CARD_ACEWD
ID CARD_ACEWD Reviewed; 262 AA.
AC H6LGM7;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Caffeyl-CoA reductase-Etf complex subunit CarD {ECO:0000305};
DE EC=1.3.1.108 {ECO:0000269|PubMed:23479729};
DE AltName: Full=Electron transfer flavoprotein small subunit {ECO:0000305};
DE Short=ETFSS {ECO:0000305};
DE AltName: Full=Electron transfer flavoprotein subunit beta {ECO:0000303|PubMed:23479729};
DE Short=Beta-ETF {ECO:0000303|PubMed:23479729};
GN Name=carD {ECO:0000303|PubMed:23479729}; OrderedLocusNames=Awo_c15730;
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1;
RX PubMed=23479729; DOI=10.1074/jbc.m112.444919;
RA Bertsch J., Parthasarathy A., Buckel W., Mueller V.;
RT "An electron-bifurcating caffeyl-CoA reductase.";
RL J. Biol. Chem. 288:11304-11311(2013).
CC -!- FUNCTION: Caffeyl-CoA reductase-Etf complex catalyzes the reduction of
CC caffeyl-CoA to yield hydrocaffeyl-CoA. It couples the endergonic
CC ferredoxin reduction with NADH as reductant to the exergonic reduction
CC of caffeoyl-CoA with the same reductant. It uses the mechanism of
CC electron bifurcation to overcome the steep energy barrier in ferredoxin
CC reduction. The electron transfer flavoprotein (Etf) mediates the
CC electron transfer between the different donors and acceptors. The
CC complex can also reduce 4-coumaroyl-CoA and feruloyl-CoA.
CC {ECO:0000269|PubMed:23479729}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrocaffeoyl-CoA + 2 NAD(+) + 2 reduced [2Fe-2S]-[ferredoxin]
CC = (E)-caffeoyl-CoA + 2 NADH + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:46956, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:87136, ChEBI:CHEBI:87137;
CC EC=1.3.1.108; Evidence={ECO:0000269|PubMed:23479729};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:23479729};
CC Note=Binds 1 FAD per subunit. {ECO:0000305|PubMed:23479729};
CC -!- COFACTOR:
CC Name=AMP; Xref=ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:23479729};
CC Note=Binds 1 AMP per subunit. {ECO:0000305|PubMed:23479729};
CC -!- SUBUNIT: Part of the homotrimeric caffeyl-CoA reductase-Etf complex
CC composed of (R)-2-hydroxyisocaproyl-CoA dehydratase CarC, and the
CC electron transfer flavoprotein (ETF) alpha (CarE) and beta (CarD)
CC subunits. {ECO:0000269|PubMed:23479729}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23479729}.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
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DR EMBL; CP002987; AFA48355.1; -; Genomic_DNA.
DR RefSeq; WP_014355958.1; NC_016894.1.
DR PDB; 6FAH; X-ray; 3.13 A; B/F=1-262.
DR PDBsum; 6FAH; -.
DR AlphaFoldDB; H6LGM7; -.
DR SMR; H6LGM7; -.
DR STRING; 931626.Awo_c15730; -.
DR EnsemblBacteria; AFA48355; AFA48355; Awo_c15730.
DR KEGG; awo:Awo_c15730; -.
DR eggNOG; COG2086; Bacteria.
DR HOGENOM; CLU_060196_2_1_9; -.
DR OMA; ADLNEWD; -.
DR OrthoDB; 1027643at2; -.
DR BioCyc; MetaCyc:MON-21377; -.
DR BRENDA; 1.3.1.108; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; PTHR21294; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..262
FT /note="Caffeyl-CoA reductase-Etf complex subunit CarD"
FT /id="PRO_0000435669"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 13..17
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 36..51
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 164..178
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:6FAH"
SQ SEQUENCE 262 AA; 28237 MW; 96E9640EBDF403A4 CRC64;
MRILVCAKQV PDTNEVKIDP KTGTMIREGV PSILNPDDAN ALEAALVIKD ENPGTEVIVM
TMGPPQASEM LRECLAMGAD EAYLLSDRAF GGADTWATSA TLAAGIKKVK KVDLVLAGRQ
AIDGDTAQVG SQIAQRLKMP VVTYVEDIKI EDKKAIVHRQ MEDGYEVIEV QLPCLLTCVK
ELNDPRYMSV GGIMDAYEQP ITIWNHEDIG LSPEACGLNA SPTQVFRSFS PPAKGGGEMI
TGTTVNEVAG SLVSKLKEKH II
