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CRTY_HALSA
ID   CRTY_HALSA              Reviewed;         237 AA.
AC   Q9HNE5;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   31-MAY-2011, sequence version 2.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Lycopene beta-cyclase {ECO:0000303|PubMed:12003928};
DE            EC=5.5.1.19 {ECO:0000250|UniProtKB:B0R753};
GN   Name=crtY {ECO:0000303|PubMed:12003928}; OrderedLocusNames=VNG_2137G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN   [2]
RP   IDENTIFICATION.
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=12003928; DOI=10.1128/jb.184.11.2889-2897.2002;
RA   Peck R.F., Johnson E.A., Krebs M.P.;
RT   "Identification of a lycopene beta-cyclase required for bacteriorhodopsin
RT   biogenesis in the archaeon Halobacterium salinarum.";
RL   J. Bacteriol. 184:2889-2897(2002).
CC   -!- FUNCTION: Catalyzes the cyclization of both ends of lycopene to form
CC       beta-carotene, a retinal precursor. Is required for bacteriorhodopsin
CC       biogenesis, a light-driven proton pump with a covalently bound retinal
CC       cofactor. {ECO:0000250|UniProtKB:B0R753}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a carotenoid psi-end group = a carotenoid beta-end derivative;
CC         Xref=Rhea:RHEA:55620, ChEBI:CHEBI:139114, ChEBI:CHEBI:139120;
CC         EC=5.5.1.19; Evidence={ECO:0000250|UniProtKB:B0R753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55621;
CC         Evidence={ECO:0000250|UniProtKB:B0R753};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-lycopene = gamma-carotene; Xref=Rhea:RHEA:32219,
CC         ChEBI:CHEBI:15948, ChEBI:CHEBI:27740; EC=5.5.1.19;
CC         Evidence={ECO:0000250|UniProtKB:B0R753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32220;
CC         Evidence={ECO:0000250|UniProtKB:B0R753};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=gamma-carotene = all-trans-beta-carotene;
CC         Xref=Rhea:RHEA:32239, ChEBI:CHEBI:17579, ChEBI:CHEBI:27740;
CC         EC=5.5.1.19; Evidence={ECO:0000250|UniProtKB:B0R753};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32240;
CC         Evidence={ECO:0000250|UniProtKB:B0R753};
CC   -!- PATHWAY: Carotenoid biosynthesis; beta-carotene biosynthesis.
CC       {ECO:0000250|UniProtKB:B0R753}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:B0R753};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the lycopene beta-cyclase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG20275.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE004437; AAG20275.1; ALT_INIT; Genomic_DNA.
DR   PIR; G84363; G84363.
DR   RefSeq; WP_012289440.1; NC_002607.1.
DR   AlphaFoldDB; Q9HNE5; -.
DR   STRING; 64091.VNG_2137G; -.
DR   PaxDb; Q9HNE5; -.
DR   EnsemblBacteria; AAG20275; AAG20275; VNG_2137G.
DR   GeneID; 5953587; -.
DR   KEGG; hal:VNG_2137G; -.
DR   PATRIC; fig|64091.14.peg.1634; -.
DR   HOGENOM; CLU_1631607_0_0_2; -.
DR   InParanoid; Q9HNE5; -.
DR   OrthoDB; 90912at2157; -.
DR   PhylomeDB; Q9HNE5; -.
DR   UniPathway; UPA00802; -.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016767; F:geranylgeranyl-diphosphate geranylgeranyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR   GO; GO:0045436; F:lycopene beta cyclase activity; IEA:RHEA.
DR   GO; GO:0016120; P:carotene biosynthetic process; IEA:UniProt.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR017825; Lycopene_cyclase_dom.
DR   Pfam; PF18916; Lycopene_cyc; 2.
DR   TIGRFAMs; TIGR03462; CarR_dom_SF; 2.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis; Cell membrane; Isomerase; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..237
FT                   /note="Lycopene beta-cyclase"
FT                   /id="PRO_0000408501"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   237 AA;  25822 MW;  66A9A770C9BEF601 CRC64;
     MTTSYLTFLA VAVGPPLVAL GVVRAARWDG DRARAAGVGI LLALALSYTT PWDNYLIATG
     VWWYGEGTVV GRLWQMPIEE YLFVITQTLL TGLWVQALPL RPTAGFSPTR RDAVLGALAG
     VLVGCGGAVL LTVDATFYIG AIIAWAAPVL ALQWAVGWRY LWRRRRVFAA AVLVPTLFLS
     AADRYAIADG IWILAGQYTT GITVLGLPIE EGAFFFVTNV FVSQGLILYA WVLARWR
 
 
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