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P80030

- FABI_BRANA

UniProt

P80030 - FABI_BRANA

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Protein

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

Gene
N/A
Organism
Brassica napus (Rape)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei98 – 981NAD; via carbonyl oxygen3 Publications
Binding sitei105 – 1051NAD3 Publications
Binding sitei259 – 2591NAD; via carbonyl oxygen3 Publications
Active sitei261 – 2611Proton acceptorBy similarity
Active sitei271 – 2711Proton acceptorBy similarity
Binding sitei279 – 2791NAD3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1632NAD3 Publications
Nucleotide bindingi209 – 2102NAD3 Publications
Nucleotide bindingi309 – 3135NAD3 Publications

GO - Molecular functioni

  1. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB-EC

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
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

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

Plastidchloroplast Curated

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 7373Chloroplast2 PublicationsAdd
BLAST
Chaini74 – 385312Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplasticPRO_0000031984Add
BLAST

Proteomic databases

PRIDEiP80030.

Expressioni

Tissue specificityi

Seeds and leaves.

Interactioni

Subunit structurei

Homotetramer.3 Publications

Structurei

Secondary structure

1
385
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi93 – 975Combined sources
Beta strandi100 – 1045Combined sources
Helixi105 – 11511Combined sources
Beta strandi119 – 1257Combined sources
Helixi126 – 13712Combined sources
Turni138 – 1425Combined sources
Helixi143 – 1453Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi155 – 1617Combined sources
Helixi168 – 1703Combined sources
Helixi173 – 1764Combined sources
Helixi179 – 1835Combined sources
Helixi189 – 20012Combined sources
Beta strandi203 – 2086Combined sources
Turni214 – 2174Combined sources
Helixi220 – 2223Combined sources
Helixi225 – 23511Combined sources
Helixi237 – 24610Combined sources
Helixi247 – 2493Combined sources
Beta strandi250 – 26011Combined sources
Helixi262 – 2643Combined sources
Turni272 – 2743Combined sources
Helixi275 – 29723Combined sources
Beta strandi300 – 3067Combined sources
Helixi312 – 3176Combined sources
Helixi319 – 33012Combined sources
Beta strandi331 – 3333Combined sources
Helixi339 – 34911Combined sources
Helixi352 – 3543Combined sources
Beta strandi361 – 3655Combined sources
Helixi368 – 3703Combined sources
Helixi378 – 3803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWUX-ray2.50A/B85-380[»]
1D7OX-ray1.90A84-380[»]
1ENOX-ray1.90A74-383[»]
1ENPX-ray2.60A74-383[»]
ProteinModelPortaliP80030.
SMRiP80030. Positions 84-380.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80030.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041G → A AA sequence (PubMed:1912504)Curated
Sequence conflicti109 – 1091V → I AA sequence (PubMed:1912504)Curated
Sequence conflicti280 – 2812AA → N AA sequence (PubMed:1912504)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti333 – 3331I → V.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60064 mRNA. Translation: AAB20114.2.
PIRiS17761.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S60064 mRNA. Translation: AAB20114.2 .
PIRi S17761.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CWU X-ray 2.50 A/B 85-380 [» ]
1D7O X-ray 1.90 A 84-380 [» ]
1ENO X-ray 1.90 A 74-383 [» ]
1ENP X-ray 2.60 A 74-383 [» ]
ProteinModelPortali P80030.
SMRi P80030. Positions 84-380.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P80030.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00094 .

Miscellaneous databases

EvolutionaryTracei P80030.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
PRINTSi PR00081. GDHRDH.
ProtoNeti Search...

Publicationsi

  1. "cDNA cloning and expression of Brassica napus enoyl-acyl carrier protein reductase in Escherichia coli."
    Kater M.M., Koningstein G.M., Nijkamp H.J., Stuitje A.R.
    Plant Mol. Biol. 17:895-909(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-86.
    Strain: cv. Rafal.
  2. "Amino acid sequence analysis of rape seed (Brassica napus) NADH-enoyl ACP reductase."
    Slabas A.R., Cottingham I., Austin A., Fawcett T., Sidebottom C.M.
    Plant Mol. Biol. 17:911-914(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 74-122; 146-174; 181-193; 250-295; 301-311; 316-346 AND 371-385.
    Tissue: Seed.
  3. "Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase."
    Rafferty J.B., Simon J.W., Baldock C., Artymiuk P.J., Baker P.J., Stuitje A.R., Slabas A.R., Rice D.W.
    Structure 3:927-938(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 74-383 IN COMPLEX WITH NAD, SUBUNIT.
  4. "Inhibitor binding studies on enoyl reductase reveal conformational changes related to substrate recognition."
    Roujeinikova A., Sedelnikova S., de Boer G.J., Stuitje A.R., Slabas A.R., Rafferty J.B., Rice D.W.
    J. Biol. Chem. 274:30811-30817(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 85-380 IN COMPLEX WITH NAD.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 84-380 IN COMPLEX WITH NAD.

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 26, 2014
This is version 112 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

External Data

Dasty 3