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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)DescriptionActionsGraphical viewLength
Metal bindingi307Magnesium 11
Metal bindingi307Magnesium 2Curated1
Metal bindingi311Magnesium 11
Metal bindingi311Magnesium 2Curated1
Metal bindingi451Magnesium 31
Metal bindingi455Magnesium 31

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)DescriptionActionsGraphical viewLength
Mutagenesisi307D → A: Strongly reduced activity. 1 Publication1
Mutagenesisi308D → A: Reduces affinity for substrate about 12-fold. 1
Mutagenesisi311D → A: Strongly reduced activity. 1 Publication1
Mutagenesisi451D → A: No effect. 1 Publication1
Mutagenesisi452D → A: No effect. 1 Publication1
Mutagenesisi455E → A: Strongly reduced activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001864391 – 554(+)-delta-cadinene synthase isozyme XC1Add BLAST554

Proteomic databases

PRIDEiQ39761.

Structurei

Secondary structure

1554
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni31 – 37Combined sources7
Helixi46 – 64Combined sources19
Helixi70 – 82Combined sources13
Helixi86 – 88Combined sources3
Helixi90 – 102Combined sources13
Helixi111 – 123Combined sources13
Helixi130 – 136Combined sources7
Beta strandi141 – 143Combined sources3
Helixi145 – 149Combined sources5
Helixi151 – 161Combined sources11
Helixi169 – 185Combined sources17
Helixi186 – 188Combined sources3
Helixi193 – 202Combined sources10
Turni205 – 207Combined sources3
Helixi210 – 222Combined sources13
Helixi229 – 260Combined sources32
Helixi262 – 265Combined sources4
Helixi273 – 283Combined sources11
Helixi287 – 289Combined sources3
Helixi290 – 310Combined sources21
Helixi316 – 328Combined sources13
Helixi331 – 336Combined sources6
Helixi339 – 341Combined sources3
Helixi342 – 359Combined sources18
Helixi360 – 362Combined sources3
Helixi366 – 390Combined sources25
Helixi397 – 404Combined sources8
Helixi405 – 407Combined sources3
Helixi410 – 419Combined sources10
Helixi427 – 434Combined sources8
Helixi438 – 456Combined sources19
Helixi468 – 476Combined sources9
Helixi480 – 502Combined sources23
Beta strandi503 – 505Combined sources3
Helixi510 – 526Combined sources17
Helixi538 – 548Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G4DX-ray2.40A/B1-554[»]
3G4FX-ray2.65A/B1-554[»]
ProteinModelPortaliQ39761.
SMRiQ39761.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ39761.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi307 – 311DDXXD motif5

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3G4DX-ray2.40A/B1-554[»]
3G4FX-ray2.65A/B1-554[»]
ProteinModelPortaliQ39761.
SMRiQ39761.
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 2, 2016
This is version 85 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.