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Enoyl-[acyl-carrier-protein] reductase [NADH] (ENR) (EC 1.3.1.9)

 H1S5V0_9BURK            Unreviewed;       398 AA.
H1S5V0;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
22-NOV-2017, entry version 32.
RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000256|HAMAP-Rule:MF_01838};
Short=ENR {ECO:0000256|HAMAP-Rule:MF_01838};
EC=1.3.1.9 {ECO:0000256|HAMAP-Rule:MF_01838};
Name=fabV {ECO:0000256|HAMAP-Rule:MF_01838};
ORFNames=OR16_16217 {ECO:0000313|EMBL:EHP42182.1};
Cupriavidus basilensis OR16.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Cupriavidus.
NCBI_TaxID=1127483 {ECO:0000313|EMBL:EHP42182.1, ECO:0000313|Proteomes:UP000005808};
[1] {ECO:0000313|EMBL:EHP42182.1, ECO:0000313|Proteomes:UP000005808}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR16 {ECO:0000313|EMBL:EHP42182.1,
ECO:0000313|Proteomes:UP000005808};
PubMed=22461549; DOI=10.1128/JB.06752-11;
Cserhati M., Kriszt B., Szoboszlay S., Toth A., Szabo I., Tancsics A.,
Nagy I., Horvath B., Nagy I., Kukolya J.;
"De Novo Genome Project of Cupriavidus basilensis OR16.";
J. Bacteriol. 194:2109-2110(2012).
-!- FUNCTION: Involved in the final reduction of the elongation cycle
of fatty acid synthesis (FAS II). Catalyzes the reduction of a
carbon-carbon double bond in an enoyl moiety that is covalently
linked to an acyl carrier protein (ACP). {ECO:0000256|HAMAP-
Rule:MF_01838}.
-!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NAD(+) = a
trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
{ECO:0000256|HAMAP-Rule:MF_01838}.
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00946250}.
-!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01838,
ECO:0000256|SAAS:SAAS00946236}.
-!- SIMILARITY: Belongs to the TER reductase family.
{ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00946247}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EHP42182.1}.
-----------------------------------------------------------------------
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EMBL; AHJE01000038; EHP42182.1; -; Genomic_DNA.
RefSeq; WP_006158794.1; NZ_AHJE01000038.1.
EnsemblBacteria; EHP42182; EHP42182; OR16_16217.
PATRIC; fig|1127483.3.peg.3255; -.
OrthoDB; POG091H03HI; -.
UniPathway; UPA00094; -.
Proteomes; UP000005808; Unassembled WGS sequence.
GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
HAMAP; MF_01838; FabV_reductase; 1.
InterPro; IPR024906; Eno_Rdtase_FAD-bd_dom.
InterPro; IPR024910; Enoyl-CoA_Rdtase_cat_dom.
InterPro; IPR010758; Trans-2-enoyl-CoA_reductase.
PANTHER; PTHR37480; PTHR37480; 1.
Pfam; PF07055; Eno-Rase_FAD_bd; 1.
Pfam; PF12242; Eno-Rase_NADH_b; 1.
Pfam; PF12241; Enoyl_reductase; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000005808};
Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
ECO:0000256|SAAS:SAAS00946244};
Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
ECO:0000256|SAAS:SAAS00946244};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01838,
ECO:0000256|SAAS:SAAS00946244};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01838,
ECO:0000256|SAAS:SAAS00946244};
NAD {ECO:0000256|HAMAP-Rule:MF_01838, ECO:0000256|SAAS:SAAS00946240};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01838,
ECO:0000256|SAAS:SAAS00946243, ECO:0000313|EMBL:EHP42182.1}.
DOMAIN 82 317 Enoyl_reductase.
{ECO:0000259|Pfam:PF12241}.
DOMAIN 324 386 Eno-Rase_FAD_bd.
{ECO:0000259|Pfam:PF07055}.
NP_BIND 48 53 NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
NP_BIND 74 75 NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
NP_BIND 111 112 NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
NP_BIND 139 140 NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
NP_BIND 273 275 NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
ACT_SITE 235 235 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_01838}.
BINDING 225 225 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01838}.
BINDING 244 244 NAD. {ECO:0000256|HAMAP-Rule:MF_01838}.
SITE 75 75 Plays an important role in discriminating
NADH against NADPH. {ECO:0000256|HAMAP-
Rule:MF_01838}.
SEQUENCE 398 AA; 43164 MW; D65D331891A440C9 CRC64;
MIIGPRVRGF MCVTAHPTGC EANVNQQIAY VKANGPVANG PKKVLVIGAS TGYGLAARIT
ATFGCGADTL GVFFERAGSE SKPGTAGWYN TAAFHKAATA EGRYAMSING DGFSDEIKQQ
TIDIIKRDLG QVDLVVYSLA APRRKHPKTG EIFNSTLKPI GKEIRQRGLD TDKEVIKEIN
LQPATQEEID HTVAVMGGED WQMWIDALLA AGVLADNAKT TAFTYLGEKI THDIYWNGSI
GAAKKDLDQK VLDLRGKLAA TGGDARVAVL KAVVTQASSA IPVMPLYLSL LFKVMKETGT
HEGCIEQVDS LYRDCLYSQS PRQDAEGRLR TDEKELSPDV QARVTQLWDQ VNNDNIYALT
DFAGYKAEFL RLFGFGIDGV DYAADVNPAV EIPNLVEA


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