ID   ZDS_SYNY3               Reviewed;         489 AA.
AC   P74306;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Zeta-carotene desaturase;
DE            EC=1.3.5.6;
DE   AltName: Full=9,9'-di-cis-zeta-carotene desaturase;
DE   AltName: Full=Carotene 7,8-desaturase;
GN   Name=crtQ; OrderedLocusNames=slr0940;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
CC   -!- FUNCTION: Catalyzes the conversion of zeta-carotene to lycopene via the
CC       intermediary of neurosporene. It carries out two consecutive
CC       desaturations (introduction of double bonds) at positions C-7 and C-7'
CC       (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9,9'-di-cis-zeta-carotene + 2 a quinone = 7,7',9,9'-tetra-cis-
CC         lycopene + 2 a quinol; Xref=Rhea:RHEA:30955, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:48716, ChEBI:CHEBI:62466, ChEBI:CHEBI:132124; EC=1.3.5.6;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000305};
CC       Name=NADP(+); Xref=ChEBI:CHEBI:58349; Evidence={ECO:0000305};
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC   -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA18400.1; -; Genomic_DNA.
DR   PIR; S76141; S76141.
DR   AlphaFoldDB; P74306; -.
DR   SMR; P74306; -.
DR   IntAct; P74306; 1.
DR   STRING; 1148.1653487; -.
DR   PaxDb; P74306; -.
DR   EnsemblBacteria; BAA18400; BAA18400; BAA18400.
DR   KEGG; syn:slr0940; -.
DR   eggNOG; COG3349; Bacteria.
DR   InParanoid; P74306; -.
DR   OMA; MLTIFMM; -.
DR   PhylomeDB; P74306; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000001425; 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; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016120; P:carotene biosynthetic process; IBA:GO_Central.
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;
KW   Carotenoid biosynthesis; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..489
FT                   /note="Zeta-carotene desaturase"
FT                   /id="PRO_0000217857"
SQ   SEQUENCE   489 AA;  54370 MW;  5447520DB92204D7 CRC64;
     MRVAIVGAGL AGMATAVELV DAGHEVELYE ARSFIGGKVG SWVDGDGNHI EMGLHVFFGC
     YYNLFNLMEK VGAKQNLRLK EHTHTFVNQG GRIGELDFRF LTGAPFNGLK AFFTTSQLDT
     KDKIANSIAL ATSPIVRGLV DFDGAMKTIR DLDRISFAEW FLSKGGNEGS LKKMWDPIAY
     ALGFIDTENI SARCMLTIFQ LFAARTEASV LRMLEGSPQE YLHKPIQEYL EQRGTKFYTR
     HKVKEIKTKV TDGETRVTGL IINDGVETKT VTADAYVAAC DVPGIKNLLP ENWRTQWDFF
     NKIYYLDTVP VATVQLRFDG WVTEMNDPAK RKQLEQAFGL DNLLYTSDAE FSCFADLALT
     SPADYYRPGE GSLLQLVLTP GDPFMKESNE AIAYRVLKQV KALFPSAADL NMTWYSVIKL
     AQSLYREAPG MDLFRPSQAT PIANFFLAGS YTQQDYIDSM EGATLSGRQA AQAILANQAR
     LQTAVLASQ