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Database: UniProt
Entry: A0A498IFQ6_MALDO
LinkDB: A0A498IFQ6_MALDO
Original site: A0A498IFQ6_MALDO 
ID   A0A498IFQ6_MALDO        Unreviewed;       926 AA.
AC   A0A498IFQ6;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Zeta-carotene desaturase, chloroplastic/chromoplastic {ECO:0000256|ARBA:ARBA00015490};
DE            EC=1.3.5.6 {ECO:0000256|ARBA:ARBA00012788};
DE   AltName: Full=9,9'-di-cis-zeta-carotene desaturase {ECO:0000256|ARBA:ARBA00031301};
DE   AltName: Full=Carotene 7,8-desaturase {ECO:0000256|ARBA:ARBA00030952};
GN   ORFNames=DVH24_036749 {ECO:0000313|EMBL:RXH82408.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH82408.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH82408.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH82408.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Carotenoid biosynthesis; lycopene biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004900}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chromoplast
CC       {ECO:0000256|ARBA:ARBA00004260}.
CC   -!- SIMILARITY: Belongs to the zeta carotene desaturase family.
CC       {ECO:0000256|ARBA:ARBA00010192}.
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:RXH82408.1}.
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DR   EMBL; RDQH01000338; RXH82408.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498IFQ6; -.
DR   STRING; 3750.A0A498IFQ6; -.
DR   UniPathway; UPA00803; -.
DR   Proteomes; UP000290289; Chromosome 12.
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:InterPro.
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; 2.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   DOMAIN          72..133
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   DOMAIN          157..592
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
SQ   SEQUENCE   926 AA;  104358 MW;  C42000F02E8F3E00 CRC64;
     MASWALLPAA PVTGRCIVTP ARTKRSSSFW VRSSLDTNVS DMGVNAPKGL FPPEPERYRG
     PKLKVAIIGA GLAGMSTAVE LLDQGHEVDV YESRPFIGGK VGSFVDKKGN HIEMGLHVFF
     GCYSNLFRLM KKVDNFCLLE LLLHLAILRI IANKFSWTTT KQVGADENLL VKDHTHTFVN
     KGGSIGELDF RFPIGAPIHG ILAFLSTNQI KAGFPFATTT DFTANHHHCH ISLFWIPTYD
     KARNAVALAL SPVVKALVNP DGALQDVRNL DSISFSDWFL SKGGTRMSIQ RMWDPVAYAL
     GFIDCDNISA RCMLTIFTLF ATKTEASLLR MLKGSPDVYL SGPIRDYIIA KGGRFHLRWG
     CREILYDESS DGETYVAGFS MSKATNKKVV KADAYVAACD VPGIKRLLPS QWRELDFFNN
     IYELVGVPVV TVQLRYDGWV TELQDLERSR KSKQALGLDN LLYTPDADFS CFADLALTSP
     EDYYIEGQGS LLQCVLTPGD PYMPLPNEEI IARVTKQVLA LFPSSQGLEV TWSSVVKIGQ
     SLYREGPGKD PFRPDQKTPV KNFFLAGSYT KQDYIDSMEG ATLSGRQASA YICDAGEELV
     GLRKKFAAQD SGEYTKAVNT TDELSTVWYV GRDGTERSGT RCSVPRLVRL KRVERVVPRD
     EFWFRLTPWN DSFHIRGTQN YNLSVSSLFP SEGIFAPSPF HPVLSRLVPF AYQMIPKRAI
     HGIRCYSTAP DNNRSNNHRR ETPQRALWIL PLLIFINMLE TNRVNDNESD EFSVFDIDDV
     VTILKFDFEN AYFVTVTYLY RLNETFLVGI FTSAIYTEDC IFEDPTVRFR GKKILRFSFV
     SLVLDINCNM QICKKMCLLV IHFEFDCILN VSPTYLFLFP GHKDIPKTST EASHLHRWRY
     IIRHAETESW NVSGHLFTPA YGRSND
//
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