ID A0A109LMY5_9SPHN Unreviewed; 501 AA.
AC A0A109LMY5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN ORFNames=AUC45_14985 {ECO:0000313|EMBL:KWV90535.1};
OS Erythrobacter sp. YT30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=1735012 {ECO:0000313|EMBL:KWV90535.1, ECO:0000313|Proteomes:UP000055668};
RN [1] {ECO:0000313|EMBL:KWV90535.1, ECO:0000313|Proteomes:UP000055668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YT30 {ECO:0000313|EMBL:KWV90535.1,
RC ECO:0000313|Proteomes:UP000055668};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. YT30.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KWV90535.1}.
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DR EMBL; LMAF01000003; KWV90535.1; -; Genomic_DNA.
DR RefSeq; WP_067604367.1; NZ_LMAF01000003.1.
DR AlphaFoldDB; A0A109LMY5; -.
DR STRING; 1735012.AUC45_14985; -.
DR OrthoDB; 6636843at2; -.
DR Proteomes; UP000055668; 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:SF89; CAROTENOID 9,10(9',10')-CLEAVAGE DIOXYGENASE 1; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|RuleBase:RU364048};
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:ARBA00023002,
KW ECO:0000256|RuleBase:RU364048};
KW Reference proteome {ECO:0000313|Proteomes:UP000055668}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 292
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 479
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 501 AA; 56520 MW; 2D5AC5F180348CB6 CRC64;
MQITRHPPVK TSLKPSNHPY LSGPWTPCHE EVDVEELEAI EGDIPADIDG IYLRNTENPV
HQPLGRHHPF DGDAMVHQVS ISGGKASYRN RFVRTSCFEA EQIAGEALWG GLMDPPALSK
RPGFGAHGSL KDTASTDIIV HAGTALATLY QCGEAWQLDP VTLENLGKAS WGPLDGVSAH
PKVDEETGEL MFFNYSKHAP FMHYGVVDRA GKIAHYVPIP LPGPRLPHDM AITKNWSILN
DMPLFWDEEL LKRDIHAARI HEGVPTRFAL IPRYGQPEDI RWFEADPTYV LHWTNAYEVS
GSEGDEVILE GYFQEKPMPD PLEEAGEYSH MMAYVDEHSF KPKLHRWRFN LETGETREER
LSDRIVEFGM INPAYLMRKS RYVWSTTTKP GWFLFNGYVR HDTETGEEQV LELPDGVYAS
ESPMVPRKGA DLEDDGYLIT FLINENTGTS ECAILDASDV TRGPVCRLAL PHKISSGVHS
TWVEHEQLRK DAEFKRELLS A
//
