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Database: UniProt
Entry: A0A0Q7B2C8_9ACTN
LinkDB: A0A0Q7B2C8_9ACTN
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ID   A0A0Q7B2C8_9ACTN        Unreviewed;       475 AA.
AC   A0A0Q7B2C8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            EC=2.7.7.60 {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=4-diphosphocytidyl-2C-methyl-D-erythritol synthase {ECO:0000256|HAMAP-Rule:MF_00108};
DE   AltName: Full=MEP cytidylyltransferase {ECO:0000256|HAMAP-Rule:MF_00108};
DE            Short=MCT {ECO:0000256|HAMAP-Rule:MF_00108};
GN   Name=ispD {ECO:0000256|HAMAP-Rule:MF_00108};
GN   ORFNames=ASC77_17715 {ECO:0000313|EMBL:KQW47023.1};
OS   Nocardioides sp. Root1257.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736439 {ECO:0000313|EMBL:KQW47023.1, ECO:0000313|Proteomes:UP000051939};
RN   [1] {ECO:0000313|EMBL:KQW47023.1, ECO:0000313|Proteomes:UP000051939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1257 {ECO:0000313|EMBL:KQW47023.1,
RC   ECO:0000313|Proteomes:UP000051939};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW47023.1, ECO:0000313|Proteomes:UP000051939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1257 {ECO:0000313|EMBL:KQW47023.1,
RC   ECO:0000313|Proteomes:UP000051939};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00108}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|RuleBase:RU000363}.
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:KQW47023.1}.
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DR   EMBL; LMDV01000010; KQW47023.1; -; Genomic_DNA.
DR   RefSeq; WP_056156954.1; NZ_LMDV01000010.1.
DR   AlphaFoldDB; A0A0Q7B2C8; -.
DR   STRING; 1736439.ASC77_17715; -.
DR   UniPathway; UPA00056; UER00093.
DR   Proteomes; UP000051939; Unassembled WGS sequence.
DR   GO; GO:0050518; F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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; cd05233; SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00108; IspD; 1.
DR   InterPro; IPR012115; CDP-ribitol_syn.
DR   InterPro; IPR001228; IspD.
DR   InterPro; IPR034683; IspD/TarI.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR32125; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR32125:SF4; 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE, CHLOROPLASTIC; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF01128; IspD; 1.
DR   PIRSF; PIRSF036586; CDP-ribitol_syn; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00108};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00108}; Reference proteome {ECO:0000313|Proteomes:UP000051939};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00108}.
FT   SITE            19
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            26
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            158
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
FT   SITE            217
FT                   /note="Positions MEP for the nucleophilic attack"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00108"
SQ   SEQUENCE   475 AA;  50746 MW;  A77FAE807EBF10E7 CRC64;
     MSGPQKNVAV LLAGGVGVRV GLDVPKQLIK IAGHSIMEHT LAILDRHADV DEIIVMMAPG
     HLDAVHAMVR DGGYGKVTAI LEGAGTRNDT TLAALAALGD EDCKVLLHDA VRPLVSARII
     SDCFAALDTH DAVDVAIPSA DTIIEVGPDN TIRDIPPRSN LRRGQTPQAF KLSTIREAYR
     HAGEDPNFEA TDDCTVVLRY LPDVPIWVVP GDERNMKVTE PIDIYLADKL FQLTGNDAPA
     MRSDDAMRTA LAGKTMVVFG GSYGIGHDIA ELAASYGANV ASYSRSTTQT HVQRREDIAA
     AARDAVERFG SVDFVVNTAG VLPRGTLVEA SDETIYSATD INYIAPILIA QEFHSLLRET
     SGCLLLFTSS SYTRGRSGYS LYSSAKAATV NLTQALADEW AADKVRVNCI NPERTGTPMR
     TKAFGEEPAG SLLESTAVAK ASLEALVSGG TGHVIDLRRL DPLESLRLSD TVADL
//
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