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Protein

Zeaxanthin epoxidase, chloroplastic

Gene
N/A
Organism
Prunus armeniaca (Apricot) (Armeniaca vulgaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Involved in the epoxidation of zeaxanthin (By similarity).By similarity

Catalytic activityi

Zeaxanthin + 2 NAD(P)H + 2 O2 = violaxanthin + 2 NAD(P)+ + 2 H2O.

Cofactori

FADCurated

Pathwayi: abscisate biosynthesis

This protein is involved in the pathway abscisate biosynthesis, which is part of Plant hormone biosynthesis.
View all proteins of this organism that are known to be involved in the pathway abscisate biosynthesis and in Plant hormone biosynthesis.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi82 – 110FADSequence analysisAdd BLAST29
Nucleotide bindingi360 – 373FADSequence analysisAdd BLAST14

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Abscisic acid biosynthesis

Keywords - Ligandi

FAD, Flavoprotein, NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00090.

Names & Taxonomyi

Protein namesi
Recommended name:
Zeaxanthin epoxidase, chloroplastic (EC:1.14.13.90)
Alternative name(s):
PA-ZE
OrganismiPrunus armeniaca (Apricot) (Armeniaca vulgaris)
Taxonomic identifieri36596 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 50ChloroplastSequence analysisAdd BLAST50
ChainiPRO_000002061251 – 661Zeaxanthin epoxidase, chloroplasticAdd BLAST611

Proteomic databases

PRIDEiO81360.

Structurei

3D structure databases

ProteinModelPortaliO81360.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini558 – 607FHAPROSITE-ProRule annotationAdd BLAST50

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR017079. Zeaxanthin_epoxidase.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view]
PIRSFiPIRSF036989. Zeaxanthin_epoxidase. 1 hit.
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF51905. SSF51905. 2 hits.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O81360-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTLFYNSM NLSAAVFSRT HFPIPINKDF PLEFSPCIHT DYHLRSRTRS
60 70 80 90 100
GQKKCLTEVR ATVASPTEVP SAPASTQPKK LRILVAGGGI GGLVFALAAK
110 120 130 140 150
KKGFDVVVFE KDLSAVRGEG QYRGPIQIQS NALAALEAID MDVAEEVMRV
160 170 180 190 200
GCVTGDRING LVDGVSGTWY VKFDTFTPAV ERGLPVTRVI SRIALQQILA
210 220 230 240 250
RAVGEEIIIN DSNVVNFEDL GDKVNVILEN GQRYEGDMLV GADGIWSKVR
260 270 280 290 300
KNLFGLNEAV YSGYTCYTGI ADFVPADINS VGYRVFLGHK QYFVSSDVGG
310 320 330 340 350
GKMQWYAFHK ESPGGVDSPN GKKERLLKIF EGWCDNVIDL LLATEEDAIL
360 370 380 390 400
RRDIYDRTPI LTWGKGHVTL LGDSVHAMQP NMGQGGCMAI EDGYQLALEL
410 420 430 440 450
DKAWKKSSET GTPVDVASSL RSYENSRRLR VAIIHGMARM AALMASTYKA
460 470 480 490 500
YLGVGLGPLS FLTKFRIPHP GRVGGRVFID KAMPLMLSWV LGGNSSKLEG
510 520 530 540 550
RSPSCRLSDK ASDQLRNWFE DDDALERAID GEWYLIPCGQ DNDASQLICL
560 570 580 590 600
NRDEKNPCII GSAPHGDVSG ISIAIPKPQV SEMHARISYK DGAFYLTDLR
610 620 630 640 650
SEHGTWIADI EGKRYRVPPN FPARFRPSDA IEIGSQKVAF RVKVMKSSPG
660
SVEKEGILQA A
Length:661
Mass (Da):72,483
Last modified:November 1, 1998 - v1
Checksum:iF04716677474070A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071888 mRNA. Translation: AAC24582.1.
AF159948 mRNA. Translation: AAD42899.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF071888 mRNA. Translation: AAC24582.1.
AF159948 mRNA. Translation: AAD42899.1.

3D structure databases

ProteinModelPortaliO81360.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO81360.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00090.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
3.50.50.60. 3 hits.
InterProiIPR002938. FAD-bd.
IPR023753. FAD/NAD-binding_dom.
IPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
IPR017079. Zeaxanthin_epoxidase.
[Graphical view]
PfamiPF01494. FAD_binding_3. 1 hit.
PF00498. FHA. 1 hit.
[Graphical view]
PIRSFiPIRSF036989. Zeaxanthin_epoxidase. 1 hit.
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF51905. SSF51905. 2 hits.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiABA2_PRUAR
AccessioniPrimary (citable) accession number: O81360
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.