ID R4T228_9PSEU Unreviewed; 449 AA.
AC R4T228;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN ORFNames=AORI_6292 {ECO:0000313|EMBL:AGM08875.1};
OS Amycolatopsis keratiniphila.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis japonica group.
OX NCBI_TaxID=129921 {ECO:0000313|EMBL:AGM08875.1, ECO:0000313|Proteomes:UP000013968};
RN [1] {ECO:0000313|EMBL:AGM08875.1, ECO:0000313|Proteomes:UP000013968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCCB10007 {ECO:0000313|EMBL:AGM08875.1,
RC ECO:0000313|Proteomes:UP000013968};
RX PubMed=23627759; DOI=10.1186/1471-2164-14-289;
RA Tang B., Wang Q., Yang M., Xie F., Zhu Y., Zhuo Y., Wang S., Gao H.,
RA Ding X., Zhang L., Zhao G., Zheng H.;
RT "ContigScape: a Cytoscape plugin facilitating microbial genome gap
RT closing.";
RL BMC Genomics 14:289-289(2013).
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}.
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DR EMBL; CP003410; AGM08875.1; -; Genomic_DNA.
DR RefSeq; WP_016336591.1; NC_021252.1.
DR AlphaFoldDB; R4T228; -.
DR KEGG; aoi:AORI_6292; -.
DR PATRIC; fig|1156913.3.peg.6419; -.
DR HOGENOM; CLU_016472_0_2_11; -.
DR Proteomes; UP000013968; Chromosome.
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, ECO:0000313|EMBL:AGM08875.1};
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|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364048};
KW Reference proteome {ECO:0000313|Proteomes:UP000013968}.
FT BINDING 152
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 261
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 442
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 449 AA; 49050 MW; 0A8F7B277E911712 CRC64;
MNRYVLGNFA PVTEEITAFD LPVTGKIPDD LDGRYLRIGP NPLGLEDASA HIWTLGEGMV
HGVRLRDGRA EWYRNRWVRS ASVADRLGEP RRGQVADERL DFAPNVQIAG HGGRLYALIE
GGLPPYELTD ELDTVGPAGL GATEQGFSAN AHSKYDHATG ELHSLAFRYG ADFVQHIVIG
PDGRNRSVTD IKTPTLPYMH DFALTEHYVV FYESPMVFEP GRLATGVPFH WNRALPSRLG
LLPRAGGAVQ WFETAPVMVG HTLNAFEDNG TVVVDVVVHP RPIDFADVGA SKPVLERWTA
DLADGRVART LLHDRPQDFP RLNGRFGGKP YRYGYSAAAE LYATPSATEP DRPDEGFSSA
LLKHDLLTGV TEAHEFGRDA SAGETVFVPS ARAAAEDDGY NLVYVHDRDR GAADLVILAS
QDFTGEPLAR VHLPARVPLG LHGSWIPAA
//
