ID   A0A0P6WM87_9SPHN        Unreviewed;       488 AA.
AC   A0A0P6WM87;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN   ORFNames=SZ64_07220 {ECO:0000313|EMBL:KPL67926.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL67926.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL67926.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL67926.1,
RC   ECO:0000313|Proteomes:UP000049978};
RA   Palumuru S., Dellas N., Pearce S.L., Warden A.C., Oakeshott J.G.,
RA   Pandey G.;
RT   "Phylogenetic and kinetic characterization of a suite of dehydrogenases
RT   from a newly isolated bacterium, strain SG51-1L, that catalyze the turnover
RT   of guaiacylglycerol-beta-guaiacyl ether stereoisomers.";
RL   Appl. Environ. Microbiol. 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604294-1,
CC         ECO:0000256|RuleBase:RU364048};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1,
CC       ECO:0000256|RuleBase:RU364048};
CC   -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006787, ECO:0000256|RuleBase:RU364048}.
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:KPL67926.1}.
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DR   EMBL; JXQC01000003; KPL67926.1; -; Genomic_DNA.
DR   RefSeq; WP_054530193.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6WM87; -.
DR   STRING; 1603897.SZ64_07220; -.
DR   PATRIC; fig|1603897.4.peg.1352; -.
DR   OrthoDB; 6636843at2; -.
DR   Proteomes; UP000049978; 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:SF37; CAROTENOID CLEAVAGE DIOXYGENASE 7, CHLOROPLASTIC; 1.
DR   Pfam; PF03055; RPE65; 1.
PE   3: Inferred from homology;
KW   Dioxygenase {ECO:0000256|RuleBase:RU364048, ECO:0000313|EMBL:KPL67926.1};
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|RuleBase:RU364048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049978}.
FT   BINDING         167
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         218
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         285
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         477
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   488 AA;  55199 MW;  ED770F8CCB86F402 CRC64;
     MAHYPDTPGF TGVLRPIRLE GDILDVEIEG EIPSQLNGTF HRVHPDAQFP PKFENDQFFN
     GDGMVSMFHF HDGKVDFKQR YAQTDKWKAE REAGRSLFGA YRNPLTDEDS VQGMIRGTAN
     TNVMVHAGKL YAMKEDSPCL IMDPLTLETE GYTDFGGKIK NQTFSAHAKI DPVTGNFCNF
     GYAATGLFTT DCSYFEIDPE GNVLFETFFT VPYYCMMHDY GLTEDYAIFH IVPSTGNWDR
     LKAGKPHFGF DKTLPVYLGI LPRGSGVTNK DMRWFKAPKT IFASHVMNAF QNGTKIHFDV
     PQAEGNSFPF FPDIHDDSFD PVAALPYLHR WTVDMGSNGE EFESVEKLTD WIDEFPRIDE
     RYVGQPYRHG WGLVMDPEMP MEFLRGRASG FKMNKIGHWD HATGKQDFWW AGPQSIVQEP
     CFVPRHKDSA EGDGYIIALV DNLITNYSDL VVLDALHMSE GPIGRAKLPI RIRSGLHGNW
     ADGSKLPN
//