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Database: UniProt
Entry: A0A241WDD6_9GAMM
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ID   A0A241WDD6_9GAMM        Unreviewed;       275 AA.
AC   A0A241WDD6;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=B9T34_01385 {ECO:0000313|EMBL:OTG92026.1};
OS   Acinetobacter sp. ANC 3813.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977873 {ECO:0000313|EMBL:OTG92026.1, ECO:0000313|Proteomes:UP000194864};
RN   [1] {ECO:0000313|EMBL:OTG92026.1, ECO:0000313|Proteomes:UP000194864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 3813 {ECO:0000313|EMBL:OTG92026.1,
RC   ECO:0000313|Proteomes:UP000194864};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
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: 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:OTG92026.1}.
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DR   EMBL; NEGK01000001; OTG92026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241WDD6; -.
DR   OrthoDB; 9809438at2; -.
DR   UniPathway; UPA00056; UER00094.
DR   Proteomes; UP000194864; 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};
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   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          84..140
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          205..255
FT                   /note="GHMP kinase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08544"
FT   ACT_SITE        9
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
FT   BINDING         91..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00061"
SQ   SEQUENCE   275 AA;  30497 MW;  10608C957125510B CRC64;
     MIRVSSPAKL NLFLHITGRR ADGYHELQSI FQLIDLSDWL EFTQTESSQI TIEGLSSVDL
     EQNLIYRAAQ MLLPYAKQPT GLNIRIEKNI PMGAGLGGGS SNAASTLIVL NKLWRCGLNT
     EQLAALGLKL GADVPIFVHG QNAWAEGIGE HLTFIDLDQK QYIVLKPDCF ISTQLLFSQK
     TLTRDTKPTK FCAYQLTPFS FGNNFEPVAR SLYPEVDEAM QYLDQFGTAK LTGTGACVFA
     EVTENMNVDD ILKNAPCKSY LVNSLAESPL RHFEV
//
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