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Database: UniProt
Entry: A0A2P5A821_PARAD
LinkDB: A0A2P5A821_PARAD
Original site: A0A2P5A821_PARAD 
ID   A0A2P5A821_PARAD        Unreviewed;       454 AA.
AC   A0A2P5A821;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   08-NOV-2023, entry version 11.
DE   SubName: Full=Carotenoid oxygenase {ECO:0000313|EMBL:PON32676.1};
GN   ORFNames=PanWU01x14_359300 {ECO:0000313|EMBL:PON32676.1};
OS   Parasponia andersonii (Sponia andersonii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX   NCBI_TaxID=3476 {ECO:0000313|EMBL:PON32676.1, ECO:0000313|Proteomes:UP000237105};
RN   [1] {ECO:0000313|Proteomes:UP000237105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA   Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA   Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA   Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA   Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA   Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA   Smit S., Geurts R.;
RT   "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT   legume Parasponia.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787}.
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:PON32676.1}.
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DR   EMBL; JXTB01000793; PON32676.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P5A821; -.
DR   STRING; 3476.A0A2P5A821; -.
DR   OrthoDB; 318119at2759; -.
DR   Proteomes; UP000237105; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:InterPro.
DR   InterPro; IPR004294; Carotenoid_Oase.
DR   PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 1.
DR   PANTHER; PTHR10543:SF30; OS09G0321200 PROTEIN; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR604294-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR604294-1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237105}.
FT   BINDING         227
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         276
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         340
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   454 AA;  51517 MW;  A46A68167B5BB0DF CRC64;
     MLRAFELAPA MRIDISKTIK NTTANLLDAF VDSAFEFVNQ PLLPSQRNFA PVDELGGPVA
     IAIIQGSIPD NLPEGVYIRN GANPLFEGLK STKSVFGKSS RIWVEGEGML HALYFSKDDD
     HGINWTVHYN NRYVETETFN QEKQRNKPYF LPITGGDFPA LLSASLLNLL RFGKVDKYMS
     NTNVFEHSGK VYAITKNHVP QEIDISTLET LGNWDLSTAW NRCFTSHPKR APGTGELVIT
     GMKAIKPYIE LGVISADGKK FVHRADLKLG RCTFFHDFRV TKRYNVFLDF PLTIDITSFV
     SGGGLMKYDK EGYATMGVMP RYGDADSITW FKVDTNCTFH IFNCFEDGDE ENETAKRHDR
     IDFNANLNTY ENEQVVVWRC RALESVVLCP RKKNFDTSIK DGLLYDRPHE WRLNMRTGEV
     WEANLTADTE FSVVFRIDLG TLKLLTLRQA APQV
//
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