ID A0A1P8WSZ8_9SPHN Unreviewed; 480 AA.
AC A0A1P8WSZ8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Dioxygenase {ECO:0000256|RuleBase:RU364048};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU364048};
GN ORFNames=BWQ93_00785 {ECO:0000313|EMBL:APZ97189.1};
OS Sphingopyxis sp. QXT-31.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1357916 {ECO:0000313|EMBL:APZ97189.1, ECO:0000313|Proteomes:UP000188055};
RN [1] {ECO:0000313|EMBL:APZ97189.1, ECO:0000313|Proteomes:UP000188055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QXT-31 {ECO:0000313|EMBL:APZ97189.1,
RC ECO:0000313|Proteomes:UP000188055};
RA Liang J.S.;
RT "Microbe-microbe interactions indirectly alter the fate of arsenic in
RT presence of MnII.";
RL Submitted (JAN-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; CP019449; APZ97189.1; -; Genomic_DNA.
DR RefSeq; WP_077028855.1; NZ_CP019449.1.
DR AlphaFoldDB; A0A1P8WSZ8; -.
DR STRING; 1357916.BWQ93_00785; -.
DR KEGG; sphq:BWQ93_00785; -.
DR OrthoDB; 6636843at2; -.
DR Proteomes; UP000188055; 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};
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:UP000188055}.
FT BINDING 183
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 297
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 474
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 480 AA; 53035 MW; 12C1697F57C4D7BB CRC64;
MASNVESLIR GAVVKGIGKV ADFNRKRLPR PTDAHPFLTG IHKPMTEEVT LEELRVDGEI
PAALTGRYLR NGPNPAIAPD PASYHWFTGA GMVHGIRIEG GKAVWYRNRW VRGSEACEAL
GEELPPGPRH ITNDAPNTNV VGLAGRTFAI VEAGGKPVEL GYELDTIAHN PFDGTLLGGY
TAHPHHDPVT DEMHAITYRG DEPNKVWHVV LDQDAQVTRE LAIPVRDGPS IHDCAITENY
VLVLDLPVTF SMKMLLSGYR FPYAWNEAHQ ARVGLLPRKG SAEEIIWVPV EPCYVFHPAN
AYETEDGKVI VDVVAHETMF ASSKRGPDSE KSRMERWTID PAAGTTTRTV IHDHAQEFPR
YDERLTTKPY RYVYSVAIPD GTSTEWALAE TKLFRHDLNA GTTDVHDFGP GRHPGEFVFV
PRSAAGAEDD GWLIGLVVDM NDETTDLVIL NADDFTGKPQ AVVHLPHRVP PGFHGNWVAD
//