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Protein

9-cis-epoxycarotenoid dioxygenase 1, chloroplastic

Gene

VP14

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Not active on the all-trans isomers of violaxanthin and neoxanthin. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.3 Publications

Catalytic activityi

A 9-cis-epoxycarotenoid + O2 = 2-cis,4-trans-xanthoxin + a 12'-apo-carotenal.2 Publications
9-cis-violaxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6S)-5,6-epoxy-3-hydroxy-5,6-dihydro-12'-apo-beta-caroten-12'-al.2 Publications
9'-cis-neoxanthin + O2 = 2-cis,4-trans-xanthoxin + (3S,5R,6R)-5,6-dihydroxy-6,7-didehydro-5,6-dihydro-12'-apo-beta-caroten-12'-al.2 Publications

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Kineticsi

Vmax with 9-cis violaxanthin as substrate is more than twice the Vmax with 9-cis neoxanthin as substrate.

  1. KM=20 µM for 9-cis antheraxanthin1 Publication
  2. KM=15 µM for 9-cis luteoxanthin 8'S1 Publication
  3. KM=8 µM for 9-cis luteoxanthin 8'R1 Publication
  4. KM=27 µM for 9-cis neoxanthin1 Publication
  5. KM=58 µM for 9-cis violaxanthin1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi298 – 2981Iron; catalytic
    Metal bindingi347 – 3471Iron; catalytic
    Metal bindingi412 – 4121Iron; catalytic
    Metal bindingi590 – 5901Iron; catalytic

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Abscisic acid biosynthesis, Stress response

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BRENDAi1.13.11.51. 6752.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    9-cis-epoxycarotenoid dioxygenase 1, chloroplastic (EC:1.13.11.512 Publications)
    Alternative name(s):
    Protein VIVIPAROUS141 Publication
    Short name:
    VP-14
    Short name:
    VP141 Publication
    Gene namesi
    Name:VP14
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
    Proteomesi
    • UP000007305 Componenti: Unplaced

    Organism-specific databases

    MaizeGDBi726071.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    Plants show a viviparous phenotype.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901A → AGGG: Loss of binding to the thylakoid membrane. 1 Publication
    Mutagenesisi90 – 901A → APPP: Loss of binding to the thylakoid membrane. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2323ChloroplastSequence analysisAdd
    BLAST
    Chaini24 – 6045819-cis-epoxycarotenoid dioxygenase 1, chloroplasticPRO_0000282607Add
    BLAST

    Proteomic databases

    PaxDbiO24592.

    Expressioni

    Tissue specificityi

    Expressed in leaves, roots and embryos.1 Publication

    Inductioni

    By drought stress.1 Publication

    Interactioni

    Protein-protein interaction databases

    STRINGi4577.GRMZM2G014392_P01.

    Structurei

    Secondary structure

    1
    604
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi87 – 10115Combined sources
    Helixi102 – 1087Combined sources
    Turni115 – 1173Combined sources
    Helixi119 – 1224Combined sources
    Helixi125 – 1273Combined sources
    Beta strandi133 – 1386Combined sources
    Beta strandi141 – 1433Combined sources
    Beta strandi150 – 1556Combined sources
    Helixi170 – 1723Combined sources
    Beta strandi175 – 1839Combined sources
    Beta strandi186 – 1949Combined sources
    Helixi198 – 2069Combined sources
    Turni214 – 2196Combined sources
    Helixi223 – 23513Combined sources
    Helixi241 – 2433Combined sources
    Beta strandi252 – 2554Combined sources
    Beta strandi258 – 2614Combined sources
    Beta strandi269 – 2735Combined sources
    Beta strandi279 – 2846Combined sources
    Helixi287 – 2893Combined sources
    Turni303 – 3053Combined sources
    Beta strandi308 – 3125Combined sources
    Beta strandi315 – 3184Combined sources
    Beta strandi322 – 3265Combined sources
    Beta strandi353 – 3608Combined sources
    Beta strandi362 – 3654Combined sources
    Helixi367 – 3704Combined sources
    Turni371 – 3733Combined sources
    Beta strandi376 – 3794Combined sources
    Beta strandi386 – 3916Combined sources
    Helixi397 – 3993Combined sources
    Beta strandi401 – 4044Combined sources
    Beta strandi409 – 41810Combined sources
    Turni420 – 4223Combined sources
    Beta strandi425 – 4328Combined sources
    Beta strandi441 – 4444Combined sources
    Beta strandi449 – 4557Combined sources
    Turni457 – 4593Combined sources
    Beta strandi462 – 4687Combined sources
    Beta strandi470 – 4723Combined sources
    Beta strandi476 – 4816Combined sources
    Helixi483 – 4853Combined sources
    Beta strandi491 – 4977Combined sources
    Beta strandi506 – 5116Combined sources
    Turni512 – 5143Combined sources
    Beta strandi517 – 5215Combined sources
    Beta strandi532 – 5354Combined sources
    Beta strandi540 – 5434Combined sources
    Beta strandi549 – 55911Combined sources
    Beta strandi563 – 5697Combined sources
    Turni570 – 5734Combined sources
    Beta strandi574 – 58310Combined sources
    Beta strandi591 – 5955Combined sources
    Helixi596 – 5994Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NPEX-ray3.20A76-604[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO24592.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi90 – 945Poly-Ala

