ID   A0A0P6XGB9_9SPHN        Unreviewed;       488 AA.
AC   A0A0P6XGB9;
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_06185 {ECO:0000313|EMBL:KPL67742.1};
OS   Erythrobacter sp. SG61-1L.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=1603897 {ECO:0000313|EMBL:KPL67742.1, ECO:0000313|Proteomes:UP000049978};
RN   [1] {ECO:0000313|EMBL:KPL67742.1, ECO:0000313|Proteomes:UP000049978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG61-1L {ECO:0000313|EMBL:KPL67742.1,
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:KPL67742.1}.
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DR   EMBL; JXQC01000003; KPL67742.1; -; Genomic_DNA.
DR   RefSeq; WP_054530013.1; NZ_JXQC01000003.1.
DR   AlphaFoldDB; A0A0P6XGB9; -.
DR   STRING; 1603897.SZ64_06185; -.
DR   PATRIC; fig|1603897.4.peg.1145; -.
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:KPL67742.1};
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         476
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;  54834 MW;  15207C0148E4A9A1 CRC64;
     MTHFPDNPGF TGTLRPLRLQ GDILDMEVEG EIPAELNGAF HRVHPDNQFA PMFDDDQFFN
     GDGMVSMFRV HDGKVDFRQR YAHTDKWKLE NKAGRSLFGH YRNHLTDDPS VAGQIRGTAN
     TNVMVHAGKL YAMKEDSPCL IMDPNSLDSF GYTDFGGRLE AKTFCAHPKI DPVTGNMCAF
     SYMSKGPMTY DMSYFEISPE GELLFEIPFE NKYLCMMHDF GITQDYAVWN VMPCITNMER
     LEKRMPYFGF DHSLPTWLAV LPRKPGATAK DLRWFKAPAN CFTGHVMNAF NDGTKVYFDL
     PIAAKNSFPF FPDVTGAPFD PIGGLSYLTR WTVDLSSNGE EFEQVEQMTS IADEFPRIDD
     RYAGQAYRHG WMIAFDPHAR YEGPPGPFVG ALNTLCHIDL STGDTKSWWP GPTSGIQEPC
     FIPKSANAPE GEGYIVALVD DHVANYSDLC FFDAQRIDQG PIARAKLPVK IRQGLHGNWS
     TAKQLGVA
//