ID A0A226EJD1_FOLCA Unreviewed; 528 AA.
AC A0A226EJD1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 08-NOV-2023, entry version 17.
DE RecName: Full=Beta,beta-carotene 9',10'-oxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Fcan01_07742 {ECO:0000313|EMBL:OXA57559.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA57559.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA57559.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA57559.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA57559.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA57559.1}.
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DR EMBL; LNIX01000003; OXA57559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226EJD1; -.
DR OMA; PEMSDNH; -.
DR OrthoDB; 3145409at2759; -.
DR Proteomes; UP000198287; 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:SF24; CAROTENOID ISOMEROOXYGENASE; 1.
DR Pfam; PF03055; RPE65; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT BINDING 176
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 238
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 311
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 522
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 528 AA; 59863 MW; 9B969CAAD1ECC0BE CRC64;
MTDTRDLTKL YSNAQETKIP ELVPIEGQIP DYVNGTYLKV GPGKYHFENG FSVNHFFDAY
SSLAQFVIRN GSTVKFQNKY LETDVFRRAN AAKGSVVCEF GTGAIPDPSK GWLSRCIPQV
IPEMSDNHNM ALYQIGTNIC VAGETCFFRD LDAINIQLGD KHDTNKCYGL NFVSPHLLTD
DKTGVTYTVG SSFTTGLKYN FVRIPPMTGK PSTKEMLKKA QIFSTISSQV STLLSMHHSF
GMTSNYLVFV EQPYVLNVTK ILGGILTKGQ CFMDWLEWRG ELRNRFYLID KQSGKVHKTD
FVTQDPFMFT HFINCYEDDG HVVCDMLAFD NGDFFDANNV KKLLSNDPIR DSNFARAERF
VIPLLENAND IIDQKELVTL EYTTASVMKM GKKFVMKPEI LTTKGLELPC LNKKFIGKKY
KFFYVTGNTS PCGYFENSLV KMDLETKELK VWQGSTEEYP GEPMFIPNPS ANEDDEDNGV
ILSVVINSRM EEKDYLLFVD SKTFKEIGRA NFSQSKVPFL IHGIYLPE
//
