flavodoxin/ferredoxin-dependent (E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synthase converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, part of an alternative non-mevalonate pathway for isoprenoid biosynthesis
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
5-358
0e+00
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis
:
Pssm-ID: 440583 [Multi-domain] Cd Length: 363 Bit Score: 649.41 E-value: 0e+00
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
5-358
0e+00
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440583 [Multi-domain] Cd Length: 363 Bit Score: 649.41 E-value: 0e+00
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids ...
12-353
0e+00
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids are synthesized by the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the terminal biosynthetic steps of the MEP pathway have not been fully elucidated. GcpE gene of Escherichia coli is involved in this pathway.
Pssm-ID: 428003 [Multi-domain] Cd Length: 343 Bit Score: 612.80 E-value: 0e+00
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown ...
9-351
2.25e-170
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown biochemical function has now been identified as an enzyme of the non-mevalonate pathway of IPP biosynthesis. Chlamydial members of the family have a long insert. The family is largely restricted to Bacteria, where it is widely but not universally distributed. No homology can be detected between the GcpE family and other proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273174 [Multi-domain] Cd Length: 346 Bit Score: 478.84 E-value: 2.25e-170
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
22-84
1.76e-03
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 39.86 E-value: 1.76e-03
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism] ...
5-358
0e+00
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE [Lipid transport and metabolism]; 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase IspG/GcpE is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440583 [Multi-domain] Cd Length: 363 Bit Score: 649.41 E-value: 0e+00
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids ...
12-353
0e+00
GcpE protein; In a variety of organizms, including plants and several eubacteria, isoprenoids are synthesized by the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway. Although different enzymes of this pathway have been described, the terminal biosynthetic steps of the MEP pathway have not been fully elucidated. GcpE gene of Escherichia coli is involved in this pathway.
Pssm-ID: 428003 [Multi-domain] Cd Length: 343 Bit Score: 612.80 E-value: 0e+00
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown ...
9-351
2.25e-170
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase; This protein of previously unknown biochemical function has now been identified as an enzyme of the non-mevalonate pathway of IPP biosynthesis. Chlamydial members of the family have a long insert. The family is largely restricted to Bacteria, where it is widely but not universally distributed. No homology can be detected between the GcpE family and other proteins. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273174 [Multi-domain] Cd Length: 346 Bit Score: 478.84 E-value: 2.25e-170
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
22-84
1.76e-03
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.
Pssm-ID: 239201 [Multi-domain] Cd Length: 327 Bit Score: 39.86 E-value: 1.76e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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