ID A0A132T6Z9_9MYCO Unreviewed; 455 AA.
AC A0A132T6Z9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-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=ASJ79_23595 {ECO:0000313|EMBL:KWX66973.1};
OS Mycobacterium sp. NAZ190054.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1747766 {ECO:0000313|EMBL:KWX66973.1, ECO:0000313|Proteomes:UP000070146};
RN [1] {ECO:0000313|EMBL:KWX66973.1, ECO:0000313|Proteomes:UP000070146}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAZ190054 {ECO:0000313|EMBL:KWX66973.1,
RC ECO:0000313|Proteomes:UP000070146};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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:KWX66973.1}.
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DR EMBL; LMVQ01000156; KWX66973.1; -; Genomic_DNA.
DR RefSeq; WP_067955621.1; NZ_LMVQ01000156.1.
DR AlphaFoldDB; A0A132T6Z9; -.
DR OrthoDB; 6636843at2; -.
DR Proteomes; UP000070146; 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, ECO:0000313|EMBL:KWX66973.1};
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:UP000070146}.
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 210
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 446
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 455 AA; 50215 MW; DD3AD89019C8D0D4 CRC64;
MTETTSDHTD SALPGTGEFF RVGNYAPVTD ELTAFDLPVE GAIPPELEGW YLRNGPNPRE
ASGHWFAGDG MIHGVRIENG RAAWYRNRWV RTDSFVDPFP LYNPDGTRNL RASVANTNVV
NHAGKTLALV ESSLPYEITN ELETVGPYDF GGKLADAMTA HPKICPATGE LHFFGYGNIV
TPHVTYHRAD ANGELVIDRP LDVPALTMMH DFALTANHVV FMDLPIVFDV EIAARDDGDM
PYRWDDDYGA RFGVLRRDDP YGAVRWFEID PCYVFHVANA FDRASADGDS IVVQAVRYPE
LWRQDGGFDV DGVMWTWTID LQTGTVRESQ LDDRAVEFPR IDDRLATLPA RYAVSVGDAG
LIRYDLLTGD AVEHRFGTDA SPGGPGEAVF VPSMSGAADE SSGWYLGYVY DPDRDGSDLV
ILDASDFSGA PVARIKLPQR VPYGFHGNWI VGQPS
//
