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Database: UniProt
Entry: A0A1X9LI31_9MICO
LinkDB: A0A1X9LI31_9MICO
Original site: A0A1X9LI31_9MICO 
ID   A0A1X9LI31_9MICO        Unreviewed;       485 AA.
AC   A0A1X9LI31;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE            EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN   ORFNames=B5808_02215 {ECO:0000313|EMBL:ARJ04172.1};
OS   Cnuibacter physcomitrellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Cnuibacter.
OX   NCBI_TaxID=1619308 {ECO:0000313|EMBL:ARJ04172.1, ECO:0000313|Proteomes:UP000192775};
RN   [1] {ECO:0000313|EMBL:ARJ04172.1, ECO:0000313|Proteomes:UP000192775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XA(T) {ECO:0000313|Proteomes:UP000192775};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; CP020715; ARJ04172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X9LI31; -.
DR   STRING; 1619308.B5808_02215; -.
DR   KEGG; cphy:B5808_02215; -.
DR   Proteomes; UP000192775; 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:ARJ04172.1};
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|RuleBase:RU364048};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192775}.
FT   BINDING         170
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         217
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         283
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT   BINDING         463
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ   SEQUENCE   485 AA;  53860 MW;  404B28F493421652 CRC64;
     MALWPTDNKF LNGPFAPWAE ESEAFDLPVQ GEIPADLAGA LFRISSNPRF EPRNTDRYHW
     WEGDGMVCAV YVRDGRVGYR TRWVETDSMK VEVEQGEAVY SGFVSGGTPG RLPAGAPPAK
     NVANTNVGIF DDKLLVYYEG GLPHELHPET LATKGAYDFH GGIDTLCTAH YKIDRLSGDM
     LFFAAKGPTI TWYRADVTTG RIVESHAIDI GLPVLMHDFV VSDNYAIFFV TPSLFRLDLI
     MQGRPGVIWD ESVLPHGTQI VMMDRRTKKV TWYEANGVFG PTHFYNAYEV GDEVVIDLHR
     ISRLGNPASG NTPLSSHEWF PPALPWQWRV NVKTGKVSDR MISGVAGEFP KINDAYVGAA
     HRYGYFVTTR SLDRQTMSDG LAKHDHLLDS TVVIEGVGGL TNPSEPVFVA REGAVEEDDG
     YILSIWWNPT TELSELLVHD AVRMTRDPLA RVPLPVRVPF GFHGSWAGRD VLEGAIAAQR
     EPADL
//
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