ID I1LVC9_SOYBN Unreviewed; 540 AA.
AC I1LVC9;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 2.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=carotenoid 9,10-dioxygenase {ECO:0000256|ARBA:ARBA00039084};
DE EC=1.14.99.n4 {ECO:0000256|ARBA:ARBA00039084};
GN ORFNames=GLYMA_12G236700 {ECO:0000313|EMBL:KRH27468.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH27468.1};
RN [1] {ECO:0000313|EMBL:KRH27468.1, ECO:0000313|EnsemblPlants:KRH27468}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH27468};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH27468.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH27468}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH27468};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH27468.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH27468.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone +
CC 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial; Xref=Rhea:RHEA:26393,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173; EC=1.14.99.n4;
CC Evidence={ECO:0000256|ARBA:ARBA00036367};
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; CM000845; KRH27468.1; -; Genomic_DNA.
DR AlphaFoldDB; I1LVC9; -.
DR SMR; I1LVC9; -.
DR STRING; 3847.I1LVC9; -.
DR PaxDb; 3847-GLYMA12G36530-1; -.
DR EnsemblPlants; KRH27468; KRH27468; GLYMA_12G236700.
DR Gramene; KRH27468; KRH27468; GLYMA_12G236700.
DR eggNOG; KOG1285; Eukaryota.
DR HOGENOM; CLU_016472_0_2_1; -.
DR InParanoid; I1LVC9; -.
DR OMA; TRLHRWR; -.
DR Proteomes; UP000008827; Chromosome 12.
DR GO; GO:0009570; C:chloroplast stroma; IBA:GO_Central.
DR GO; GO:0010436; F:carotenoid dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016121; P:carotene catabolic process; IBA:GO_Central.
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|ARBA:ARBA00022964};
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:UP000008827}.
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 269
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 335
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 525
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 540 AA; 60814 MW; 94F599F0B0605534 CRC64;
MGDDGKKMSG EGGIVKVEPK PSNGFTSKVV DLLEKLVVKF LYDSSLTHHY LTGNFAPVPE
TPPTKDLPVK GYLPDCLNGE FVRVGPNPKF SPVAGYHCSG ICFSNFDLLN CRMIHGLRIK
DGKATYVSRF VRTSRLKQEE YFGGSKFMKI GDLKGLFGLL MVNIHMLRTK WKVLDVSYGT
GTANTALVYH HGKLLALSEA DKPYAIKVFE DGDLQTLGML DYDKRLGHSF TAHPKVDPFT
DVYTYRVISK DGYMHDPVPI TVSDPIMMHD FAITENYAIF LDLPLIFRPK EMVKNKTLIF
SFDSTKKARF GVLPRYAKDE KLIRWFELPN CFIFHNANAW EEEDEVVLIT CRLQNPNLDL
VGGTAKEKLE NFSNELYEMR FNMKTGEASQ KKLSASAVDF PRVNESYTGR KQRYVYGTTL
DSIAKVTGII KFDLHAEPDH GKTKLEVGGN VQGLYDLGPG KYGSEAVYVP RVPGTDSEED
DGYLIFFAHD ENTRKSFVHV INAKTMSADP VAVVELPHRV PYGFHAFFVT EEQLQEQGKL
//
