Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acetylpolyamine amidohydrolase

Gene

aphA

Organism
Mycoplana ramosa (Mycoplana bullata)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in polyamine metabolism. Catalyzes the deacetylation of various acetylated polyamines such as N-acetylputrescine, N-acetylcadaverine, N1-acetylspermine, N1-acetylspermidine and N8-acetylspermidine (PubMed:8824626, PubMed:3207420). In vitro, is also able to deacetylate L-Lys(epsilon-acetyl)coumarin, but has very low activity towards the larger tetrapeptide N-acetyl-L-Arg-L-His-L-Lys(epsilon-acetyl)-L-Lys(epsilon-acetyl)coumarin (PubMed:21268586).3 Publications

Catalytic activityi

N-acetylputrescine + H2O = acetate + putrescine.2 Publications
N-acetylcadaverine + H2O = acetate + cadaverine.2 Publications
N1-acetylspermine + H2O = acetate + spermine.2 Publications
N1-acetylspermidine + H2O = acetate + spermidine.2 Publications
N8-acetylspermidine + H2O = acetate + spermidine.2 Publications

Cofactori

Zn2+1 Publication2 PublicationsNote: Binds 1 zinc ion per subunit.4 Publications

Enzyme regulationi

Zinc ions inhibit enzyme activity in a dose-dependent manner (PubMed:8824626). Inhibited by KCl at concentrations above 10 mM (PubMed:21268586). Inhibited by o-oxyquinoline in vitro, suggesting that it is a metalloprotein (PubMed:3207420). Inhibited by various substrate N8-acetylspermidine analogs bearing different metal-binding groups such as trifluoromethylketone, thiol, or hydroxamate, and by hydroxamate analogs of short-chain acetyldiamines (PubMed:26200446).4 Publications

Kineticsi

  1. KM=50 µM for N-acetylcadaverine1 Publication
  2. KM=220 µM for N-acetylputrescine1 Publication
  3. KM=130 µM for N1-acetylspermidine1 Publication
  4. KM=310 µM for N8-acetylspermidine1 Publication
  5. KM=290 µM for N1-acetylspermine1 Publication
  1. Vmax=27 µmol/min/mg enzyme with N-acetylcadaverine as substrate1 Publication
  2. Vmax=27 µmol/min/mg enzyme with N-acetylputrescine as substrate1 Publication
  3. Vmax=16.5 µmol/min/mg enzyme with N1-acetylspermidine as substrate1 Publication
  4. Vmax=17.2 µmol/min/mg enzyme with N8-acetylspermidine as substrate1 Publication
  5. Vmax=13.4 µmol/min/mg enzyme with N1-acetylspermine as substrate1 Publication

pH dependencei

Optimum pH is 9 with acetylputrescine, N1-acetylspermidine, and N8-acetylspermidine as substrates, and is 8 with acetylcadaverine as substrate.1 Publication

Pathwayi: Amine and polyamine metabolism

This protein is involved in Amine and polyamine metabolism.1 Publication
View all proteins of this organism that are known to be involved in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei19SubstrateCombined sources1 Publication1
Binding sitei106SubstrateCombined sources1 Publication1
Binding sitei117SubstrateCombined sources1 Publication1
Active sitei159Proton donor/acceptor2 Publications1
Metal bindingi195ZincCombined sources2 Publications1
Metal bindingi197Zinc; via pros nitrogenCombined sources2 Publications1
Metal bindingi284ZincCombined sources2 Publications1
Binding sitei323SubstrateCombined sources1 Publication1
Sitei323Polarizes the scissile carbonyl of the substrate1 Publication1

GO - Molecular functioni

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14060.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylpolyamine amidohydrolase2 Publications (EC:3.5.1.-2 Publications)
Short name:
APAH1 Publication
Alternative name(s):
Acetylcadaverine deacetylase1 Publication
Acetylpolyamine deacetylaseCurated
Acetylputrescine deacetylase1 Publication (EC:3.5.1.622 Publications)
Acetylspermidine deacetylase1 Publication (EC:3.5.1.482 Publications)
Gene namesi
Name:aphA1 Publication
Synonyms:aph
OrganismiMycoplana ramosa (Mycoplana bullata)
Taxonomic identifieri40837 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeMycoplana

