SUPERFAMILY 1.75 HMM library and genome assignments server

SUPERFAMILY 2 can be accessed from supfam.org. Please contact us if you experience any problems.


Dihydropteroate synthetase-like superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   Alpha and beta proteins (a/b) [ 51349] (147)
Fold:   TIM beta/alpha-barrel [ 51350] (33)
Superfamily:   Dihydropteroate synthetase-like [ 51717] (2)
Families:   Dihydropteroate synthetase [ 51718]
  Methyltetrahydrofolate-utiluzing methyltransferases [ 51723] (2)


Superfamily statistics
Genomes (2,905) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 6,520 54,052 6
Proteins 6,502 53,983 6


Functional annotation
General category Metabolism
Detailed category Coenzyme metabolism and transport

Document:
Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Oxidoreductases0Least InformativeDirect
Enzyme Commission (EC)Transferring one-carbon groups0.001444Least InformativeInherited
Enzyme Commission (EC)Methyltransferases0.000003249Moderately InformativeDirect
Enzyme Commission (EC)Transferring alkyl or aryl groups, other than meth1Moderately InformativeInherited
Enzyme Commission (EC)Acting on CH or CH(2) groups0InformativeDirect
Enzyme Commission (EC)Diphosphotransferases0.0000000002027InformativeDirect
Enzyme Commission (EC)2-amino-4-hydroxy-6-hydroxymethyldihydropteridine 0Highly InformativeDirect
Enzyme Commission (EC)Methionine synthase0Highly InformativeDirect
Enzyme Commission (EC)(E)-4-hydroxy-3-methylbut-2-enyl-diphosphate synth0Highly InformativeDirect

Document: EC annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Oxidoreductases0Least InformativeDirect
Enzyme Commission (EC)Lyases1Least InformativeInherited
Enzyme Commission (EC)Transferring phosphorus-containing groups1Least InformativeInherited
Enzyme Commission (EC)Transferring one-carbon groups0.00000198Moderately InformativeDirect
Enzyme Commission (EC)Carbon-carbon lyases1Moderately InformativeInherited
Enzyme Commission (EC)Acting on CH or CH(2) groups0InformativeDirect
Enzyme Commission (EC)Transferring alkyl or aryl groups, other than methyl groups1InformativeInherited
Enzyme Commission (EC)With an iron-sulfur protein as acceptor0Highly InformativeDirect
Enzyme Commission (EC)Diphosphotransferases0.0000000000000129Highly InformativeDirect
Enzyme Commission (EC)Aldehyde-lyases0.006436Highly InformativeInherited

Document: EC annotation of SCOP domains

InterPro annotation
Cross references IPR011005 SSF51717 Protein matches
Abstract

All organisms require reduced folate cofactors for the synthesis of a variety of metabolites. The enzyme 7,8-dihydropteroate synthase (DHPS) catalyses the condensation of para-aminobenzoic acid (pABA) with 6-hydroxymethyl-7, 8-dihydropterin-pyrophosphate to form 7,8-dihydropteroate and pyrophosphate. DHPS is essential for the de novo synthesis of folate in prokaryotes, lower eukaryotes, and in plants, but is absent in mammals [PubMed11007651]. By contrast, higher vertebrates possess an active transport system that enables them to use dietary folates. DHPS is the target of sulphonamides, which are substrate analogues that compete with pABA, but which do not affect vertebrates as they lack the DHPS enzyme. DHPS is a single domain protein that forms an eight-stranded TIM alpha/beta barrel, where the 7,8-dihydropterin pyrophosphate substrate binds in a deep cleft in the barrel [PubMed9187658]. In the lower eukaryote Pneumocystis carinii, DHPS is the C-terminal domain of a multifunctional folate synthesis enzyme (gene fas) [PubMed1313386].

Other proteins contain a DHPS-like domain, including members of the methyltetrahydrofolate (corrinoid iron-sulphur protein methyltransferase (MeTr)) family. MeTr catalyses a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation [PubMed10997901]. Other members of this family that contain a DHPS-like domain include methionine synthase and methanogenic enzymes that activate the methyl group of methyltetrahydromethano(or -sarcino)pterin.


InterPro database


PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Enzyme Commission (EC) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.


Alignments of sequences to 13 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.


Browse and view proteins in genomes which have different domain combinations including a Dihydropteroate synthetase-like domain.


Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.


Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 13 hidden Markov models representing the Dihydropteroate synthetase-like superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.


Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Enzyme Commission (EC) · Internal database links ]