(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBV6_SEGRD

ID   D6ZBV6_SEGRD            Unreviewed;       402 AA.
AC   D6ZBV6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Bifunctional enzyme IspD/IspF {ECO:0000256|HAMAP-Rule:MF_01520};
DE   Includes:
DE     RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520};
DE              EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_01520};
DE     AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_01520};
DE     AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_01520};
DE              Short=MCT {ECO:0000256|HAMAP-Rule:MF_01520};
DE   Includes:
DE     RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|HAMAP-Rule:MF_01520};
DE              Short=MECDP-synthase {ECO:0000256|HAMAP-Rule:MF_01520};
DE              Short=MECPP-synthase {ECO:0000256|HAMAP-Rule:MF_01520};
DE              Short=MECPS {ECO:0000256|HAMAP-Rule:MF_01520};
DE              EC=4.6.1.12 {ECO:0000256|HAMAP-Rule:MF_01520};
GN   Name=ispDF {ECO:0000256|HAMAP-Rule:MF_01520};
GN   OrderedLocusNames=Srot_0446 {ECO:0000313|EMBL:ADG96933.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96933.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96933.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Bifunctional enzyme that catalyzes the formation of 4-
CC       diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-
CC       D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the
CC       conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-
CC       phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-
CC       cyclodiphosphate (ME-CPP) with a corresponding release of cytidine
CC       5-monophosphate (CMP) (IspF). {ECO:0000256|HAMAP-Rule:MF_01520,
CC       ECO:0000256|SAAS:SAAS00771987}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-
CC         2-C-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:0000256|HAMAP-Rule:MF_01520,
CC         ECO:0000256|SAAS:SAAS01130198};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-
CC         erythritol 2,4-cyclic diphosphate + CMP; Xref=Rhea:RHEA:23864,
CC         ChEBI:CHEBI:57919, ChEBI:CHEBI:58483, ChEBI:CHEBI:60377;
CC         EC=4.6.1.12; Evidence={ECO:0000256|HAMAP-Rule:MF_01520,
CC         ECO:0000256|SAAS:SAAS01115720};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01520,
CC         ECO:0000256|SAAS:SAAS01078176};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 2/6. {ECO:0000256|HAMAP-
CC       Rule:MF_01520, ECO:0000256|SAAS:SAAS01130190}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via DXP pathway; isopentenyl diphosphate from 1-
CC       deoxy-D-xylulose 5-phosphate: step 4/6. {ECO:0000256|HAMAP-
CC       Rule:MF_01520, ECO:0000256|SAAS:SAAS01078193}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the IspF family.
CC       {ECO:0000256|HAMAP-Rule:MF_01520, ECO:0000256|SAAS:SAAS00771954}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the IspD/TarI
CC       cytidylyltransferase family. IspD subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01520, ECO:0000256|SAAS:SAAS00771938}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01520}.
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DR   EMBL; CP001958; ADG96933.1; -; Genomic_DNA.
DR   RefSeq; WP_013137389.1; NC_014168.1.
DR   STRING; 640132.Srot_0446; -.
DR   EnsemblBacteria; ADG96933; ADG96933; Srot_0446.
DR   KEGG; srt:Srot_0446; -.
DR   eggNOG; ENOG4108UH8; Bacteria.
DR   eggNOG; COG0245; LUCA.
DR   eggNOG; COG1211; LUCA.
DR   HOGENOM; HOG000252034; -.
DR   KO; K12506; -.
DR   OMA; CGAGDIG; -.
DR   OrthoDB; 525632at2; -.
DR   BioCyc; SROT640132:G1GLH-446-MONOMER; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   CDD; cd00554; MECDP_synthase; 1.
DR   Gene3D; 3.30.1330.50; -; 1.
DR   Gene3D; 3.90.550.10; -; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   HAMAP; MF_01520; IspDF; 1.
DR   HAMAP; MF_00107; IspF; 1.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR026596; IspD/F.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR018294; ISPD_synthase_CS.
DR   InterPro; IPR003526; MECDP_synthase.
DR   InterPro; IPR020555; MECDP_synthase_CS.
DR   InterPro; IPR036571; MECDP_synthase_sf.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF01128; IspD; 1.
DR   Pfam; PF02542; YgbB; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   SUPFAM; SSF69765; SSF69765; 1.
DR   TIGRFAMs; TIGR00453; ispD; 1.
DR   TIGRFAMs; TIGR00151; ispF; 1.
DR   PROSITE; PS01295; ISPD; 1.
DR   PROSITE; PS01350; ISPF; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBV6.
DR   SWISS-2DPAGE; D6ZBV6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_01520,
KW   ECO:0000256|SAAS:SAAS01078191};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01520,
KW   ECO:0000256|SAAS:SAAS01078177};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01520,
KW   ECO:0000256|SAAS:SAAS01078178};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01520,
KW   ECO:0000256|SAAS:SAAS00771957};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01520,
KW   ECO:0000256|SAAS:SAAS00981526, ECO:0000313|EMBL:ADG96933.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01520,
KW   ECO:0000256|SAAS:SAAS00981527, ECO:0000313|EMBL:ADG96933.1}.
FT   DOMAIN      241    390       YgbB. {ECO:0000259|Pfam:PF02542}.
FT   REGION        1    240       2-C-methyl-D-erythritol 4-phosphate
FT                                cytidylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_01520}.
FT   REGION      241    402       2-C-methyl-D-erythritol 2,4-
FT                                cyclodiphosphate synthase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   REGION      247    249       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01520}.
FT   REGION      273    274       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01520}.
FT   REGION      277    285       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01520}.
FT   REGION      295    297       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01520}.
FT   REGION      367    371       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01520}.
FT   METAL       247    247       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   METAL       249    249       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   METAL       281    281       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   BINDING     378    378       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01520}.
FT   SITE         16     16       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   SITE         29     29       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   SITE        156    156       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_01520}.
FT   SITE        213    213       Positions MEP for the nucleophilic
FT                                attack. {ECO:0000256|HAMAP-Rule:
FT                                MF_01520}.
FT   SITE        273    273       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
FT   SITE        369    369       Transition state stabilizer.
FT                                {ECO:0000256|HAMAP-Rule:MF_01520}.
SQ   SEQUENCE   402 AA;  40457 MW;  63F712395EEEDC10 CRC64;
     MGKVAAIIVA SGSGSRLGAV DEAGEPCPKA FVFVGGHSML ARSVSAAWRS GIVDEVVAVV
     PADRTAQARS AVDPRTRLVS GGATRTESVR AGLSQIAAAD VVLVHDAARA LAPAQLFRSV
     AEAVVAGHAA VVPAVGVADT VKEVGPDGSV VRTLDRSCLR GAQTPQGFAA DVLRQAHRGA
     VARDGASELD DAGLAELAGA RVTAVEGDPL AFKITTPEDL VLAEALARTT RGGAVETLLP
     RVGSGVDVHP IELGRPCWVA GLLFPESDGC AGHSDGDVAA HALVDAVLSA AGLGDLGTVF
     GVDRPQMRGA SGELLLTEAR KLVEQAGFVI GNAVVQVVGN TPRLGPRRVE AQELLSAILG
     APVSVAATTT DGLGLTGRGE GRAAVANALV YPASPRNAKI AG
//

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