ID A0A1Z5RBA0_SORBI Unreviewed; 564 AA.
AC A0A1Z5RBA0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 08-NOV-2023, entry version 15.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OQU80715.1};
GN ORFNames=SORBI_3007G170300 {ECO:0000313|EMBL:OQU80715.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU80715.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU80715.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM000766; OQU80715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5RBA0; -.
DR EnsemblPlants; OQU80715; OQU80715; SORBI_3007G170300.
DR Gramene; OQU80715; OQU80715; SORBI_3007G170300.
DR Proteomes; UP000000768; Chromosome 7.
DR ExpressionAtlas; A0A1Z5RBA0; baseline and differential.
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:SF102; -; 1.
DR PANTHER; PTHR10543; BETA-CAROTENE DIOXYGENASE; 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:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 300
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
FT BINDING 556
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR604294-1"
SQ SEQUENCE 564 AA; 61931 MW; 2AB3B9E2230E6950 CRC64;
MAACKLPTLC TAPTPYLYAS RRSAGQTIIS TAAASACHRC RASRRRIQAA GDCTKHSAWT
SIRHERWEGD LAIEGHIPAW LNGTYLRNGP GVWEVGDHAL DHVFDGYATL VRVYFQGARG
RATGAHRQIE SDAYKAAARA HGRRRPLMRM REFSQLCPSE PGTLLDRLRH VVGLVTGAGM
SDNANTAVLP LGDGRVVCLA DVTKSSVLVD PETLETVGKL RYADRLWCPV QCTHPVVTTT
TTTTTRAAAA AEVLMLHPDF ARRGYLVARM MAAGGTGSND RREVVGRVRC RGGTTPAWVH
SFAVTAKYIV VPEMPLRYSV ACLLMSELTP FYIMDWLPHS GSYMHVICRS TGNTVASVEV
PPFVAFHFIN AYEENGDDDD GVRPNAIIAD CCEYYADPAI IQALALHRLR SPETAKDFPD
SRIPLDGSAA MGELETVLDP EEHGRGVELS TINPDYVGKE YRYLYACTAR RPCNFFNALT
KMDLVEKETT SWHEEGTVPS EPFFVARPGA TNEDDGVVIS TASTMDGDGY VLLLDAATFK
EIARLRLPYG LPFGFHGCWI PDNN
//
