CARE_ACEWD
ID CARE_ACEWD Reviewed; 396 AA.
AC H6LGM8;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Caffeyl-CoA reductase-Etf complex subunit CarE {ECO:0000305};
DE EC=1.3.1.108 {ECO:0000269|PubMed:23479729};
DE AltName: Full=Electron transfer flavoprotein large subunit {ECO:0000305};
DE Short=ETFLS {ECO:0000305};
DE AltName: Full=Electron transfer flavoprotein subunit alpha {ECO:0000303|PubMed:23479729};
DE Short=Alpha-ETF {ECO:0000303|PubMed:23479729};
GN Name=carE {ECO:0000303|PubMed:23479729}; OrderedLocusNames=Awo_c15740;
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 iron-
CC sulfur cluster may be involved in electron transport, possibly in the
CC intramolecular electron transfer from the Etf protein subunit to the
CC caffeyl-CoA reductase subunit inside the complex. The complex can also
CC reduce 4-coumaroyl-CoA and feruloyl-CoA. {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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:23479729};
CC Note=Binds 2 [4Fe-4S] cluster per subunit.
CC {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 alpha-subunit/FixB family.
CC {ECO:0000305}.
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DR EMBL; CP002987; AFA48356.1; -; Genomic_DNA.
DR RefSeq; WP_014355959.1; NC_016894.1.
DR PDB; 6FAH; X-ray; 3.13 A; A/E=1-396.
DR PDBsum; 6FAH; -.
DR AlphaFoldDB; H6LGM8; -.
DR SMR; H6LGM8; -.
DR STRING; 931626.Awo_c15740; -.
DR EnsemblBacteria; AFA48356; AFA48356; Awo_c15740.
DR KEGG; awo:Awo_c15740; -.
DR eggNOG; COG2025; Bacteria.
DR HOGENOM; CLU_034178_1_1_9; -.
DR OMA; VKVCPAQ; -.
DR OrthoDB; 1400253at2; -.
DR BioCyc; MetaCyc:MON-21378; -.
DR BRENDA; 1.3.1.108; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR CDD; cd01715; ETF_alpha; 1.
DR Gene3D; 3.40.50.620; -; 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; PTHR43153; 1.
DR Pfam; PF01012; ETF; 1.
DR Pfam; PF00766; ETF_alpha; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR PIRSF; PIRSF000089; Electra_flavoP_a; 1.
DR SMART; SM00893; ETF; 1.
DR SUPFAM; SSF52467; SSF52467; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..396
FT /note="Caffeyl-CoA reductase-Etf complex subunit CarE"
FT /id="PRO_0000435670"
FT BINDING 335..363
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P13804"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 84..100
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 143..155
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 292..302
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 314..316
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 336..340
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 380..392
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:6FAH"
SQ SEQUENCE 396 AA; 42488 MW; DA3AC9778ADAB1AF CRC64;
MAIKVIEEKC IGCSKCQKSC PFDAITIENK IAVIGDACTN CGTCIDVCPT EAILQEGTEK
IVRDLSMYKG VWVFAEQREG KIMPVVFELL GEGKKLANEI GTELCAILCG SNVAELTDEL
FAYGADKVYL ADAPELEKYT TDGYSKIINE AIGLYKPEIV LYGATHIGRD LAPCLAVKVN
TGLTADCTKL EIDPDDKKIR QTRPAFGGNL MATIVCPGSR PQMSTVRPGV MDKAAYDPSQ
KGEVIKLDAT FNEGDIRTKV LEIVKTTTDN ISISDADFIV SGGMGLGKPE GFELLKQLAD
KLGGTVATSR ACVDAGWADH AQQVGQTGTT VKPQIYFACG ISGAIQHIAG MQDSDIIIAI
NKNENAPIFE VADYGIVGDL YKVIPAIIEE LDKIGK
