FABV_BURMA
ID FABV_BURMA Reviewed; 397 AA.
AC Q62L02;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000303|PubMed:20055482};
DE Short=ENR {ECO:0000303|PubMed:20055482};
DE EC=1.3.1.9 {ECO:0000269|PubMed:20055482};
DE AltName: Full=NADH-dependent enoyl-ACP reductase {ECO:0000303|PubMed:20055482};
DE AltName: Full=Trans-2-enoyl-CoA reductase [NADH] {ECO:0000303|PubMed:20055482};
DE Short=TER {ECO:0000303|PubMed:20055482};
DE EC=1.3.1.44 {ECO:0000269|PubMed:20055482};
GN Name=fabV {ECO:0000303|PubMed:20055482}; OrderedLocusNames=BMA0885;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP TYR-235; LYS-244 AND LYS-245, ACTIVITY REGULATION, REACTION MECHANISM, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 23344;
RX PubMed=20055482; DOI=10.1021/bi902001a;
RA Lu H., Tonge P.J.;
RT "Mechanism and inhibition of the FabV enoyl-ACP reductase from Burkholderia
RT mallei.";
RL Biochemistry 49:1281-1289(2010).
CC -!- FUNCTION: Involved in the final reduction of the elongation cycle of
CC fatty acid synthesis (FAS II). Catalyzes the NADH-dependent reduction
CC of the carbon-carbon double bond in the enoyl moiety that is covalently
CC linked to an acyl carrier protein (ACP). It is also able to reduce
CC trans-2-dodecenoyl-CoA (DD-CoA). {ECO:0000269|PubMed:20055482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000269|PubMed:20055482};
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:20055482};
CC -!- ACTIVITY REGULATION: Inhibited by triclosan.
CC {ECO:0000269|PubMed:20055482}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for DD-CoA (with His tag) {ECO:0000269|PubMed:20055482};
CC KM=4.4 uM for DD-CoA (without His tag) {ECO:0000269|PubMed:20055482};
CC KM=23 uM for NADH {ECO:0000269|PubMed:20055482};
CC Note=kcat is 1728 min(-1) for reductase activity with DD-CoA as
CC substrate (without His tag). kcat is 1242 min(-1) for reductase
CC activity with DD-CoA as substrate (with His tag).
CC {ECO:0000269|PubMed:20055482};
CC pH dependence:
CC Optimum pH is 7.9. {ECO:0000269|PubMed:20055482};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01838}.
CC -!- SIMILARITY: Belongs to the TER reductase family. {ECO:0000255|HAMAP-
CC Rule:MF_01838}.
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DR EMBL; CP000010; AAU49089.1; -; Genomic_DNA.
DR RefSeq; WP_004192836.1; NC_006348.1.
DR RefSeq; YP_102617.1; NC_006348.1.
DR AlphaFoldDB; Q62L02; -.
DR SMR; Q62L02; -.
DR STRING; 243160.BMA0885; -.
DR EnsemblBacteria; AAU49089; AAU49089; BMA0885.
DR GeneID; 56595374; -.
DR KEGG; bma:BMA0885; -.
DR PATRIC; fig|243160.12.peg.915; -.
DR eggNOG; COG3007; Bacteria.
DR HOGENOM; CLU_057698_1_0_4; -.
DR OMA; EGCIEQI; -.
DR BRENDA; 1.3.1.9; 1030.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000006693; Chromosome 1.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
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 Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; NAD; Oxidoreductase.
FT CHAIN 1..397
FT /note="Enoyl-[acyl-carrier-protein] reductase [NADH]"
FT /id="PRO_0000220038"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838,
FT ECO:0000305|PubMed:20055482"
FT BINDING 48..53
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 74..75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 139..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT BINDING 244
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838,
FT ECO:0000305|PubMed:20055482"
FT BINDING 273..275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT SITE 75
FT /note="Plays an important role in discriminating NADH
FT against NADPH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01838"
FT MUTAGEN 235
FT /note="Y->A: 250-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20055482"
FT MUTAGEN 235
FT /note="Y->S: 200-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20055482"
FT MUTAGEN 244
FT /note="K->A: This mutation causes a small decrease in the
FT affinity for both DD-CoA and NADH, and a 110-fold decrease
FT in catalytic efficiency is observed. Loss of reductase
FT activity; when associated with A-245."
FT /evidence="ECO:0000269|PubMed:20055482"
FT MUTAGEN 244
FT /note="K->R: This mutation causes a small decrease in the
FT affinity for both DD-CoA and NADH, and a 950-fold decrease
FT in catalytic efficiency is observed."
FT /evidence="ECO:0000269|PubMed:20055482"
FT MUTAGEN 245
FT /note="K->A: 3-fold decrease in affinity for DD-CoA. Loss
FT of reductase activity; when associated with A-244."
FT /evidence="ECO:0000269|PubMed:20055482"
FT MUTAGEN 245
FT /note="K->M: 10-fold decrease in affinity for DD-CoA, and
FT 70-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:20055482"
SQ SEQUENCE 397 AA; 42802 MW; D2295F17FDD6D18A CRC64;
MIIKPRVRGF ICVTTHPAGC AASVREQIAY VARRGPIERG PKKVLVIGAS TGYGLAARIA
AAFGVGAATL GVFFERAPAD AKPGTAGWYN SAAFHDEAAA RGLQATSVNG DAFSDEIKHK
TIDAIRRDLG QVDLVVYSVA APRRTHPKTG VTHQSTLKPI GHAVRLRGID TDNEAIKETL
LQPATPDEIA DTVAVMGGED WRMWIDALDA AGVLADGAKT TAFTYLGEQV THDIYWNGSI
GEAKKDLDRT VLALRGKLAA RGGDARVSVL KAVVTQASSA IPMMPLYLSL LFKVMKARGT
HEGCIEQVDG LLRDSLYSAQ PHVDAEGRLR ADRLELDPAV QARVLELWDQ VTDDNLYTLT
DFAGYKAEFL RLFGFGIDGV DYDAPVEPNV RIPNLIE
