We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - A8KRL3 (TENA_HELPX)
Protein
Aminopyrimidine aminohydrolase
Gene
tenA
Organism
Helicobacter pylori (Campylobacter pylori)
Status
Functioni
Catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds to give a hydroxymethylpyrimidine (HMP). Displays low activity on 4-amino-5-aminomethyl-2-methylpyrimidine as substrate, indicating that the enzyme may act on a different HMP precursor that may derive from the human stomach food assumption or processing. Is probably involved in thiamine biosynthesis. Does not display thiaminase II activity, as it is unable to hydrolyze thiamine.
1 PublicationMiscellaneous
H.pylori is expected to possess a reduced thiamine biosynthetic pathway. Some enzymes involved in de novo thiamine biosynthesis in other organisms, such as ThiO, ThiS and ThiG, are missing in this species. The very acidic environment of the stomach makes the accumulation of formylaminopyrimidine very unlikely because it is mainly a base-degraded derivative of thiamine; formylaminopyrimidine is the precursor identified in a thiamine salvage pathway in Bacillus species.1 PublicationCurated
Catalytic activityi
- 4-amino-5-aminomethyl-2-methylpyrimidine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + NH4+1 PublicationEC:3.5.99.21 Publication
Kineticsi
kcat is 1.7 min(-1) for the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine.1 Publication
- KM=58 µM for 4-amino-5-aminomethyl-2-methylpyrimidine1 Publication
pH dependencei
Activity is lost at pH 6.1 Publication
: thiamine diphosphate biosynthesis Pathwayi
This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 44 | SubstrateBy similarity | 1 | |
Active sitei | 135 | NucleophileBy similarity | 1 | |
Binding sitei | 139 | SubstrateBy similarity | 1 | |
Binding sitei | 165 | SubstrateBy similarity | 1 | |
Active sitei | 207 | Proton donorBy similarity | 1 |
GO - Molecular functioni
- thiaminase activity Source: UniProtKB-EC
GO - Biological processi
- thiamine biosynthetic process Source: UniProtKB-KW
- thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Hydrolase |
Biological process | Thiamine biosynthesis |
Enzyme and pathway databases
UniPathwayi | UPA00060 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:tenA1 Publication |
Organismi | Helicobacter pylori (Campylobacter pylori) |
Taxonomic identifieri | 210 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 47 | F → Y: Activity remains very low with 4-amino-5-aminomethyl-2-methylpyrimidine as substrate, and the catalytic efficiency is even decreased by 33-fold. | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000431514 | 1 – 217 | Aminopyrimidine aminohydrolaseAdd BLAST | 217 |
Interactioni
Subunit structurei
Homotetramer.
1 PublicationProtein-protein interaction databases
STRINGi | 1345592.CBOM010000005_gene576 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | A8KRL3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | A8KRL3 |
Family & Domainsi
Sequence similaritiesi
Belongs to the TenA family.Curated
Phylogenomic databases
eggNOGi | COG0819, Bacteria |
Family and domain databases
Gene3Di | 1.20.910.10, 1 hit |
InterProi | View protein in InterPro IPR016084, Haem_Oase-like_multi-hlx IPR004305, Thiaminase-2/PQQC IPR027574, Thiaminase_II |
Pfami | View protein in Pfam PF03070, TENA_THI-4, 1 hit |
SUPFAMi | SSF48613, SSF48613, 1 hit |
TIGRFAMsi | TIGR04306, salvage_TenA, 1 hit |
i Sequence
Sequence statusi: Complete.
A8KRL3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MQVSQYLYQN AQSIWGDCIS HPFVQGIGRG TLERDKFRFY IIQDYLFLLE
60 70 80 90 100
YAKVFALGVV KACDEAVMRE FSNAIQDILN NEMSIHNHYI RELQITQKEL
110 120 130 140 150
QNACPTLANK SYTSYMLAEG FKGSIKEVAA AVLSCGWSYL VIAQNLSQIP
160 170 180 190 200
NALEHAFYGH WIKGYSSKEF QACVNWNINL LDSLTLASSK QEIEKLKEIF
210
ITTSEYEYLF WDMAYQS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM900414 Genomic DNA Translation: CAP12589.1 |
RefSeqi | WP_001198306.1, NZ_BNAZ01000048.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM900414 Genomic DNA Translation: CAP12589.1 |
RefSeqi | WP_001198306.1, NZ_BNAZ01000048.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2RD3 | X-ray | 2.70 | A/D | 1-217 | [»] | |
3IBX | X-ray | 2.40 | A/D | 1-217 | [»] | |
SMRi | A8KRL3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 1345592.CBOM010000005_gene576 |
Phylogenomic databases
eggNOGi | COG0819, Bacteria |
Enzyme and pathway databases
UniPathwayi | UPA00060 |
Miscellaneous databases
EvolutionaryTracei | A8KRL3 |
Family and domain databases
Gene3Di | 1.20.910.10, 1 hit |
InterProi | View protein in InterPro IPR016084, Haem_Oase-like_multi-hlx IPR004305, Thiaminase-2/PQQC IPR027574, Thiaminase_II |
Pfami | View protein in Pfam PF03070, TENA_THI-4, 1 hit |
SUPFAMi | SSF48613, SSF48613, 1 hit |
TIGRFAMsi | TIGR04306, salvage_TenA, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TENA_HELPX | |
Accessioni | A8KRL3Primary (citable) accession number: A8KRL3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 7, 2015 |
Last sequence update: | December 4, 2007 | |
Last modified: | June 2, 2021 | |
This is version 37 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families