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O04408

- KSA_PEA

UniProt

O04408 - KSA_PEA

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Protein

Ent-copalyl diphosphate synthase, chloroplastic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalyzes the conversion of geranylgeranyl diphosphate to the gibberellin precursor ent-copalyl diphosphate.

Catalytic activityi

Geranylgeranyl diphosphate = ent-copalyl diphosphate.

Cofactori

Magnesium.Curated

Pathwayi

GO - Molecular functioni

  1. ent-copalyl diphosphate synthase activity Source: UniProtKB-EC
  2. magnesium ion binding Source: InterPro
  3. terpene synthase activity Source: InterPro

GO - Biological processi

  1. gibberellin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00390.

Names & Taxonomyi

Protein namesi
Recommended name:
Ent-copalyl diphosphate synthase, chloroplastic (EC:5.5.1.13)
Short name:
Ent-CDP synthase
Alternative name(s):
Ent-copalyl diphosphate synthase
Ent-kaurene synthase A
Short name:
KSA
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

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
Chaini? – 801Ent-copalyl diphosphate synthase, chloroplasticPRO_0000033624
Transit peptidei1 – ?ChloroplastSequence Analysis

Structurei

3D structure databases

ProteinModelPortaliO04408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi373 – 3764DXDD motif

Domaini

The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity, presumably through binding to Mg2+.

Sequence similaritiesi

Belongs to the terpene synthase family.Curated

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
1.50.10.20. 1 hit.
1.50.30.10. 1 hit.
InterProiIPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamiPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 2 hits.
SSF48576. SSF48576. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O04408-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFTHFSTHFH LPSSSSLFFL HPFYKSSSLG AVSFVAKDKE KRCRAISKSR
60 70 80 90 100
TQEYEGVFQT NVATLKLSEI NVEDVIVIDD EEEQDIRVGL VNKIKSILSS
110 120 130 140 150
LEDGEITISA YDTAWVALVE DVNAISTPQF PSSLEWIAKN QLQDGSWGDS
160 170 180 190 200
RLFSAHDRII NTLACVIALR SWNMHSEKCD KGMIFFRENL SKLENENEEH
210 220 230 240 250
MPIGFEVAFP SLLEGARGIK PLMCPNDSPI LKNIFEKRDE KLTRIPKEIM
260 270 280 290 300
HKVPTTLLHS LEGMSGLDWK QLLKLQSQDG SFLFSPSSTA FALMQTKDGN
310 320 330 340 350
CLKYLNNVVK KFNGGVPNVY PVDLFEHIWV VDRLERLGIS RFFRHEIKDC
360 370 380 390 400
MNYVSKIWSE KGICWARNSN VQDIDDTAMA FRLLRLHGHQ VSAHVFKHFE
410 420 430 440 450
RNGEFFCFAG QCTQAVTGMY NLFRASQVLF PGEKILEHAK HFSAKVLKEK
460 470 480 490 500
REANELIDKW IIMKNLPEEV GYALDMPWYA NLDRIETRFY IDQYGAESDV
510 520 530 540 550
WIGKTLYRMA YVNNNNYLEL AKLDYNNCQA QHLIEWNVIQ TWYLESRLGE
560 570 580 590 600
FGLSKRDLLL AYFLATGSIF EPERSHERLA WAKTTALLET IKCYVRNEDL
610 620 630 640 650
RKDFAKKFND HIDVRDYSIA RRMKRNKTEH ELVESLFATI GEISWDVRLS
660 670 680 690 700
YGHEIGYDMH QCWKKWLSSW QSEGDKCEGE AELLIQIINL CSNHWISEGP
710 720 730 740 750
SMQSTIQHLL QLTNSICHKL SCYQKDKELK GISCQENITN SEVESKMQEL
760 770 780 790 800
VQMVFQKCPN DIDFNVKNTF FTIAKSFYYA AFCDSRTINF HIAKVLFEKV

V
Length:801
Mass (Da):92,718
Last modified:July 1, 1997 - v1
Checksum:i5CB88ADE00366844
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U63652 mRNA. Translation: AAB58822.1.
PIRiT06783.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U63652 mRNA. Translation: AAB58822.1 .
PIRi T06783.

3D structure databases

ProteinModelPortali O04408.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00390 .

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
1.50.10.20. 1 hit.
1.50.30.10. 1 hit.
InterProi IPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 2 hits.
SSF48576. SSF48576. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The LS locus of pea encodes the gibberellin biosynthesis enzyme ent-kaurene synthase A."
    Ait-Ali T., Swain S.M., Reid J.B., Sun T.-P., Kamiya Y.
    Plant J. 11:443-454(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiKSA_PEA
AccessioniPrimary (citable) accession number: O04408
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 74 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

External Data

Dasty 3