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Protein

Acyclic carotenoid 1,2-hydratase

Gene

crtC

Organism
Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas gelatinosa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of carotenoids spheroidene and spirilloxanthin. Catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and 1,1'-(HO)2-neurosporene and that of lycopene to 1-HO-lycopene and 1,1'-(HO)2-lycopene. Can also act on demethylspheroidene, spheroidene, 1-HO-3,4-didehydrolycopene and geranylgeraniol.2 Publications

Catalytic activityi

1-hydroxy-1,2-dihydrolycopene = lycopene + H2O.2 Publications
1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene = 1-hydroxy-1,2-dihydrolycopene + H2O.2 Publications
1-hydroxy-1,2-dihydroneurosporene = neurosporene + H2O.2 Publications
1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene = 1-hydroxy-1,2-dihydroneurosporene + H2O.2 Publications

Kineticsi

  1. KM=7.8 µM for spheroidene (at pH 8 and at 28 degrees Celsius)2 Publications
  2. KM=24.7 µM for lycopene (at pH 8 and at 28 degrees Celsius)2 Publications
  3. KM=26.9 µM for lycopene (at pH 8 and at 28 degrees Celsius)2 Publications
  4. KM=36.8 µM for 1-HO-neurosporene (at pH 8 and at 28 degrees Celsius)2 Publications
  5. KM=38.5 µM for neurosporene (at pH 8 and at 28 degrees Celsius)2 Publications
  1. Vmax=0.32 nmol/h/mg enzyme with lycopene as substrate (at pH 8 and at 28 degrees Celsius)2 Publications
  2. Vmax=0.54 nmol/h/mg enzyme with lycopene as substrate (at pH 8 and at 28 degrees Celsius)2 Publications
  3. Vmax=0.78 nmol/h/mg enzyme with 1-HO-neurosporene as substrate (at pH 8 and at 28 degrees Celsius)2 Publications
  4. Vmax=2.73 nmol/h/mg enzyme with neurosporene as substrate (at pH 8 and at 28 degrees Celsius)2 Publications
  5. Vmax=4.92 nmol/h/mg enzyme with spheroidene as substrate (at pH 8 and at 28 degrees Celsius)2 Publications

pH dependencei

Optimum pH is 8. No activity is detected at pH 4.0-5.0. At higher pH values, it shows rapid decrease in activity, although 50% of the relative activity is still detected at pH 9.0. It retains much residual activity after 30 minutes incubation at pH 4.0-8.0, indicating that CrtC is stable in both slightly alkaline and acid environments.2 Publications

Temperature dependencei

Optimum temperature is 30 degrees Celsius. Enzyme activity is significantly lower at 20 degrees Celsius and 40 degrees Celsius.2 Publications

Pathwayi: spheroidene biosynthesis

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

GO - Molecular functioni

  • hydro-lyase activity Source: UniProtKB

GO - Biological processi

  • carotenoid metabolic process Source: UniProtKB
  • chlorophyll biosynthetic process Source: UniProtKB-KW
  • photosynthesis Source: UniProtKB-KW
  • spheroidene biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionLyase
Biological processCarotenoid biosynthesis, Chlorophyll biosynthesis, Photosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15841.
UniPathwayiUPA00683.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyclic carotenoid 1,2-hydratase (EC:4.2.1.1312 Publications)
Alternative name(s):
1-hydroxyneurosporene hydratase
Hydroxylycopene hydratase
Hydroxyneurosporene synthase
Lycopene hydratase
Neurosporene hydratase
Gene namesi
Name:crtC
OrganismiRubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas gelatinosa)
Taxonomic identifieri28068 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesRubrivivax

Subcellular locationi

P95619:
  • Cell membrane 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004229971 – 406Acyclic carotenoid 1,2-hydrataseAdd BLAST406

Structurei

3D structure databases

ProteinModelPortaliP95619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CrtC hydratase family.Curated

Sequencei

Sequence statusi: Complete.

P95619-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAAESGADA RVRPVDRVEP ADAPAGDAGG LRAAVPGDGG SAVRPGDARL
60 70 80 90 100
DVLVPPGLVD EPAAGALPGG GQRAPGAGRA DGGDVRPVGG RDADGAPRFD
110 120 130 140 150
QPVPPGGYLW WYVDAVSDDG RHGLTFIAFV GSVFSPYYAW AGGPKADRAD
160 170 180 190 200
PENHCALNIA LYGDAGKRWT MTERGRRWMR RSRDEFVIGP SRLHWDGESL
210 220 230 240 250
LVEFDEVGVP IPRRVKGRVR VWPKALCRFV TSLDSGGRHR WGPIAPCSRI
260 270 280 290 300
EVELDSPRVR WSGHAYLDSN EGDEPIDRPF REWDWSRATM ADSSTAVIYD
310 320 330 340 350
VRQKRDGDRV IAERFLLDGS TESFEAPPRQ PLPTTLWRIG RTMRTEPGVP
360 370 380 390 400
ALVEQTLEDT PFYARSMVRS GLLGEVVTSV HETMLLPRVI TLPVRLMLPW

RMPRRA
Length:406
Mass (Da):44,592
Last modified:May 1, 1997 - v1
Checksum:i0CBDA1B64E549D38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY234384 Genomic DNA. Translation: AAO93124.1.

Similar proteinsi

Entry informationi

Entry nameiCRTC_RUBGE
AccessioniPrimary (citable) accession number: P95619
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 24, 2013
Last sequence update: May 1, 1997
Last modified: March 15, 2017
This is version 56 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families