位置:首页 > 蛋白库 > ISPD_GLOVI
ISPD_GLOVI
ID   ISPD_GLOVI              Reviewed;         233 AA.
AC   Q7NGU6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000255|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000255|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000255|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000255|HAMAP-Rule:MF_00108}; OrderedLocusNames=glr2791;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
CC   -!- FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-
CC       erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
CC       {ECO:0000255|HAMAP-Rule:MF_00108}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-
CC         methyl-D-erythritol + diphosphate; Xref=Rhea:RHEA:13429,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC         ChEBI:CHEBI:57823, ChEBI:CHEBI:58262; EC=2.7.7.60;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00108};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 2/6. {ECO:0000255|HAMAP-Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00108}.
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; BA000045; BAC90732.1; -; Genomic_DNA.
DR   RefSeq; NP_925737.1; NC_005125.1.
DR   RefSeq; WP_011142785.1; NC_005125.1.
DR   AlphaFoldDB; Q7NGU6; -.
DR   SMR; Q7NGU6; -.
DR   STRING; 251221.35213360; -.
DR   EnsemblBacteria; BAC90732; BAC90732; BAC90732.
DR   KEGG; gvi:glr2791; -.
DR   PATRIC; fig|251221.4.peg.2820; -.
DR   eggNOG; COG1211; Bacteria.
DR   HOGENOM; CLU_061281_1_0_3; -.
DR   InParanoid; Q7NGU6; -.
DR   OMA; ERQHSVY; -.
DR   OrthoDB; 1836139at2; -.
DR   PhylomeDB; Q7NGU6; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000000557; Chromosome.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02516; CDP-ME_synthetase; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   PROSITE; PS01295; ISPD; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..233
FT                   /note="2-C-methyl-D-erythritol 4-phosphate
FT                   cytidylyltransferase"
FT                   /id="PRO_0000075577"
FT   SITE            13
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            20
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            153
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
FT   SITE            209
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   233 AA;  24894 MW;  05C265F0A72C14E9 CRC64;
     MHLLIPAAGR GSRMGADGNK LLLPLSGRPL LAWTLAAAAQ APSTRWIGII GQPMDEEAIR
     LLAQKLGLRV PVHWIEGGET RQQSVYRGLL ALPVEAQQVL IHDGARCLAS PALFERCAAA
     LAEFSAIVAA VPVKDTIKQV YPQSRQVEKT IPREQLWAAQ TPQGGNVGRL KAAHAWAAAQ
     AVAVTDDAAL CELRGEPVQV VPGEETNLKI TTPADLLVAE AILKTQLRQD PSP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024