ID   A0A1I6AVY7_9BACI        Unreviewed;       476 AA.
AC   A0A1I6AVY7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Carotenoid cleavage dioxygenase {ECO:0000313|EMBL:SFQ72868.1};
GN   ORFNames=SAMN05421670_3666 {ECO:0000313|EMBL:SFQ72868.1};
OS   Psychrobacillus psychrotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Psychrobacillus.
OX   NCBI_TaxID=126156 {ECO:0000313|EMBL:SFQ72868.1, ECO:0000313|Proteomes:UP000198734};
RN   [1] {ECO:0000313|Proteomes:UP000198734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11706 {ECO:0000313|Proteomes:UP000198734};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOXU01000009; SFQ72868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6AVY7; -.
DR   STRING; 126156.SAMN05421670_3666; -.
DR   Proteomes; UP000198734; 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:SFQ72868.1};
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:UP000198734}.
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         216
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         280
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         461
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   476 AA;  54799 MW;  61E47561488C3D7E CRC64;
     MTKVEFNPYL SAPLYGRPSI EELFVEELPV IEGEIPVDFS GAYIRNGPSQ KYEPMERHHW
     FDGDGMLHGI YIKDGKVSYR NRYIETKGYQ YEDKTKKSEW VGLMGNVLQN PSFERLKNTS
     NTDVIYHNNN LLSLWYMSGE PYRIDAKTLE TLGVENFQGQ LSTSISAHSK VDENTGELIF
     FDYGNKFPYM MYGVVSADGK SVHSVPIELP GPRNPHDMWI TENHSILMDL PLFNDLEALK
     KGRYKVKFHR ELPSRFGVIP RYGSSEDIQW FEAEPCYIYH SINAWEEGDE IVLIGCRVKE
     PQPPKNASAS EIERMMQYLQ MNAQLHYWRL NRITGEVKEG ELCDMNTEFP VMNLNYLGRK
     SRYSYNAHIE SALTLKFNGL VKYDTWTGGS TRYMFGPHQY GTEAAFAPKK NASCEDDGYV
     ITYLYNEELD HSELIILDAK QFDIGPIARI ALPQPVPMGF HATWISGENF YGKEEA
//