CRTC_RUBGE
ID CRTC_RUBGE Reviewed; 406 AA.
AC P95619;
DT 24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Acyclic carotenoid 1,2-hydratase;
DE EC=4.2.1.131 {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
DE AltName: Full=1-hydroxyneurosporene hydratase;
DE AltName: Full=Hydroxylycopene hydratase;
DE AltName: Full=Hydroxyneurosporene synthase;
DE AltName: Full=Lycopene hydratase;
DE AltName: Full=Neurosporene hydratase;
GN Name=crtC;
OS Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas
OS gelatinosa).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Rubrivivax.
OX NCBI_TaxID=28068;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=8879238; DOI=10.1007/bf02173002;
RA Ouchane S., Picaud M., Reiss-Husson F., Vernotte C., Astier C.;
RT "Development of gene transfer methods for Rubrivivax gelatinosus S1:
RT construction, characterization and complementation of a puf operon deletion
RT strain.";
RL Mol. Gen. Genet. 252:379-385(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=9303322; DOI=10.1093/emboj/16.15.4777;
RA Ouchane S., Picaud M., Vernotte C., Astier C.;
RT "Photooxidative stress stimulates illegitimate recombination and mutability
RT in carotenoid-less mutants of Rubrivivax gelatinosus.";
RL EMBO J. 16:4777-4787(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=8999844; DOI=10.1074/jbc.272.3.1670;
RA Ouchane S., Picaud M., Vernotte C., Reiss-Husson F., Astier C.;
RT "Pleiotropic effects of puf interposon mutagenesis on carotenoid
RT biosynthesis in Rubrivivax gelatinosus. A new gene organization in purple
RT bacteria.";
RL J. Biol. Chem. 272:1670-1676(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=11790744; DOI=10.1128/jb.184.3.746-753.2002;
RA Pinta V., Picaud M., Reiss-Husson F., Astier C.;
RT "Rubrivivax gelatinosus acsF (previously orf358) codes for a conserved,
RT putative binuclear-iron-cluster-containing protein involved in aerobic
RT oxidative cyclization of Mg-protoporphyrin IX monomethylester.";
RL J. Bacteriol. 184:746-753(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1;
RX PubMed=12664193; DOI=10.1007/s00203-003-0538-3;
RA Pinta V., Ouchane S., Picaud M., Takaichi S., Astier C., Reiss-Husson F.;
RT "Characterization of unusual hydroxy- and ketocarotenoids in Rubrivivax
RT gelatinosus: involvement of enzyme CrtF or CrtA.";
RL Arch. Microbiol. 179:354-362(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND SUBSTRATE SPECIFICITY.
RC STRAIN=S1;
RX PubMed=12745254; DOI=10.1016/s0003-9861(03)00099-7;
RA Steiger S., Mazet A., Sandmann G.;
RT "Heterologous expression, purification, and enzymatic characterization of
RT the acyclic carotenoid 1,2-hydratase from Rubrivivax gelatinosus.";
RL Arch. Biochem. Biophys. 414:51-58(2003).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=21590288; DOI=10.1007/s00253-011-3324-1;
RA Hiseni A., Arends I.W., Otten L.G.;
RT "Biochemical characterization of the carotenoid 1,2-hydratases (CrtC) from
RT Rubrivivax gelatinosus and Thiocapsa roseopersicina.";
RL Appl. Microbiol. Biotechnol. 91:1029-1036(2011).
CC -!- FUNCTION: Involved in the biosynthesis of carotenoids spheroidene and
CC spirilloxanthin. Catalyzes the hydration of neurosporene to the
CC corresponding hydroxylated carotenoids 1-HO-neurosporene and 1,1'-
CC (HO)2-neurosporene and that of lycopene to 1-HO-lycopene and 1,1'-
CC (HO)2-lycopene. Can also act on demethylspheroidene, spheroidene, 1-HO-
CC 3,4-didehydrolycopene and geranylgeraniol.
