ID V7BJQ1_PHAVU Unreviewed; 581 AA.
AC V7BJQ1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=PHAVU_007G186000g {ECO:0000313|EMBL:ESW16806.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW16806.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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; CM002294; ESW16806.1; -; Genomic_DNA.
DR RefSeq; XP_007144812.1; XM_007144750.1.
DR AlphaFoldDB; V7BJQ1; -.
DR STRING; 3885.V7BJQ1; -.
DR EnsemblPlants; ESW16806; ESW16806; PHAVU_007G186000g.
DR GeneID; 18626318; -.
DR Gramene; ESW16806; ESW16806; PHAVU_007G186000g.
DR KEGG; pvu:PHAVU_007G186000g; -.
DR eggNOG; KOG0029; Eukaryota.
DR OMA; LNMTWYS; -.
DR OrthoDB; 348089at2759; -.
DR PhylomeDB; V7BJQ1; -.
DR UniPathway; UPA00803; -.
DR Proteomes; UP000000226; Chromosome 7.
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: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 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:UP000000226}.
FT DOMAIN 83..547
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
SQ SEQUENCE 581 AA; 64069 MW; EC603B1696783DFB CRC64;
MAMASLIQCS AATSFSATRG GDSTGFFSPF TARFSKTHKS RLRCSLDDNV SDMSVNAPKG
LFPPEPEHYR GPKLKVAIVG AGLAGMSTAV ELLDQGHEVD IYESRSFIGG KVGSFVDKRG
NHIEMGLHVF FGCYNNLFRL LKKVGAHNNL LVKDHTHTFV NKGGQIGELD FRFPVGAPIH
GIRAFLTTNQ LNTYDKARNA VALAQSPVVK ALIDPDGALR DIRNLDSISF SDWFLSKGGT
RMSIQKMWDP VAYALGFIDC DNISARCMLT IFALFATKTE ASLLRMLKGS PDVYLSGPIR
KYITDRGGRF HLRWGCRELL YDKTADGSIY VTGLSMSKAT AKKIVKADAY VAACDVPGIK
RLIPSEWREQ KFFNNIYELV GVPVVTVQLR YNGWVTELQD LEKSRQLRKA IGLDNLLYTP
DADFSCFADL ALSSPEDYYI EGQGSLLQCV LTPGDPYMPL PNDEIIARVA KQVLSLFPSA
QGLEVTWSSV VKIGQSLYRE GPGKDPFRPD QITPVKNFFL AGSYTKQDYI DSMEGATLSG
RQASAYICNA GEGLVALRKE VDAELKDDLE FTNTKDELSL V
//
