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P80030

- FABI_BRANA

UniProt

P80030 - FABI_BRANA

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
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
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    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

    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-SubCell

    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 – 975
    Beta strandi100 – 1045
    Helixi105 – 11511
    Beta strandi119 – 1257
    Helixi126 – 13712
    Turni138 – 1425
    Helixi143 – 1453
    Beta strandi150 – 1523
    Beta strandi155 – 1617
    Helixi168 – 1703
    Helixi173 – 1764
    Helixi179 – 1835
    Helixi189 – 20012
    Beta strandi203 – 2086
    Turni214 – 2174
    Helixi220 – 2223
    Helixi225 – 23511
    Helixi237 – 24610
    Helixi247 – 2493
    Beta strandi250 – 26011
    Helixi262 – 2643
    Turni272 – 2743
    Helixi275 – 29723
    Beta strandi300 – 3067
    Helixi312 – 3176
    Helixi319 – 33012
    Beta strandi331 – 3333
    Helixi339 – 34911
    Helixi352 – 3543
    Beta strandi361 – 3655
    Helixi368 – 3703
    Helixi378 – 3803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MAATAAASSL QMATTRPSIS AASSKARTYV VGANPRNAYK IACTPHLSNL    50
    GCLRNDSALP ASKKSFSFST KAMSESSESK ASSGLPIDLR GKRAFIAGIA 100
    DDNGYGWAVA KSLAAAGAEI LVGTWVPALN IFETSLRRGK FDQSRVLPDG 150
    SLMEIKKVYP LDAVFDNPED VPEDVKANKR YAGSSNWTVQ EAAECVRQDF 200
    GSIDILVHSL ANGPEVSKPL LETSRKGYLA AISASSYSFV SLLSHFLPIM 250
    NPGGASISLT YIASERIIPG YGGGMSSAKA ALESDTRVLA FEAGRKQNIR 300
    VNTISAGPLG SRAAKAIGFI DTMIEYSYNN APIQKTLTAD EVGNAAAFLV 350
    SPLASAITGA TIYVDNGLNS MGVALDSPVF KDLNK 385
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S60064 mRNA. Translation: AAB20114.2.
    PIRiS17761.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S60064 mRNA. Translation: AAB20114.2 .
    PIRi S17761.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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: October 1, 2014
    This is version 110 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