    Domaini

    The N-terminal amphipathic alpha-helix (81-100) is essential, but not sufficient, for the thylakoid membrane targeting.

    Sequence similaritiesi

    Belongs to the carotenoid oxygenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG1285. Eukaryota.
    COG3670. LUCA.
    HOGENOMiHOG000254836.
    KOiK09840.

    Family and domain databases

    InterProiIPR004294. Carotenoid_Oase.
    [Graphical view]
    PANTHERiPTHR10543. PTHR10543. 1 hit.
    PfamiPF03055. RPE65. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O24592-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MQGLAPPTSV SIHRHLPARS RARASNSVRF SPRAVSSVPP AECLQAPFHK
    60 70 80 90 100
    PVADLPAPSR KPAAIAVPGH AAAPRKAEGG KKQLNLFQRA AAAALDAFEE
    110 120 130 140 150
    GFVANVLERP HGLPSTADPA VQIAGNFAPV GERPPVHELP VSGRIPPFID
    160 170 180 190 200
    GVYARNGANP CFDPVAGHHL FDGDGMVHAL RIRNGAAESY ACRFTETARL
    210 220 230 240 250
    RQERAIGRPV FPKAIGELHG HSGIARLALF YARAACGLVD PSAGTGVANA
    260 270 280 290 300
    GLVYFNGRLL AMSEDDLPYH VRVADDGDLE TVGRYDFDGQ LGCAMIAHPK
    310 320 330 340 350
    LDPATGELHA LSYDVIKRPY LKYFYFRPDG TKSDDVEIPL EQPTMIHDFA
    360 370 380 390 400
    ITENLVVVPD HQVVFKLQEM LRGGSPVVLD KEKTSRFGVL PKHAADASEM
    410 420 430 440 450
    AWVDVPDCFC FHLWNAWEDE ATGEVVVIGS CMTPADSIFN ESDERLESVL
    460 470 480 490 500
    TEIRLDARTG RSTRRAVLPP SQQVNLEVGM VNRNLLGRET RYAYLAVAEP
    510 520 530 540 550
    WPKVSGFAKV DLSTGELTKF EYGEGRFGGE PCFVPMDPAA AHPRGEDDGY
    560 570 580 590 600
    VLTFVHDERA GTSELLVVNA ADMRLEATVQ LPSRVPFGFH GTFITGQELE

    AQAA
    Length:604
    Mass (Da):65,495
    Last modified:September 22, 2009 - v2
    Checksum:i710FDF61BD0F5BD5
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U95953 mRNA. Translation: AAB62181.2.
    PIRiT04351.
    RefSeqiNP_001105902.2. NM_001112432.2.
    UniGeneiZm.463.

    Genome annotation databases

    GeneIDi732819.
    KEGGizma:732819.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U95953 mRNA. Translation: AAB62181.2.
    PIRiT04351.
    RefSeqiNP_001105902.2. NM_001112432.2.
    UniGeneiZm.463.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NPEX-ray3.20A76-604[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi4577.GRMZM2G014392_P01.

    Proteomic databases

    PaxDbiO24592.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi732819.
    KEGGizma:732819.

    Organism-specific databases

    MaizeGDBi726071.

    Phylogenomic databases

    eggNOGiKOG1285. Eukaryota.
    COG3670. LUCA.
    HOGENOMiHOG000254836.
    KOiK09840.

    Enzyme and pathway databases

    BRENDAi1.13.11.51. 6752.

    Miscellaneous databases

    EvolutionaryTraceiO24592.

    Family and domain databases

    InterProiIPR004294. Carotenoid_Oase.
    [Graphical view]
    PANTHERiPTHR10543. PTHR10543. 1 hit.
    PfamiPF03055. RPE65. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiNCED1_MAIZE
    AccessioniPrimary (citable) accession number: O24592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: September 22, 2009
    Last modified: February 17, 2016
    This is version 74 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, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.