ISPE_MENPI
ID ISPE_MENPI Reviewed; 405 AA.
AC P56848;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic;
DE EC=2.7.1.148;
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase;
DE Short=CMK;
DE Flags: Precursor;
GN Name=ISPE; Synonyms=IPK;
OS Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Menthinae;
OC Mentha.
OX NCBI_TaxID=34256;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Black Mitcham;
RX PubMed=10570138; DOI=10.1073/pnas.96.24.13714;
RA Lange B.M., Croteau R.;
RT "Isopentenyl diphosphate biosynthesis via a mevalonate-independent pathway:
RT isopentenyl monophosphate kinase catalyzes the terminal enzymatic step.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13714-13719(1999).
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-
CC erythritol 2-phosphate + ADP + H(+); Xref=Rhea:RHEA:18437,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57823,
CC ChEBI:CHEBI:57919, ChEBI:CHEBI:456216; EC=2.7.1.148;
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an isopentenyl monophosphate
CC kinase. {ECO:0000305|PubMed:10570138}.
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DR EMBL; AF179283; AAF13866.1; -; mRNA.
DR EMBL; AJ249324; CAB65292.1; -; mRNA.
DR AlphaFoldDB; P56848; -.
DR SMR; P56848; -.
DR BRENDA; 2.7.4.26; 3222.
DR UniPathway; UPA00056; UER00094.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR HAMAP; MF_00061; IspE; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR004424; IspE.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43527:SF2; PTHR43527:SF2; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00154; ispE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Plastid; Transferase; Transit peptide.
FT TRANSIT 1..97
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 98..405
FT /note="4-diphosphocytidyl-2-C-methyl-D-erythritol kinase,
FT chloroplastic"
FT /id="PRO_0000016481"
FT BINDING 190..200
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 44603 MW; D9AD576811F654D2 CRC64;
MASSSHFLYS HHHSYASYNS KSHFNSFTNA TFPQFSSFKP NGSSSFRKKL QSSRIHIIRA
AASDPTTGRN QLEVVYDLEN KLNKLADEVD REAGISRLTL FSPCKINVFL RITGKREDGF
HDLASLFHVI SLGDKIKFSL SPSKFNGSFV TNVPGVPLDE KNLIIKALNL FRKKTGTDKH
FWIHLDKKVP TGAGLGGGSS NAATALWAAN QFSGCIATEK DLQEWSGEIG SDIPFFFSHG
AAYCTGRGEV VEDIPPPVPR DLSMVLMKPQ EACPTGEVYK RLRLDQTSDI DPLVLLEKIS
KGGISQDVCV NDLEPPAFEV VPSLKRLKQR IAAAGRSQYD AVFMSGSGST IVGVGSPDPP
QFVYDGDEYK NIFFSEAKFI TRSANQWYSE PLSTDESPSF PQDAE