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
//