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UniProtKB - Q70I53 (HDAH_ALCSD)
Protein
Histone deacetylase-like amidohydrolase
Gene
hdaH
Organism
Alcaligenes sp. (strain DSM 11172) (Bordetella sp. (strain FB188))
Status
Functioni
Exhibits significant levels of protein deacetylase activity comparable to those of eukaryotic HDACs in assays both with fluorogenic peptidic substrates and acetate-radiolabeled histones. Accepts proteins with epsilon-acetylated lysine residues and tritiated-acetate-prelabeled chicken histones as substrates. The natural substrate protein is not yet known.
1 PublicationCofactori
Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication
Activity regulationi
Zinc, and cobalt and nickel at a lesser extent, are able to increase the catalytic activity (2.2-, 1.3- and 1.1-fold respectively) at concentrations of 1 mM. Higher concentrations have an inhibitory effect. Magnesium, manganese and calcium have no effect on activity at concentrations between 0 and 10 mM. At 100 mM, the catalytic activity is increased between 1.2- and 2.1-fold. Hydroxamates like TSA and SAHA inhibit the enzyme (PubMed:15060035). Is also inhibited by azobenzenes, stilbenes and arylazopyrazoles (PubMed:27756124).2 Publications
pH dependencei
Optimum pH is 8.0.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 143 | Proton donor/acceptorBy similarity | 1 | |
Metal bindingi | 180 | ZincCombined sources1 Publication | 1 | |
Metal bindingi | 182 | Zinc; via pros nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 268 | ZincCombined sources1 Publication | 1 | |
Sitei | 312 | Polarizes the scissile carbonyl of the substrateBy similarity | 1 |
GO - Molecular functioni
- hydrolase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
Keywordsi
Molecular function | Hydrolase |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.5.1.4, 236 3.5.1.98, 236 |
Names & Taxonomyi
Protein namesi | Recommended name: Histone deacetylase-like amidohydrolase (EC:3.5.1.-)Short name: HDAC-like amidohydrolase Short name: HDAH |
Gene namesi | Name:hdaH Synonyms:hdaH1 |
Organismi | Alcaligenes sp. (strain DSM 11172) (Bordetella sp. (strain FB188)) |
Taxonomic identifieri | 242601 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › |
Pathology & Biotechi
Chemistry databases
ChEMBLi | CHEMBL6017 |
DrugBanki | DB07553, 9,9,9-TRIFLUORO-8-OXO-N-PHENYLNONANAMIDE DB08505, methyl 4-bromo-N-[8-(hydroxyamino)-8-oxooctanoyl]-L-phenylalaninate |
DrugCentrali | Q70I53 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000114728 | 2 – 369 | Histone deacetylase-like amidohydrolaseAdd BLAST | 368 |
Interactioni
Subunit structurei
Homotetramer; dimer of dimers.
1 PublicationChemistry databases
BindingDBi | Q70I53 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q70I53 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q70I53 |
Family & Domainsi
Sequence similaritiesi
Belongs to the histone deacetylase family.Curated
Family and domain databases
Gene3Di | 3.40.800.20, 1 hit |
InterProi | View protein in InterPro IPR000286, His_deacetylse IPR023801, His_deacetylse_dom IPR037138, His_deacetylse_dom_sf IPR023696, Ureohydrolase_dom_sf |
Pfami | View protein in Pfam PF00850, Hist_deacetyl, 1 hit |
PRINTSi | PR01270, HDASUPER |
SUPFAMi | SSF52768, SSF52768, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q70I53-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MAIGYVWNTL YGWVDTGTGS LAAANLTARM QPISHHLAHP DTKRRFHELV
60 70 80 90 100
CASGQIEHLT PIAAVAATDA DILRAHSAAH LENMKRVSNL PTGGDTGDGI
110 120 130 140 150
TMMGNGGLEI ARLSAGGAVE LTRRVATGEL SAGYALVNPP GHHAPHNAAM
160 170 180 190 200
GFCIFNNTSV AAGYARAVLG MERVAILDWD VHHGNGTQDI WWNDPSVLTI
210 220 230 240 250
SLHQHLCFPP DSGYSTERGA GNGHGYNINV PLPPGSGNAA YLHAMDQVVL
260 270 280 290 300
HALRAYRPQL IIVGSGFDAS MLDPLARMMV TADGFRQMAR RTIDCAADIC
310 320 330 340 350
DGRIVFVQEG GYSPHYLPFC GLAVIEELTG VRSLPDPYHE FLAGMGGNTL
360
LDAERAAIEE IVPLLADIR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ580773 Genomic DNA Translation: CAE45336.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ580773 Genomic DNA Translation: CAE45336.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ZZ0 | X-ray | 1.60 | A/B/C/D | 1-369 | [»] | |
1ZZ1 | X-ray | 1.57 | A/B/C/D | 1-369 | [»] | |
1ZZ3 | X-ray | 1.76 | A/B/C/D | 1-369 | [»] | |
2GH6 | X-ray | 2.20 | A/B/C/D | 2-369 | [»] | |
2VCG | X-ray | 1.90 | A/B/C/D | 2-369 | [»] | |
5G17 | X-ray | 1.51 | A/B | 2-369 | [»] | |
5G1A | X-ray | 1.42 | A/B | 2-369 | [»] | |
5G1B | X-ray | 1.70 | A/B | 2-369 | [»] | |
5G1C | X-ray | 1.81 | A/B | 2-369 | [»] | |
5G3W | X-ray | 1.60 | A/B/C/D | 2-369 | [»] | |
6GJK | X-ray | 1.47 | A/B | 2-369 | [»] | |
SMRi | Q70I53 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Chemistry databases
BindingDBi | Q70I53 |
ChEMBLi | CHEMBL6017 |
DrugBanki | DB07553, 9,9,9-TRIFLUORO-8-OXO-N-PHENYLNONANAMIDE DB08505, methyl 4-bromo-N-[8-(hydroxyamino)-8-oxooctanoyl]-L-phenylalaninate |
DrugCentrali | Q70I53 |
Enzyme and pathway databases
BRENDAi | 3.5.1.4, 236 3.5.1.98, 236 |
Miscellaneous databases
EvolutionaryTracei | Q70I53 |
Family and domain databases
Gene3Di | 3.40.800.20, 1 hit |
InterProi | View protein in InterPro IPR000286, His_deacetylse IPR023801, His_deacetylse_dom IPR037138, His_deacetylse_dom_sf IPR023696, Ureohydrolase_dom_sf |
Pfami | View protein in Pfam PF00850, Hist_deacetyl, 1 hit |
PRINTSi | PR01270, HDASUPER |
SUPFAMi | SSF52768, SSF52768, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | HDAH_ALCSD | |
Accessioni | Q70I53Primary (citable) accession number: Q70I53 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 21, 2004 |
Last sequence update: | January 23, 2007 | |
Last modified: | June 2, 2021 | |
This is version 60 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families