HAMAP rule MF_01963
General rule information
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Accession | MF_01963 |
Dates | 23-NOV-2011 (Created)
1-JUN-2023 (Last updated, Version 18) |
Name | MTAP |
Scope(s) |
Bacteria Archaea |
Template(s) | Q97W94 (MTAP_SACS2); Q8U4Q8 (MTAP_PYRFU); Q8U2I1 (PNPH_PYRFU); Q9HZK1 (MTIP_PSEAE); [ Recover all ] |
Triggered by |
case c? <OC:Bacteria> or <OC:Archaea>
HAMAP; MF_01963 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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case <FT:3=D-x-D> and <FT:7=S> and <FT:8=[AVMI]> | |
Identifier | MTAP |
Protein name | RecName: Full=S-methyl-5'-thioadenosine phosphorylase; EC=2.4.2.28; AltName: Full=5'-methylthioadenosine phosphorylase; Short=MTA phosphorylase; Short=MTAP; |
Gene name | Name=mtnP; |
else case <FT:3=N-x-A> and <FT:7=E> and <FT:8=[AVMI]> | |
Identifier | MTIP |
Protein name | RecName: Full=Probable S-methyl-5'-thioinosine phosphorylase; EC=2.4.2.44; AltName: Full=5'-methylthioinosine phosphorylase; Short=MTI phosphorylase; Short=MTIP; |
else case <FT:3=N-x-A> and <FT:7=E> and not <FT:8=[AVMI]> | |
Identifier | PNPH |
Protein name | RecName: Full=Probable 6-oxopurine nucleoside phosphorylase; EC=2.4.2.1; AltName: Full=Purine nucleoside phosphorylase; Short=PNP; |
else | |
Identifier | PNPH |
Protein name | RecName: Full=Purine nucleoside phosphorylase; Short=PNP; EC=2.4.2.1; |
end case |
Comments
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case <FT:3=D-x-D> and <FT:7=S> and <FT:8=[AVMI]> | |
FUNCTION | Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates. |
CATALYTIC ACTIVITY | Reaction=phosphate + S-methyl-5'-thioadenosine = adenine + S-methyl-5- thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:11852, ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:43474, ChEBI:CHEBI:58533; EC=2.4.2.28; |
PATHWAY | Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'- thioadenosine (phosphorylase route): step 1/1. |
SUBUNIT | Homohexamer. Dimer of a homotrimer. |
else case <FT:3=N-x-A> and <FT:7=E> and <FT:8=[AVMI]> | |
FUNCTION | Catalyzes the reversible phosphorylation of S-methyl-5'- thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine. |
CATALYTIC ACTIVITY | Reaction=phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl- 5-thio-alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:30643, ChEBI:CHEBI:17368, ChEBI:CHEBI:43474, ChEBI:CHEBI:48595, ChEBI:CHEBI:58533; EC=2.4.2.44; |
PATHWAY | Purine metabolism; purine nucleoside salvage. |
SUBUNIT | Homotrimer. |
MISCELLANEOUS | Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it has been shown that conserved amino acid substitutions in the substrate binding pocket convert the substrate specificity of this enzyme from 6-aminopurines to 6-oxopurines. |
else case <FT:3=N-x-A> and <FT:7=E> | |
FUNCTION | Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage. |
CATALYTIC ACTIVITY | Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; |
PATHWAY | Purine metabolism; purine nucleoside salvage. |
SUBUNIT | Homohexamer. Dimer of a homotrimer. |
MISCELLANEOUS | Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it has been shown that conserved amino acid substitutions in the substrate binding pocket convert the substrate specificity of this enzyme from 6-aminopurines to 6-oxopurines. |
else | |
FUNCTION | Purine nucleoside phosphorylase involved in purine salvage. |
CATALYTIC ACTIVITY | Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; |
PATHWAY | Purine metabolism; purine nucleoside salvage. |
SUBUNIT | Homohexamer. Dimer of a homotrimer. |
MISCELLANEOUS | Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it lacks several conserved amino acids in the substrate binding pocket that confer specificity towards MTA. |
end case | |
SIMILARITY | Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily. |
Keywords
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Gene Ontology
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case <FT:3=D-x-D> and <FT:7=S> and <FT:8=[AVI]> | |
GO:0017061; Molecular function:S-methyl-5-thioadenosine phosphorylase activity | |
GO:0019509; Biological process:L-methionine salvage from methylthioadenosine | |
else; https://www.ebi.ac.uk/QuickGO/term/else | |
GO:0016763; Molecular function:pentosyltransferase activity | |
GO:0006166; Biological process:purine ribonucleoside salvage | |
end case |
Cross-references
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Features
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From: MTAP_SACS2 (Q97W94) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 58 | 59 | /ligand="phosphate" /ligand_id="ChEBI:CHEBI:43474" |
R-[HN] | ||||||||
BINDING | 91 | 92 | /ligand="phosphate" /ligand_id="ChEBI:CHEBI:43474" |
[ST]-A | ||||||||
BINDING | 214 | 216 | /ligand="substrate" | [DN]-x-[DA] | ||||||||
BINDING | 16 | 16 | /ligand="phosphate" /ligand_id="ChEBI:CHEBI:43474" |
[ST] | ||||||||
BINDING | 190 | 190 | /ligand="substrate" | M | ||||||||
BINDING | 191 | 191 | /ligand="phosphate" /ligand_id="ChEBI:CHEBI:43474" |
[ST] | ||||||||
From: PNPH_PYRFU (Q8U2I1) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
SITE | 169 | 169 | /note="Important for substrate specificity" | [SE] | ||||||||
SITE | 223 | 223 | /note="Important for substrate specificity" |
Additional information
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Size range | 237-355 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |