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