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi158H → A: Reduces enzyme activity by 97%. 1 Publication1
Mutagenesisi159H → A: Abolishes enzyme activity. 1
Mutagenesisi323Y → F: Reduces enzyme activity by 99%. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1795187.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001147371 – 341Acetylpolyamine amidohydrolaseAdd BLAST341

Interactioni

Subunit structurei

Homodimer.2 Publications

Chemistry databases

BindingDBiQ48935.

Structurei

Secondary structure

1341
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 4Combined sources3
Helixi7 – 11Combined sources5
Beta strandi17 – 19Combined sources3
Beta strandi22 – 24Combined sources3
Helixi31 – 42Combined sources12
Beta strandi47 – 49Combined sources3
Helixi59 – 61Combined sources3
Helixi65 – 80Combined sources16
Helixi105 – 111Combined sources7
Beta strandi113 – 115Combined sources3
Helixi124 – 143Combined sources20
Beta strandi147 – 151Combined sources5
Beta strandi164 – 166Combined sources3
Beta strandi169 – 171Combined sources3
Helixi173 – 183Combined sources11
Beta strandi189 – 193Combined sources5
Beta strandi195 – 197Combined sources3
Helixi200 – 206Combined sources7
Beta strandi210 – 219Combined sources10
Helixi221 – 223Combined sources3
Helixi238 – 240Combined sources3
Beta strandi244 – 249Combined sources6
Helixi255 – 272Combined sources18
Beta strandi275 – 281Combined sources7
Beta strandi294 – 296Combined sources3
Helixi298 – 309Combined sources12
Beta strandi315 – 319Combined sources5
Helixi327 – 340Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3Q9BX-ray2.25A/B/C/D/E/F/G/H/I/J/K/L1-341[»]
3Q9CX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L1-341[»]
3Q9EX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L1-341[»]
3Q9FX-ray2.35A/B/C/D/E/F/G/H/I/J/K/L1-341[»]
4ZUMX-ray1.42A/B1-341[»]
4ZUNX-ray1.40A/B1-341[»]
4ZUOX-ray1.33A/B1-341[»]
4ZUPX-ray1.42A/B1-341[»]
4ZUQX-ray1.22A/B1-341[»]
4ZURX-ray1.13A/B1-341[»]
ProteinModelPortaliQ48935.
SMRiQ48935.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ48935.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone deacetylase family.Curated

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiView protein in InterPro
IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiView protein in Pfam
PF00850. Hist_deacetyl. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequencei

Sequence statusi: Complete.

Q48935-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRVIFSEDHK LRNAKTELYG GELVPPFEAP FRAEWILAAV KEAGFDDVVA
60 70 80 90 100
PARHGLETVL KVHDAGYLNF LETAWDRWKA AGYKGEAIAT SFPVRRTSPR
110 120 130 140 150
IPTDIEGQIG YYCNAAETAI SPGTWEAALS SMASAIDGAD LIAAGHKAAF
160 170 180 190 200
SLCRPPGHHA GIDMFGGYCF INNAAVAAQR LLDKGAKKIA ILDVDFHHGN
210 220 230 240 250
GTQDIFYERG DVFFASLHGD PAEAFPHFLG YAEETGKGAG AGTTANYPMG
260 270 280 290 300
RGTPYSVWGE ALTDSLKRIA AFGAEAIVVS LGVDTFEQDP ISFFKLTSPD
310 320 330 340
YITMGRTIAA SGVPLLVVME GGYGVPEIGL NVANVLKGVA G
Length:341
Mass (Da):36,332
Last modified:November 1, 1996 - v1
Checksum:i950583DF79059F4A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10463 Genomic DNA. Translation: BAA01256.1.
PIRiT48858.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiAPAH_MYCRA
AccessioniPrimary (citable) accession number: Q48935
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 10, 2017
This is version 66 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families