ID A0A1Y3ULX1_9ACTN Unreviewed; 303 AA.
AC A0A1Y3ULX1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=4-diphosphocytidyl-2-C-methyl-D-erythritol kinase {ECO:0000256|ARBA:ARBA00017473, ECO:0000256|HAMAP-Rule:MF_00061};
DE Short=CMK {ECO:0000256|HAMAP-Rule:MF_00061};
DE EC=2.7.1.148 {ECO:0000256|ARBA:ARBA00012052, ECO:0000256|HAMAP-Rule:MF_00061};
DE AltName: Full=4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase {ECO:0000256|ARBA:ARBA00032554, ECO:0000256|HAMAP-Rule:MF_00061};
GN Name=ispE {ECO:0000256|HAMAP-Rule:MF_00061};
GN ORFNames=B5G20_00535 {ECO:0000313|EMBL:OUN48067.1};
OS Collinsella sp. An7.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC Coriobacteriaceae; Collinsella.
OX NCBI_TaxID=1965651 {ECO:0000313|EMBL:OUN48067.1, ECO:0000313|Proteomes:UP000195627};
RN [1] {ECO:0000313|Proteomes:UP000195627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An7 {ECO:0000313|Proteomes:UP000195627};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group
CC of 4-diphosphocytidyl-2C-methyl-D-erythritol. {ECO:0000256|HAMAP-
CC Rule:MF_00061}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_00061};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 3/6. {ECO:0000256|HAMAP-Rule:MF_00061}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. IspE subfamily.
CC {ECO:0000256|ARBA:ARBA00009684, ECO:0000256|HAMAP-Rule:MF_00061}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00061}.
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:OUN48067.1}.
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DR EMBL; NFHP01000001; OUN48067.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3ULX1; -.
DR OrthoDB; 3173073at2; -.
DR UniPathway; UPA00056; UER00094.
DR Proteomes; UP000195627; Unassembled WGS sequence.
DR GO; GO:0050515; F:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00154; ispE; 1.
DR PANTHER; PTHR43527; 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43527:SF2; 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE, CHLOROPLASTIC; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF010376; IspE; 1.
DR SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00061}; Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00061};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00061};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00061}.
FT DOMAIN 96..152
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 209..284
FT /note="GHMP kinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08544"
FT ACT_SITE 20
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT ACT_SITE 145
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ SEQUENCE 303 AA; 32449 MW; 7FAF065BDAEEB112 CRC64;
MSTSAHREPG RFLLISAPAK INLYLGVHNE KDERGYHRVD SVMTTLDLAD VIAIGPADEL
SVHTVPPSDF PMDQNSAYRA ARAMGEAFGR DANFAILIDK RIPQQAGLGG PSTDAAATIL
GIATYWGVDA RDPRLDEVAR SIGADVPFFL YGPPAFCDGA GDRVRELFRP LTGTPVALVR
ADGPGVSTVE AYRRFDENPP ALPPLEPLLD ALRLHDETQI FAHVANNLAP ASCELNPQMA
EALAWIREQP EVRAANVAGS GSTVFAVCTT QMAAEAIALA AQERGWWGYA ARMEKSGPFV
AAG
//
