FABV_TREDE
ID FABV_TREDE Reviewed; 397 AA.
AC Q73Q47;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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:17382934, ECO:0000269|PubMed:22906002, ECO:0000269|PubMed:23050861};
GN Name=fabV {ECO:0000303|PubMed:23050861}; OrderedLocusNames=TDE_0597;
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=17382934; DOI=10.1016/j.febslet.2007.03.013;
RA Tucci S., Martin W.;
RT "A novel prokaryotic trans-2-enoyl-CoA reductase from the spirochete
RT Treponema denticola.";
RL FEBS Lett. 581:1561-1566(2007).
RN [3]
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-240; LEU-276; VAL-277;
RP ILE-287; LEU-291; PHE-295 AND TYR-370, ACTIVITY REGULATION, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=22906002; DOI=10.1021/bi300879n;
RA Bond-Watts B.B., Weeks A.M., Chang M.C.;
RT "Biochemical and structural characterization of the trans-enoyl-CoA
RT reductase from Treponema denticola.";
RL Biochemistry 51:6827-6837(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
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. In vitro it can also use hexenoyl-CoA and dodecenoyl-CoA
CC as substrates (PubMed:22906002). {ECO:0000269|PubMed:17382934,
CC ECO:0000269|PubMed:22906002, 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:17382934, ECO:0000269|PubMed:22906002,
CC ECO:0000269|PubMed:23050861};
CC -!- ACTIVITY REGULATION: Inhibited by lauroyl-CoA.
CC {ECO:0000269|PubMed:22906002}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 uM for crotonyl-CoA (at pH 6.2 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:17382934};
CC KM=5.2 uM for NAD {ECO:0000269|PubMed:22906002};
CC KM=12 uM for dodecenoyl-CoA {ECO:0000269|PubMed:22906002};
CC KM=12 uM for hexenoyl-CoA {ECO:0000269|PubMed:22906002};
CC KM=69.7 uM for NAD (at pH 6.2 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23050861};
CC KM=70 uM for crotonyl-CoA {ECO:0000269|PubMed:22906002};
CC KM=190 uM for NADP {ECO:0000269|PubMed:22906002};
CC Note=kcat is 385.9 sec(-1) for reductase activity (at pH 6.2 and 25
CC degrees Celsius) (PubMed:23050861). kcat is 112 sec(-1) for reductase
CC activity with hexenoyl-CoA as substrate (PubMed:22906002). kcat is 91
CC sec(-1) for reductase activity with crotonyl-CoA as substrate
CC (PubMed:22906002). kcat is 90 sec(-1) for reductase activity with
CC dodecenoyl-CoA as substrate (PubMed:22906002).
CC {ECO:0000269|PubMed:22906002, ECO:0000269|PubMed:23050861};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17382934,
CC ECO:0000269|PubMed:22906002, 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 T.denticola 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; AE017226; AAS11092.1; -; Genomic_DNA.
DR RefSeq; NP_971211.1; NC_002967.9.
DR RefSeq; WP_002681770.1; NC_002967.9.
DR PDB; 4FBG; X-ray; 3.02 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-397.
DR PDB; 4GGO; X-ray; 2.00 A; A/B/C/D=1-397.
DR PDB; 4GGP; X-ray; 2.05 A; A/B/C/D=1-397.
DR PDBsum; 4FBG; -.
DR PDBsum; 4GGO; -.
DR PDBsum; 4GGP; -.
DR AlphaFoldDB; Q73Q47; -.
DR SMR; Q73Q47; -.
DR STRING; 243275.TDE_0597; -.
DR EnsemblBacteria; AAS11092; AAS11092; TDE_0597.
DR GeneID; 2741560; -.
DR KEGG; tde:TDE_0597; -.
DR PATRIC; fig|243275.7.peg.577; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_12; -.
DR OMA; EGCIEQI; -.
DR OrthoDB; 678530at2; -.
DR BRENDA; 1.3.1.44; 6426.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008212; 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; 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.
