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Protein

(+)-delta-cadinene synthase isozyme XC1

Gene
N/A
Organism
Gossypium arboreum (Tree cotton) (Gossypium nanking)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for the cyclization of trans,trans-farnesyl diphosphate (FPP) to (+)-delta cadinene.1 Publication

Catalytic activityi

(2E,6E)-farnesyl diphosphate = (+)-delta-cadinene + diphosphate.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 3 Mg2+ ions per subunit.1 Publication

Pathwayi: terpenoid biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi307 – 3071Magnesium 1
Metal bindingi307 – 3071Magnesium 2Curated
Metal bindingi311 – 3111Magnesium 1
Metal bindingi311 – 3111Magnesium 2Curated
Metal bindingi451 – 4511Magnesium 3
Metal bindingi455 – 4551Magnesium 3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi4.2.3.13. 2497.
UniPathwayiUPA00213.

Names & Taxonomyi

Protein namesi
Recommended name:
(+)-delta-cadinene synthase isozyme XC1 (EC:4.2.3.13)
Short name:
D-cadinene synthase XC1
OrganismiGossypium arboreum (Tree cotton) (Gossypium nanking)
Taxonomic identifieri29729 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsMalvalesMalvaceaeMalvoideaeGossypium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071D → A: Strongly reduced activity. 1 Publication
Mutagenesisi308 – 3081D → A: Reduces affinity for substrate about 12-fold.
Mutagenesisi311 – 3111D → A: Strongly reduced activity. 1 Publication
Mutagenesisi451 – 4511D → A: No effect. 1 Publication
Mutagenesisi452 – 4521D → A: No effect. 1 Publication
Mutagenesisi455 – 4551E → A: Strongly reduced activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 554554(+)-delta-cadinene synthase isozyme XC1PRO_0000186439Add
BLAST

Proteomic databases

PRIDEiQ39761.

Structurei

Secondary structure

1
554
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni31 – 377Combined sources
Helixi46 – 6419Combined sources
Helixi70 – 8213Combined sources
Helixi86 – 883Combined sources
Helixi90 – 10213Combined sources
Helixi111 – 12313Combined sources
Helixi130 – 1367Combined sources
Beta strandi141 – 1433Combined sources
Helixi145 – 1495Combined sources
Helixi151 – 16111Combined sources
Helixi169 – 18517Combined sources
Helixi186 – 1883Combined sources
Helixi193 – 20210Combined sources
Turni205 – 2073Combined sources
Helixi210 – 22213Combined sources
Helixi229 – 26032Combined sources
Helixi262 – 2654Combined sources
Helixi273 – 28311Combined sources
Helixi287 – 2893Combined sources
Helixi290 – 31021Combined sources
Helixi316 – 32813Combined sources
Helixi331 – 3366Combined sources
Helixi339 – 3413Combined sources
Helixi342 – 35918Combined sources
Helixi360 – 3623Combined sources
Helixi366 – 39025Combined sources
Helixi397 – 4048Combined sources
Helixi405 – 4073Combined sources
Helixi410 – 41910Combined sources
Helixi427 – 4348Combined sources
Helixi438 – 45619Combined sources
Helixi468 – 4769Combined sources
Helixi480 – 50223Combined sources
Beta strandi503 – 5053Combined sources
Helixi510 – 52617Combined sources
Helixi538 – 54811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G4DX-ray2.40A/B1-554[»]
3G4FX-ray2.65A/B1-554[»]
ProteinModelPortaliQ39761.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ39761.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi307 – 3115DDXXD motif

Domaini

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

Sequence similaritiesi

Belongs to the terpene synthase family.Curated

Phylogenomic databases

KOiK14183.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.

Sequencei

Sequence statusi: Complete.

Q39761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASQVSQMPS SSPLSSNKDE MRPKADFQPS IWGDLFLNCP DKNIDAETEK
60 70 80 90 100
RHQQLKEEVR KMIVAPMANS TQKLAFIDSV QRLGVSYHFT KEIEDELENI
110 120 130 140 150
YHNNNDAEND LYTTSIRFRL LREHGYNVSC DVFNKFKDEQ GNFKSSVTSD
160 170 180 190 200
VRGLLELYQA SYLRVHGEDI LDEAISFTTH HLSLAVASLD HPLSEEVSHA
210 220 230 240 250
LKQSIRRGLP RVEARHYLSV YQDIESHNKA LLEFAKIDFN MLQFLHRKEL
260 270 280 290 300
SEICRWWKDL DFQRKLPYAR DRVVEGYFWI SGVYFEPQYS LGRKMLTKVI
310 320 330 340 350
AMASIVDDTY DSYATYEELI PYTNAIERWD IKCIDEIPEY MKPSYKALLD
360 370 380 390 400
VYEEMVQLVA EHGRQYRVEY AKNAMIRLAQ SYLVEAKWTL QNYKPSFEEF
410 420 430 440 450
KANALPTCGY AMLAITSFVG MGDIVTPETF KWAASDPKII QASTIICRFM
460 470 480 490 500
DDVAEHKFKH RREDDCSAIE CYMEEYGVTA QEAYDVFNKH VESAWKDLNQ
510 520 530 540 550
EFLKPTEMPT EVLNRSLNLA RVMDVLYREG DGYTYVGKAA KGGITSLLIE

PIAL
Length:554
Mass (Da):64,138
Last modified:November 1, 1996 - v1
Checksum:i59D6922DEDF9DCAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23206 mRNA. Translation: AAA93064.1.
PIRiS68365.

Genome annotation databases

KEGGiag:AAA93064.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23206 mRNA. Translation: AAA93064.1.
PIRiS68365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G4DX-ray2.40A/B1-554[»]
3G4FX-ray2.65A/B1-554[»]
ProteinModelPortaliQ39761.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ39761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA93064.

Phylogenomic databases

KOiK14183.

Enzyme and pathway databases

UniPathwayiUPA00213.
BRENDAi4.2.3.13. 2497.

Miscellaneous databases

EvolutionaryTraceiQ39761.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCS1_GOSAR
AccessioniPrimary (citable) accession number: Q39761
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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

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.