Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth (By similarity).By similarity

Catalytic activityi

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Enzyme regulationi

Inactivated by phenylglyoxal by binding covalently to two arginine residues.

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei98NAD; via carbonyl oxygen3 Publications1
Binding sitei105NAD3 Publications1
Binding sitei259NAD; via carbonyl oxygen3 Publications1
Active sitei261Proton acceptorBy similarity1
Active sitei271Proton acceptorBy similarity1
Binding sitei279NAD3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi162 – 163NAD3 Publications2
Nucleotide bindingi209 – 210NAD3 Publications2
Nucleotide bindingi309 – 313NAD3 Publications5

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.3.1.9. 944.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic (EC:1.3.1.9)
Alternative name(s):
NADH-dependent enoyl-ACP reductase
OrganismiBrassica napus (Rape)
Taxonomic identifieri3708 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 73Chloroplast2 PublicationsAdd BLAST73
ChainiPRO_000003198474 – 385Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplasticAdd BLAST312

Proteomic databases

PRIDEiP80030.

Expressioni

Tissue specificityi

Seeds and leaves.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Structurei

Secondary structure

1385
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi93 – 97Combined sources5
Beta strandi100 – 104Combined sources5
Helixi105 – 115Combined sources11
Beta strandi119 – 125Combined sources7
Helixi126 – 137Combined sources12
Turni138 – 142Combined sources5
Helixi143 – 145Combined sources3
Beta strandi150 – 152Combined sources3
Beta strandi155 – 161Combined sources7
Helixi168 – 170Combined sources3
Helixi173 – 176Combined sources4
Helixi179 – 183Combined sources5
Helixi189 – 200Combined sources12
Beta strandi203 – 208Combined sources6
Turni214 – 217Combined sources4
Helixi220 – 222Combined sources3
Helixi225 – 235Combined sources11
Helixi237 – 246Combined sources10
Helixi247 – 249Combined sources3
Beta strandi250 – 260Combined sources11
Helixi262 – 264Combined sources3
Turni272 – 274Combined sources3
Helixi275 – 297Combined sources23
Beta strandi300 – 306Combined sources7
Helixi312 – 317Combined sources6
Helixi319 – 330Combined sources12
Beta strandi331 – 333Combined sources3
Helixi339 – 349Combined sources11
Helixi352 – 354Combined sources3
Beta strandi361 – 365Combined sources5
Helixi368 – 370Combined sources3
Helixi378 – 380Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CWUX-ray2.50A/B85-380[»]
1D7OX-ray1.90A84-380[»]
1ENOX-ray1.90A74-383[»]
1ENPX-ray2.60A74-383[»]
ProteinModelPortaliP80030.
SMRiP80030.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80030.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK00208.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 4 hits.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P80030-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATAAASSL QMATTRPSIS AASSKARTYV VGANPRNAYK IACTPHLSNL
60 70 80 90 100
GCLRNDSALP ASKKSFSFST KAMSESSESK ASSGLPIDLR GKRAFIAGIA
110 120 130 140 150
DDNGYGWAVA KSLAAAGAEI LVGTWVPALN IFETSLRRGK FDQSRVLPDG
160 170 180 190 200
SLMEIKKVYP LDAVFDNPED VPEDVKANKR YAGSSNWTVQ EAAECVRQDF
210 220 230 240 250
GSIDILVHSL ANGPEVSKPL LETSRKGYLA AISASSYSFV SLLSHFLPIM
260 270 280 290 300
NPGGASISLT YIASERIIPG YGGGMSSAKA ALESDTRVLA FEAGRKQNIR
310 320 330 340 350
VNTISAGPLG SRAAKAIGFI DTMIEYSYNN APIQKTLTAD EVGNAAAFLV
360 370 380
SPLASAITGA TIYVDNGLNS MGVALDSPVF KDLNK
Length:385
Mass (Da):40,479
Last modified:February 1, 1994 - v2
Checksum:iC435BCE32A8D059B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti104G → A AA sequence (PubMed:1912504).Curated1
Sequence conflicti109V → I AA sequence (PubMed:1912504).Curated1
Sequence conflicti280 – 281AA → N AA sequence (PubMed:1912504).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti333I → V.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60064 mRNA. Translation: AAB20114.2.
PIRiS17761.
RefSeqiXP_013685121.1. XM_013829667.1.
XP_013685122.1. XM_013829668.1.
XP_013714468.1. XM_013859014.1.
XP_013714469.1. XM_013859015.1.

Genome annotation databases

GeneIDi106389421.
106418332.
KEGGibna:106389421.
bna:106418332.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60064 mRNA. Translation: AAB20114.2.
PIRiS17761.
RefSeqiXP_013685121.1. XM_013829667.1.
XP_013685122.1. XM_013829668.1.
XP_013714468.1. XM_013859014.1.
XP_013714469.1. XM_013859015.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CWUX-ray2.50A/B85-380[»]
1D7OX-ray1.90A84-380[»]
1ENOX-ray1.90A74-383[»]
1ENPX-ray2.60A74-383[»]
ProteinModelPortaliP80030.
SMRiP80030.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP80030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi106389421.
106418332.
KEGGibna:106389421.
bna:106418332.

Phylogenomic databases

KOiK00208.

Enzyme and pathway databases

UniPathwayiUPA00094.
BRENDAi1.3.1.9. 944.

Miscellaneous databases

EvolutionaryTraceiP80030.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 4 hits.
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFABI_BRANA
AccessioniPrimary (citable) accession number: P80030
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1994
Last modified: November 2, 2016
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.