GenomeNet

Database: UniProt
Entry: A0A022RZ17_ERYGU
LinkDB: A0A022RZ17_ERYGU
Original site: A0A022RZ17_ERYGU 
ID   A0A022RZ17_ERYGU        Unreviewed;       479 AA.
AC   A0A022RZ17;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
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   ORFNames=MIMGU_mgv1a005547mg {ECO:0000313|EMBL:EYU45246.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU45246.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU45246.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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       {ECO:0000256|RuleBase:RU362008}.
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         Evidence={ECO:0000256|ARBA:ARBA00000914,
CC         ECO:0000256|RuleBase:RU362008};
CC   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004900, ECO:0000256|RuleBase:RU362008}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|RuleBase:RU362008}. Plastid, chromoplast
CC       {ECO:0000256|RuleBase:RU362008}.
CC   -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC       {ECO:0000256|ARBA:ARBA00010192, ECO:0000256|RuleBase:RU362008}.
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; KI630191; EYU45246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022RZ17; -.
DR   STRING; 4155.A0A022RZ17; -.
DR   eggNOG; KOG0029; Eukaryota.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0052887; F:7,9,9'-tricis-neurosporene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016719; F:9,9'-di-cis-zeta-carotene desaturase activity; IBA:GO_Central.
DR   GO; GO:0052886; F:9,9'-dicis-carotene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
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; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR014103; Zeta_caro_desat.
DR   NCBIfam; TIGR02732; zeta_caro_desat; 1.
DR   PANTHER; PTHR42923; PROTOPORPHYRINOGEN OXIDASE; 1.
DR   PANTHER; PTHR42923:SF41; ZETA-CAROTENE DESATURASE, CHLOROPLASTIC_CHROMOPLASTIC; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Carotenoid biosynthesis {ECO:0000256|RuleBase:RU362008};
KW   Chloroplast {ECO:0000256|RuleBase:RU362008};
KW   Chromoplast {ECO:0000256|RuleBase:RU362008};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362008}; Plastid {ECO:0000256|RuleBase:RU362008};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT   DOMAIN          1..460
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   479 AA;  53269 MW;  1C7ABD0DFB6510E8 CRC64;
     MSTAVELLDQ GHEVDIYDSK SFVGGKVGSF VDKQGNHIEM GLHVFFGCYN NLFRLMKKVG
     AEKNLLVKDH THTFVNKGGD IGELDFRFPI GAPIHGMRAF LTTNQLGTYD KARNAVALAL
     SPVVRALVDP DGAMQNIRDL DNISFSEWFM SKGGTRKSIQ RMWDPVAYAL GFIDCDNISA
     RCMLTIFSLF ATKTEASLLR MLKGSPDVYL SGPIRKYITD RGGRFHLRWG CREVLYDRSA
     DGGVYVTGLA MSKATEKKTV KADAYVAACD VPGIKRLLPQ DWRESQFFDN IYKLVGVPVV
     TVQLRYNGWV TELKDLERSR QLRQASGLDN LLYTPDADFS CFADLALTSP ADYYIEGQGS
     LLQCVLTPGD PYMPLLNDEI IKRVTKQVLV LFPSSQGLEV TWSSVVKIGQ SLYREGPGKD
     PFRPDQKTPI KNFFLAGSYT KQDYIDSMEG ATLSGRLASA FICGAGEELV ALPNYLLKK
//
DBGET integrated database retrieval system