ID A0A1N6FGT0_9BURK Unreviewed; 477 AA.
AC A0A1N6FGT0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Carotenoid cleavage dioxygenase {ECO:0000313|EMBL:SIN94455.1};
GN ORFNames=SAMN05444165_0191 {ECO:0000313|EMBL:SIN94455.1};
OS Paraburkholderia phenazinium.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=60549 {ECO:0000313|EMBL:SIN94455.1, ECO:0000313|Proteomes:UP000185151};
RN [1] {ECO:0000313|EMBL:SIN94455.1, ECO:0000313|Proteomes:UP000185151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS95 {ECO:0000313|EMBL:SIN94455.1,
RC ECO:0000313|Proteomes:UP000185151};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|PIRSR:PIRSR604294-1};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR604294-1};
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family.
CC {ECO:0000256|ARBA:ARBA00006787}.
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DR EMBL; FSRU01000001; SIN94455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6FGT0; -.
DR Proteomes; UP000185151; 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:0000313|EMBL:SIN94455.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000185151}.
FT REGION 455..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 265
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 439
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 477 AA; 52233 MW; 795C3531E62A74CC CRC64;
MTSDMTTLDL NAGATAPVVD EIDLVDLRVT GTIPRDLNGV LIRNGPNPLQ GRFEGNNVLN
WWPEAAMWHG ISFQDGRVTG YRNRWARTQR WAKVHAPDIA ASLLDTNPNV NVLHHAGEIL
ALAEGGAPLA MTAGLESLGT SRRHPGLAGG MTAHPKIDPE TGELMTFRAD WQKPWLRYGV
TDANGAPGVD VEIAVPSASM MHDMAITATR SILLDLNVAY DFSMLSRGYR MPLRWHDERQ
ARIGVMPRHG GEVRWFEIAP CFIQHGVNAY DVGTSTVVLD AVRYTHYLRV ADRGAAFEDN
PVGVLRRYVI DLDRGTVTET QLDDAGIELP RINEGRTGRP YRFAYAAEQP TNREIRGVVR
YDLADASMQR YRVPEGDQNS EPVFVARPDA TAEDDGWLLV CVYRRATDTS DVVILDGRDI
ASAPIATVQL PRRIPAGFHG AWLPIVSGVN ATAVRSPDAA GMPGAGQSRS SSSRSRG
//
