FABV_CLOAB
ID FABV_CLOAB Reviewed; 398 AA.
AC Q97LU2;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000303|PubMed:23050861};
DE Short=TER {ECO:0000303|PubMed:23050861};
DE EC=1.3.1.44 {ECO:0000269|PubMed:23050861};
GN Name=fabV {ECO:0000303|PubMed:23050861}; OrderedLocusNames=CA_C0462;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP BIOTECHNOLOGY.
RX PubMed=21358636; DOI=10.1038/nchembio.537;
RA Bond-Watts B.B., Bellerose R.J., Chang M.C.;
RT "Enzyme mechanism as a kinetic control element for designing synthetic
RT biofuel pathways.";
RL Nat. Chem. Biol. 7:222-227(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF PHE-11;
RP GLU-75; TYR-225; TYR-235; LYS-244 AND LYS-245, AND SUBUNIT.
RX PubMed=23050861; DOI=10.1042/bj20120871;
RA Hu K., Zhao M., Zhang T., Zha M., Zhong C., Jiang Y., Ding J.;
RT "Structures of trans-2-enoyl-CoA reductases from Clostridium acetobutylicum
RT and Treponema denticola: insights into the substrate specificity and the
RT catalytic mechanism.";
RL Biochem. J. 449:79-89(2013).
CC -!- FUNCTION: Involved in the fatty acid synthesis (FAS II). Catalyzes the
CC reduction of the carbon-carbon double bond of crotonyl-CoA to yield
CC butyryl-CoA. {ECO:0000269|PubMed:23050861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + NAD(+) = a (2E)-enoyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:18177, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.1.44;
CC Evidence={ECO:0000269|PubMed:23050861};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=105.4 uM for NAD (at pH 6.2 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23050861};
CC Note=kcat is 28.2 sec(-1) for reductase activity (at pH 6.2 and 25
CC degrees Celsius). {ECO:0000269|PubMed:23050861};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23050861}.
CC -!- BIOTECHNOLOGY: Used in the biosynthesis of medium-chain volatile
CC alcohols as biofuels engineered by microorganisms. The switch from the
CC native flavin-dependent enoyl-CoA reductase used in the production of
CC n-butanol, a key second-generation biofuel, to a flavin-independent
CC trans-enoyl-CoA reductase from C.acetobutylicum leads to an order of
CC magnitude increase in product yield in engineered E.coli.
CC {ECO:0000269|PubMed:21358636}.
CC -!- MISCELLANEOUS: Possesses high activity for the reduction reaction, but
CC no activity for the reverse oxidation reaction.
CC {ECO:0000305|PubMed:23050861}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; AE001437; AAK78442.1; -; Genomic_DNA.
DR PIR; G96956; G96956.
DR RefSeq; NP_347102.1; NC_003030.1.
DR RefSeq; WP_010963784.1; NC_003030.1.
DR PDB; 4EUE; X-ray; 2.00 A; A=1-398.
DR PDB; 4EUF; X-ray; 2.70 A; A=1-398.
DR PDB; 4EUH; X-ray; 2.10 A; A=1-398.
DR PDBsum; 4EUE; -.
DR PDBsum; 4EUF; -.
DR PDBsum; 4EUH; -.
DR AlphaFoldDB; Q97LU2; -.
DR SMR; Q97LU2; -.
DR STRING; 272562.CA_C0462; -.
DR EnsemblBacteria; AAK78442; AAK78442; CA_C0462.
DR GeneID; 44996971; -.
DR KEGG; cac:CA_C0462; -.
DR PATRIC; fig|272562.8.peg.661; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_9; -.
DR OMA; EGCIEQI; -.
DR OrthoDB; 678530at2; -.
DR BRENDA; 1.3.1.44; 1452.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050343; F:trans-2-enoyl-CoA reductase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IDA:UniProtKB.
DR HAMAP; MF_01838; FabV_reductase; 1.
DR InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
DR InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
DR PANTHER; PTHR37480; PTHR37480; 1.
DR Pfam; PF07055; Eno-Rase_FAD_bd; 1.
DR Pfam; PF12242; Eno-Rase_NADH_b; 1.
DR Pfam; PF12241; Enoyl_reductase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..398
FT /note="Trans-2-enoyl-CoA reductase [NADH]"
FT /id="PRO_0000220040"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838,
FT ECO:0000305|PubMed:23050861"
FT BINDING 47..52
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 274..276
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 11
FT /note="F->K: Slight decrease of catalytic efficiency and 3-
FT fold increase of the affinity for NADH compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 75
FT /note="E->A: Able to use both NADH and NADPH as cofactor."
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 225
FT /note="Y->A: 12-fold decrease of catalytic efficiency and
FT slight decrease of the affinity for NADH compared to wild-
FT type."
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 235
FT /note="Y->F: Loss of reductase activity."
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 244
FT /note="K->A: Loss of reductase activity."
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 245
FT /note="K->A: Slight decrease of catalytic efficiency and
FT affinity for NADH compared to wild-type."
FT /evidence="ECO:0000269|PubMed:23050861"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 17..33
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 51..62
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 86..100
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4EUE"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4EUE"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 214..224
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4EUE"
FT TURN 232..237
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 239..262
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 285..298
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4EUE"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:4EUE"
FT TURN 335..338
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 340..352
FT /evidence="ECO:0007829|PDB:4EUE"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 364..374
FT /evidence="ECO:0007829|PDB:4EUE"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:4EUE"
SQ SEQUENCE 398 AA; 45650 MW; 59324A21CA466DFC CRC64;
MIVKAKFVKG FIRDVHPYGC RREVLNQIDY CKKAIGFRGP KKVLIVGASS GFGLATRISV
AFGGPEAHTI GVSYETGATD RRIGTAGWYN NIFFKEFAKK KGLVAKNFIE DAFSNETKDK
VIKYIKDEFG KIDLFVYSLA APRRKDYKTG NVYTSRIKTI LGDFEGPTID VERDEITLKK
VSSASIEEIE ETRKVMGGED WQEWCEELLY EDCFSDKATT IAYSYIGSPR TYKIYREGTI
GIAKKDLEDK AKLINEKLNR VIGGRAFVSV NKALVTKASA YIPTFPLYAA ILYKVMKEKN
IHENCIMQIE RMFSEKIYSN EKIQFDDKGR LRMDDLELRK DVQDEVDRIW SNITPENFKE
LSDYKGYKKE FMNLNGFDLD GVDYSKDLDI ELLRKLEP
