM PGEPRLYSDE YLPGLTRLAN AIHTGGAKAI VQLHHAGRET ASAMIGQTAV
GPSSIPSVVY REPVNEYTTE QVYELIDSYI DSSVRCKKAG FDGIEFHSAH GYMGLQFMSP
RTNKRIDEFG GGVEGRSYFH KLIIEGIRKA CGEEFAIIVR MDSIEARVGG IEENEAVVFA
RLLESYGADA LNISAGTYAA WDTIVPTPDM PQGWNWHGTR RIREAVKVPV MAAGRYSDPF
VIEQSIERGD TDFVCLGRQS IADPEFPNKM AGGDLADIVP CIGCTQRCMS FNDHDSLQEG
DWGVSCMLNP MSNNRKDVQY DMAEESKKVM IIGAGVAGME AAWIAAERGH DVTIYEKNDE
SKVGGQFLIA AYPPFKQDLT RPIRYYKHMC KKNGVKMVFN TNVDTEFIKS VKPDVLVVAT
GATPFKLNIP GSDAPNVYQA NDVLVGKSIL GNSALVIGGG MVGVETAEFC QDYCARVAVV
EMRDDIAMDL YMTVRDSLLR RFKQEGIEIY RKTCVSRIEG NTVYAEQDGK EIVLDGFDNI
IFAVGSKPEV QFEDVESLAD QVFVIGDAKK ARSAVEAIYE GARVGMSI
//
