CARC_ACEWD
ID CARC_ACEWD Reviewed; 379 AA.
AC H6LGM6;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Caffeyl-CoA reductase-Etf complex subunit CarC {ECO:0000303|PubMed:23479729};
DE EC=1.3.1.108 {ECO:0000269|PubMed:23479729};
DE AltName: Full=Caffeoyl-CoA reductase CarC {ECO:0000303|PubMed:23479729};
DE AltName: Full=NADH-dependent caffeyl-CoA reduction {ECO:0000303|PubMed:23479729};
GN Name=carC {ECO:0000303|PubMed:23479729}; OrderedLocusNames=Awo_c15720;
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: The Caffeyl-CoA reductase-Etf complex catalyzes the reduction
CC of 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. Also reduces 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 or 2 FAD 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 acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP002987; AFA48354.1; -; Genomic_DNA.
DR RefSeq; WP_014355957.1; NC_016894.1.
DR PDB; 6FAH; X-ray; 3.13 A; C/D=1-379.
DR PDBsum; 6FAH; -.
DR AlphaFoldDB; H6LGM6; -.
DR SMR; H6LGM6; -.
DR STRING; 931626.Awo_c15720; -.
DR EnsemblBacteria; AFA48354; AFA48354; Awo_c15720.
DR KEGG; awo:Awo_c15720; -.
DR eggNOG; COG1960; Bacteria.
DR HOGENOM; CLU_018204_0_2_9; -.
DR OMA; EWDETHH; -.
DR OrthoDB; 760677at2; -.
DR BioCyc; MetaCyc:MON-21379; -.
DR BRENDA; 1.3.1.108; 52.
DR Proteomes; UP000007177; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase 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 Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR006089; Acyl-CoA_DH_CS.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..379
FT /note="Caffeyl-CoA reductase-Etf complex subunit CarC"
FT /id="PRO_0000435668"
FT ACT_SITE 362
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 122..131
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 155..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 239..242
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 267
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 335..339
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT BINDING 364..366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P15651"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 80..90
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 144..157
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 163..172
FT /evidence="ECO:0007829|PDB:6FAH"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 230..266
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 278..306
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 312..337
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 338..342
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:6FAH"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6FAH"
FT HELIX 365..376
FT /evidence="ECO:0007829|PDB:6FAH"
SQ SEQUENCE 379 AA; 41436 MW; ADCC82C213CBAAFC CRC64;
MYFSEQNKMI RKLARDFAEK ELTTEILDEV EESGEFPQEI LDKMAKFGFF GIKIPKSLGG
SGGDHMSYVI CMEEFARVSG VASVYLSSPN SLAGGPLLLS GTEEQIEKYL KPIITGKKKL
AFALTEPGAG SDAGGMSTTA VDMGDYYLLN GRKTFITMAP LCDDAVIYAK TDMSKGTRGI
SAFIVDLKSE GVSMGKNEHK MGLIGCATSD IIMEDVKVPK ENRLGEVNKG FSNAMKTLDV
GRLGVASQSI GVAQGALDEA IKYAKERKQF GKRIADFQAI AFMIADMATK LEAAKLLVYN
AASLMDNKKN ATKEASMAKF YASEICNEIC AKAVQIHGGY GYIKEYKVER MYRDCRVFTI
YEGTSQVQQM VISGMLLKK
