(data stored in ACNUC29543 zone)

SWISSPROT: A5GQL9_SYNR3

ID   A5GQL9_SYNR3            Unreviewed;       483 AA.
AC   A5GQL9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 65.
DE   RecName: Full=Zeta-carotene desaturase {ECO:0000256|RuleBase:RU362008};
DE            EC=1.3.5.6 {ECO:0000256|RuleBase:RU362008};
DE   AltName: Full=9,9'-di-cis-zeta-carotene desaturase {ECO:0000256|RuleBase:RU362008};
GN   Name=crtQ {ECO:0000313|EMBL:CAK27178.1};
GN   Synonyms=zds {ECO:0000313|EMBL:CAK27178.1};
GN   OrderedLocusNames=SynRCC307_0275 {ECO:0000313|EMBL:CAK27178.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK27178.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|EMBL:CAK27178.1, ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of zeta-carotene to lycopene
CC       via the intermediary of neurosporene. It carries out two
CC       consecutive desaturations (introduction of double bonds) at
CC       positions C-7 and C-7'. {ECO:0000256|RuleBase:RU362008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9,9'-di-cis-zeta-carotene + 2 a quinone = 7,7',9,9'-
CC         tetra-cis-lycopene + 2 a quinol; Xref=Rhea:RHEA:30955,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:48716, ChEBI:CHEBI:62466,
CC         ChEBI:CHEBI:132124; EC=1.3.5.6;
CC         Evidence={ECO:0000256|RuleBase:RU362008};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC       {ECO:0000256|RuleBase:RU362008}.
CC   -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC       {ECO:0000256|RuleBase:RU362008}.
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DR   EMBL; CT978603; CAK27178.1; -; Genomic_DNA.
DR   RefSeq; WP_011934693.1; NC_009482.1.
DR   STRING; 316278.SynRCC307_0275; -.
DR   EnsemblBacteria; CAK27178; CAK27178; SynRCC307_0275.
DR   KEGG; syr:SynRCC307_0275; -.
DR   eggNOG; ENOG4105CVN; Bacteria.
DR   eggNOG; COG3349; LUCA.
DR   HOGENOM; HOG000150110; -.
DR   KO; K00514; -.
DR   OMA; MLTIFMM; -.
DR   OrthoDB; 630753at2; -.
DR   BioCyc; SSP316278:G1GJL-272-MONOMER; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000001115; Chromosome.
DR   GO; GO:0052887; F:7,9,9'-tricis-neurosporene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052886; F:9,9'-dicis-carotene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016719; F:carotene 7,8-desaturase activity; IEA:InterPro.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR014103; Zeta_caro_desat.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02732; zeta_caro_desat; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GQL9.
DR   SWISS-2DPAGE; A5GQL9.
KW   Carotenoid biosynthesis {ECO:0000256|RuleBase:RU362008};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362008,
KW   ECO:0000313|EMBL:CAK27178.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT   DOMAIN       10    478       Amino_oxidase. {ECO:0000259|Pfam:
FT                                PF01593}.
SQ   SEQUENCE   483 AA;  53118 MW;  40118C91D8D349B6 CRC64;
     MRVAIVGSGL AGLSAAVDLV DAGHSVDLYE ARPFMGGKVG SWVDDGGNHI EMGLHVFFFN
     YTNLFALMRK VGAFDNLLPK DHTHLFVNEG GDLRELDFRF ALGAPFNGLK AFFTTPQLDW
     IDKLRNALAL GTSPIVRGLV DYEGAMRTIR ALDRISFSEW FLGHGGSPES IRRMWNPIAY
     ALGFIDCEAI SARCMLTIFM MFAARTEASK LNLLKGSPHR WLTGPIFDYI KARGGQLHLR
     HRVTAVHHKG DNGTTEVTGL TMGTPDGDVE VEADAYLAAC DVPGIQRLLP EEWRRFEQFD
     NIYKLEAVPV ATVQLRYDGW VTELGDQPQA AAARADVAHP AGLNNLLYTA DADFSCFADL
     ALASPEDYRK EGQGSLLQCV LTPGDPWIPR KTEEIVAHTD AQVRKLFPSS SGLKLVWSNV
     VKLAQSLYRE APGMEPYRPD QRTPVSNFFL AGSYTRQDYI DSMEGATMSG RLAAKAILNG
     AGG
//

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