ID J4CDD2_THEOR Unreviewed; 382 AA.
AC J4CDD2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000313|EMBL:BAM40937.1};
GN ORFNames=TOT_030000198 {ECO:0000313|EMBL:BAM40937.1};
OS Theileria orientalis strain Shintoku.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Piroplasmida;
OC Theileriidae; Theileria.
OX NCBI_TaxID=869250 {ECO:0000313|EMBL:BAM40937.1, ECO:0000313|Proteomes:UP000003786};
RN [1] {ECO:0000313|EMBL:BAM40937.1, ECO:0000313|Proteomes:UP000003786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shintoku {ECO:0000313|EMBL:BAM40937.1,
RC ECO:0000313|Proteomes:UP000003786};
RX PubMed=22951932;
RA Hayashida K., Hara Y., Abe T., Yamasaki C., Toyoda A., Kosuge T.,
RA Suzuki Y., Sato Y., Kawashima S., Katayama T., Wakaguri H., Inoue N.,
RA Homma K., Tada-Umezaki M., Yagi Y., Fujii Y., Habara T., Kanehisa M.,
RA Watanabe H., Ito K., Gojobori T., Sugawara H., Imanishi T., Weir W.,
RA Gardner M., Pain A., Shiels B., Hattori M., Nene V., Sugimoto C.;
RT "Comparative genome analysis of three eukaryotic parasites with differing
RT abilities to transform leukocytes reveals key mediators of Theileria-
RT induced leukocyte transformation.";
RL MBio 3:e00204-e00212(2012).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AP011948; BAM40937.1; -; Genomic_DNA.
DR RefSeq; XP_009691238.1; XM_009692943.1.
DR AlphaFoldDB; J4CDD2; -.
DR STRING; 869250.J4CDD2; -.
DR EnsemblProtists; BAM40937; BAM40937; TOT_030000198.
DR GeneID; 20715392; -.
DR KEGG; tot:TOT_030000198; -.
DR VEuPathDB; PiroplasmaDB:TOT_030000198; -.
DR eggNOG; ENOG502QPIQ; Eukaryota.
DR OrthoDB; 226678at2759; -.
DR Proteomes; UP000003786; Chromosome 3.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:InterPro.
DR CDD; cd13944; lytB_ispH; 1.
DR Gene3D; 3.40.50.11270; -; 1.
DR Gene3D; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 2.
DR HAMAP; MF_00191; IspH; 1.
DR InterPro; IPR003451; LytB/IspH.
DR NCBIfam; TIGR00216; ispH_lytB; 1.
DR PANTHER; PTHR30426; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR PANTHER; PTHR30426:SF0; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF02401; LYTB; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003786};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..382
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003778718"
SQ SEQUENCE 382 AA; 42568 MW; 1AD5E0FD985220FC CRC64;
MFTYVLYSCL AVYLTSSLAV YGRIAGRSQA GCKIGFNRRL TAFITPKTHD YRHILRAAER
ETTSDKKLYL VNPRGFCEGV SRAIRTVEET VRIFGPPIYV KHEIVHNEAV CNRLRAKGVV
FIEDLNLVPE NSIIIYSAHG ISPEIRELAK SRNLVEIDAS CPLVNKVHVY VKNKAKEGYK
IVLIGHKNHQ EIIGTSGEAP EAVTVVENVS DVQALDFPTD TKLFYVTQTT LSLDDCKHIK
DALVAKYPHI ETIPSGSICY ATTNRQTAIH KVTKLVDMVL IVGSKLSSNA KRLVEAALNR
DVKSYLVFDA DDVTEELVGS ARNIALSSSA STPEDLTQAV MDKLSSPPFN FVVEEFDGAV
ERVPNWRLPR YFMFAPVTYN NV
//