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..397
FT /note="Trans-2-enoyl-CoA reductase [NADH]"
FT /id="PRO_0000220050"
FT ACT_SITE 240
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838,
FT ECO:0000305|PubMed:22906002, ECO:0000305|PubMed:23050861"
FT BINDING 53..58
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 79..80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 116..117
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 144..145
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 249
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT BINDING 276..278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:23050861"
FT SITE 80
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000269|PubMed:23050861"
FT MUTAGEN 240
FT /note="Y->F: Loss of reductase activity, but no significant
FT change in the affinity for crotonyl-CoA."
FT /evidence="ECO:0000269|PubMed:22906002"
FT MUTAGEN 276
FT /note="L->A: Significant decrease of the catalytic
FT efficiency; when associated with A-277. The catalytic
FT efficiency is slightly reduces and the affinity is
FT relatively similar to wild-type; when associated with A-277
FT and A-295."
FT /evidence="ECO:0000269|PubMed:22906002"
FT MUTAGEN 277
FT /note="V->A: Significant decrease of the catalytic
FT efficiency; when associated with A-276. The catalytic
FT efficiency is slightly reduces and the affinity is
FT relatively similar to wild-type; when associated with A-276
FT and A-295."
FT /evidence="ECO:0000269|PubMed:22906002"
FT MUTAGEN 287
FT /note="I->A: Shows 7-, 13- and 15-fold decrease of
FT catalytic efficiency of the reductase activity for
FT hexenoyl-CoA, crotonyl-CoA and dodecenoyl-CoA,
FT respectively. The affinity is relatively similar to wild-
FT type. This mutation may increase the accessibility of the
FT longer acyl chain to the active site pocket."
FT /evidence="ECO:0000269|PubMed:22906002"
FT MUTAGEN 291
FT /note="L->A: The catalytic efficiency and affinity are
FT relatively similar to wild-type toward crotonyl-CoA and
FT hexenoyl-CoA."
FT /evidence="ECO:0000269|PubMed:22906002"
FT MUTAGEN 295
FT /note="F->A: The catalytic efficiency and affinity are
FT relatively similar to wild-type toward crotonyl-CoA and
FT hexenoyl-CoA. The catalytic efficiency is slightly reduces
FT and the affinity is relatively similar to wild-type; when
FT associated with A-276 and A-277."
FT /evidence="ECO:0000269|PubMed:22906002"
FT MUTAGEN 370
FT /note="Y->A: The catalytic efficiency and affinity are
FT relatively similar to wild-type toward crotonyl-CoA and
FT hexenoyl-CoA."
FT /evidence="ECO:0000269|PubMed:22906002"
FT HELIX 17..34
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4FBG"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:4GGO"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 169..174
FT /evidence="ECO:0007829|PDB:4GGO"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 244..262
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 287..301
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:4GGO"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:4GGO"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:4GGO"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:4GGO"
FT TURN 377..379
FT /evidence="ECO:0007829|PDB:4GGO"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:4GGO"
SQ SEQUENCE 397 AA; 43759 MW; 7D5916140E5A8F35 CRC64;
MIVKPMVRNN ICLNAHPQGC KKGVEDQIEY TKKRITAEVK AGAKAPKNVL VLGCSNGYGL
ASRITAAFGY GAATIGVSFE KAGSETKYGT PGWYNNLAFD EAAKREGLYS VTIDGDAFSD
EIKAQVIEEA KKKGIKFDLI VYSLASPVRT DPDTGIMHKS VLKPFGKTFT GKTVDPFTGE
LKEISAEPAN DEEAAATVKV MGGEDWERWI KQLSKEGLLE EGCITLAYSY IGPEATQALY
RKGTIGKAKE HLEATAHRLN KENPSIRAFV SVNKGLVTRA SAVIPVIPLY LASLFKVMKE
KGNHEGCIEQ ITRLYAERLY RKDGTIPVDE ENRIRIDDWE LEEDVQKAVS ALMEKVTGEN
AESLTDLAGY RHDFLASNGF DVEGINYEAE VERFDRI
