ID A0A388LMF2_CHABU Unreviewed; 749 AA.
AC A0A388LMF2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=CBR_g37129 {ECO:0000313|EMBL:GBG83415.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG83415.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG83415.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG83415.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBG83415.1}.
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DR EMBL; BFEA01000438; GBG83415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388LMF2; -.
DR STRING; 69332.A0A388LMF2; -.
DR EnsemblPlants; GBG83415; GBG83415; CBR_g37129.
DR Gramene; GBG83415; GBG83415; CBR_g37129.
DR OMA; LNMTWYS; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000265515; 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; IEA:UniProtKB-EC.
DR GO; GO:0052886; F:9,9'-dicis-carotene:quinone oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0052889; P:9,9'-di-cis-zeta-carotene desaturation to 7,9,7',9'-tetra-cis-lycopene; IEA:EnsemblPlants.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901177; P:lycopene biosynthetic process; IEA:EnsemblPlants.
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 PRINTS; PR00419; ADXRDTASE.
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:UP000265515}.
FT DOMAIN 236..700
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 122..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 82317 MW; E6308FB291738AA9 CRC64;
MAMAASMSVA GTAVPAAYVE AGTWGKSSTT LDTCSLLSCR RQSVPGACMD AAGRGSRERG
LAAWMGSRRC PDCFYWSMSS SVVGRRGSRS RLGARLGSAA AGAAAEQFLS GQRLVLDPKK
EEEEGGFVPT GSDVGCAPRQ QRRRSRMMVR RVVRAGLREV QRQREEQQEE DSAAAGENGS
WGGEIFQSTS SSSIDRASLA TMVSNMRRKA PKGLFPPEPA KYNGPKLRVA IVGSGLAGMS
TAVELLDQGH EVDIFEGRPF IGGKVASYKD KNGNHVEMGL HVFFGCYNNL FRLMNKVGGD
RNLLLKDHTH TFINRGGGVG ELDFRFFTGA PLHGIKAFLS TNQLSFGDKV QNSLALATSP
IVRALVDPEG AMQDIRDLDK VSFTEWFLGQ GGSRGSIDRM WNPVAYALGF IDCDNISARC
MLTIFAFFAT KTEASVLRML KGSPDNGLSG PIRKYIEDRG GRFHVRWGCR EILYEEQLDG
SAVVTGLVVG KSTEKKVVKA DCYVAACDIP GIQRLLPKRW REWEFFDNIY KLSGVPVVTV
QLRYDGWVTE MQDIQRSRNS KSAVGIDNLL YSADADFSCF ADLALTSPED YYKEGEGSLL
QCVITPGDPY MPLSNEEIVR RVNEQVFKLF PSSRGLNLTW SSVVKIAQSL YREAPGMDLF
RPDQSTPVPN FFLSGSYTKQ DYIDSMEGAT LSGRQASTKI CQAGQLLYDL SQSLTAKAAQ
QQEQQISGES DQQLQHQKEE DEEELLTFV
//
