ID I8IKP6_ASPO3 Unreviewed; 404 AA.
AC I8IKP6;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase {ECO:0000256|ARBA:ARBA00012579, ECO:0000256|RuleBase:RU004395};
DE EC=4.6.1.12 {ECO:0000256|ARBA:ARBA00012579, ECO:0000256|RuleBase:RU004395};
GN ORFNames=Ao3042_04020 {ECO:0000313|EMBL:EIT79541.1};
OS Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT79541.1, ECO:0000313|Proteomes:UP000002812};
RN [1] {ECO:0000313|EMBL:EIT79541.1, ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|EMBL:EIT79541.1,
RC ECO:0000313|Proteomes:UP000002812};
RX PubMed=22933657; DOI=10.1128/EC.00160-12;
RA Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL Eukaryot. Cell 11:1178-1178(2012).
RN [2] {ECO:0000313|Proteomes:UP000002812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA Zhao G., Hou L., Wang C., Cao X.;
RT "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT RIB40 for soy-sauce fermentation.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; EC=4.6.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00000200,
CC ECO:0000256|RuleBase:RU004395};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 4/6. {ECO:0000256|ARBA:ARBA00004709}.
CC -!- SIMILARITY: Belongs to the IspD/TarI cytidylyltransferase family. IspD
CC subfamily. {ECO:0000256|ARBA:ARBA00009789}.
CC -!- SIMILARITY: Belongs to the IspF family.
CC {ECO:0000256|RuleBase:RU004395}.
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:EIT79541.1}.
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DR EMBL; AKHY01000126; EIT79541.1; -; Genomic_DNA.
DR AlphaFoldDB; I8IKP6; -.
DR HOGENOM; CLU_042800_2_5_1; -.
DR UniPathway; UPA00056; UER00095.
DR Proteomes; UP000002812; Unassembled WGS sequence.
DR GO; GO:0008685; F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0070567; F:cytidylyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd02516; CDP-ME_synthetase; 1.
DR CDD; cd00554; MECDP_synthase; 1.
DR Gene3D; 3.30.1330.50; 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase; 1.
DR HAMAP; MF_01520; IspDF; 1.
DR HAMAP; MF_00107; IspF; 1.
DR InterPro; IPR026596; IspD/F.
DR InterPro; IPR034683; IspD/TarI.
DR InterPro; IPR003526; MECDP_synthase.
DR InterPro; IPR020555; MECDP_synthase_CS.
DR InterPro; IPR036571; MECDP_synthase_sf.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR NCBIfam; TIGR00151; ispF; 1.
DR PANTHER; PTHR43181; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43181:SF1; 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF01128; IspD; 1.
DR Pfam; PF02542; YgbB; 1.
DR SUPFAM; SSF69765; IpsF-like; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS01350; ISPF; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229,
KW ECO:0000256|RuleBase:RU004395};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU004395};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 232..384
FT /note="2-C-methyl-D-erythritol 2,4-cyclodiphosphate
FT synthase"
FT /evidence="ECO:0000259|Pfam:PF02542"
SQ SEQUENCE 404 AA; 43753 MW; 4A5BB48594A418E1 CRC64;
MSSTHPTFGT VLVAAGTGTR AGNAKCSKVY RELAGETVIS RVVRAFRAWD PGHPIVIVRH
ENDAALLTNA IEGADGQVYE TVCEATRQAS VLEGLRFLSS LEQPPSHVLF HDAARPFIPP
SLLDKIRDGM REQPDVGIIL AIPVSDTIKS VAENGLYRAQ TPQAFLLPTA LKIHDQLAYD
TSIEYTDDQA YPSVSYKGEE KNMKLTYPTD FEQAERILQA KPRLPEVSIP DVRVGHGYDT
HRLIPATEII LCGVKIPHTS GLLGHSDADV GLHAVTNALL GRIGADDIGS RFSPSDPRWK
GASSDQFVRH ARKLVSDAGG VITHVDVSLI CERPKIGPHR DALKTSVARI LSLDKSRVSI
KAGTNEKVGF VGREEGIIGF ATVTAVFPGG VPQAEINPDY DTTY
//
