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CRTC_THIRO
ID   CRTC_THIRO              Reviewed;         405 AA.
AC   Q7X3G5;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Acyclic carotenoid 1,2-hydratase;
DE            EC=4.2.1.131;
DE   AltName: Full=Hydroxylycopene hydratase;
DE   AltName: Full=Lycopene hydratase;
GN   Name=crtC;
OS   Thiocapsa roseopersicina.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiocapsa.
OX   NCBI_TaxID=1058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC   STRAIN=BBS;
RX   PubMed=12788703; DOI=10.1128/aem.69.6.3093-3102.2003;
RA   Kovacs A.T., Rakhely G., Kovacs K.L.;
RT   "Genes involved in the biosynthesis of photosynthetic pigments in the
RT   purple sulfur photosynthetic bacterium Thiocapsa roseopersicina.";
RL   Appl. Environ. Microbiol. 69:3093-3102(2003).
RN   [2]
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 spirilloxanthin.
CC       Catalyzes the hydration of lycopene to the corresponding hydroxylated
CC       carotenoids 1-HO-lycopene and 1,1'-(HO)2-lycopene. Can also act on
CC       geranylgeraniol. {ECO:0000269|PubMed:12788703,
CC       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: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:21590288};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.8 uM for lycopene (at pH 8 and at 28 degrees Celsius)
CC         {ECO:0000269|PubMed:21590288};
CC         Vmax=0.15 nmol/h/mg enzyme with lycopene (at pH 8 and at 28 degrees
CC         Celsius) {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: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:21590288};
CC   -!- INDUCTION: Repressed by oxygen. {ECO:0000305|PubMed:12788703}.
CC   -!- SIMILARITY: Belongs to the CrtC hydratase family. {ECO:0000305}.
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DR   EMBL; AF528191; AAP59035.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7X3G5; -.
DR   STRING; 1058.SAMN05421783_11330; -.
DR   KEGG; ag:AAP59035; -.
DR   BRENDA; 4.2.1.131; 6357.
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; Chlorophyll biosynthesis; Lyase; Photosynthesis.
FT   CHAIN           1..405
FT                   /note="Acyclic carotenoid 1,2-hydratase"
FT                   /id="PRO_0000422998"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  44114 MW;  02B38D5BDFA515EE CRC64;
     MRAAGILTPG ALWAPGPSDT RDERRHDAGR LQPALPGDGR GPLRPGVTRM EGLLHASSVA
     QQGAGALSGR GERASGSRGT DGGHVGTPGG SDPARGPRFD LRITPGGYLW WYLDALSDDG
     DHGLTIIAML GSVFSPYYAW ARRRGNPDPL NHCALNVALY GKAGKRWTMT ERGRKALRQA
     PGRLDIGPSH LTWDGTALTI DVNEITAPIP SRVRGRIRVI PAAVNAREFT LDPAERHVWW
     PIAPISRVEV DLEKPALRWS GHGYLDSNRG EEPLEDAFQC WDWSRANTPS GTTMLYDVTA
     RHGTGASLAL RFNASGEVEE FPPPPRVRLP TTGIWRIKRG TQCEAGHQAR VVETLEDTPF
     YARSLVETRL AGETATCVHE SLSLDRFASP VVQLMLPFRM PRVGG
 
 
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