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=rhodopin = all-trans-lycopene + H2O; Xref=Rhea:RHEA:31607,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15948, ChEBI:CHEBI:35331;
CC EC=4.2.1.131; Evidence={ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1'-dihydroxy-1,1',2,2'-tetrahydrolycopene = H2O + rhodopin;
CC Xref=Rhea:RHEA:31611, ChEBI:CHEBI:15377, ChEBI:CHEBI:35331,
CC ChEBI:CHEBI:63065; EC=4.2.1.131;
CC Evidence={ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hydroxy-all-trans-1,2-dihydro-neurosporene = all-trans-
CC neurosporene + H2O; Xref=Rhea:RHEA:54220, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16833, ChEBI:CHEBI:138077; EC=4.2.1.131;
CC Evidence={ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1'-dihydroxy-1,1',2,2'-tetrahydroneurosporene = 1-hydroxy-
CC all-trans-1,2-dihydro-neurosporene + H2O; Xref=Rhea:RHEA:54148,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:138076, ChEBI:CHEBI:138077;
CC EC=4.2.1.131; Evidence={ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.8 uM for spheroidene (at pH 8 and at 28 degrees Celsius)
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC KM=24.7 uM for lycopene (at pH 8 and at 28 degrees Celsius)
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC KM=26.9 uM for lycopene (at pH 8 and at 28 degrees Celsius)
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC KM=36.8 uM for 1-HO-neurosporene (at pH 8 and at 28 degrees Celsius)
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC KM=38.5 uM for neurosporene (at pH 8 and at 28 degrees Celsius)
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC Vmax=0.32 nmol/h/mg enzyme with lycopene as substrate (at pH 8 and at
CC 28 degrees Celsius) {ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC Vmax=0.54 nmol/h/mg enzyme with lycopene as substrate (at pH 8 and at
CC 28 degrees Celsius) {ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC Vmax=0.78 nmol/h/mg enzyme with 1-HO-neurosporene as substrate (at pH
CC 8 and at 28 degrees Celsius) {ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC Vmax=2.73 nmol/h/mg enzyme with neurosporene as substrate (at pH 8
CC and at 28 degrees Celsius) {ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC Vmax=4.92 nmol/h/mg enzyme with spheroidene as substrate (at pH 8 and
CC at 28 degrees Celsius) {ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC pH dependence:
CC Optimum pH is 8. No activity is detected at pH 4.0-5.0. At higher pH
CC values, it shows rapid decrease in activity, although 50% of the
CC relative activity is still detected at pH 9.0. It retains much
CC residual activity after 30 minutes incubation at pH 4.0-8.0,
CC indicating that CrtC is stable in both slightly alkaline and acid
CC environments. {ECO:0000269|PubMed:12745254,
CC ECO:0000269|PubMed:21590288};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Enzyme activity is
CC significantly lower at 20 degrees Celsius and 40 degrees Celsius.
CC {ECO:0000269|PubMed:12745254, ECO:0000269|PubMed:21590288};
CC -!- PATHWAY: Carotenoid biosynthesis; spheroidene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12745254}.
CC -!- SIMILARITY: Belongs to the CrtC hydratase family. {ECO:0000305}.
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DR EMBL; AY234384; AAO93124.1; -; Genomic_DNA.
DR AlphaFoldDB; P95619; -.
DR SMR; P95619; -.
DR BioCyc; MetaCyc:MON-15841; -.
DR BRENDA; 4.2.1.131; 5401.
DR SABIO-RK; P95619; -.
DR UniPathway; UPA00683; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0016116; P:carotenoid metabolic process; IDA:UniProtKB.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:1901180; P:spheroidene biosynthetic process; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Cell membrane; Chlorophyll biosynthesis; Lyase;
KW Membrane; Photosynthesis.
FT CHAIN 1..406
FT /note="Acyclic carotenoid 1,2-hydratase"
FT /id="PRO_0000422997"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 44592 MW; 0CBDA1B64E549D38 CRC64;
MRAAESGADA RVRPVDRVEP ADAPAGDAGG LRAAVPGDGG SAVRPGDARL DVLVPPGLVD
EPAAGALPGG GQRAPGAGRA DGGDVRPVGG RDADGAPRFD QPVPPGGYLW WYVDAVSDDG
RHGLTFIAFV GSVFSPYYAW AGGPKADRAD PENHCALNIA LYGDAGKRWT MTERGRRWMR
RSRDEFVIGP SRLHWDGESL LVEFDEVGVP IPRRVKGRVR VWPKALCRFV TSLDSGGRHR
WGPIAPCSRI EVELDSPRVR WSGHAYLDSN EGDEPIDRPF REWDWSRATM ADSSTAVIYD
VRQKRDGDRV IAERFLLDGS TESFEAPPRQ PLPTTLWRIG RTMRTEPGVP ALVEQTLEDT
PFYARSMVRS GLLGEVVTSV HETMLLPRVI TLPVRLMLPW RMPRRA
