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Protein

Acetylpolyamine aminohydrolase

Gene

aphA

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

Functioni

Acts on many types of acetylpolyamines. Has high affinity towards acetylputrescine, acetylcadaverine, acetylspermidine, and acetylspermine. Acts on L-Lys-(epsilon-acetyl)-coumarin, but has very low activity towards acetylated peptides.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Enzyme regulationi

Inhibited by KCl at concentrations above 10 mM.

pH dependencei

Optimum pH is about 8.0.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei159Proton acceptor1 Publication1
Metal bindingi195Zinc; catalytic1
Metal bindingi197Zinc; catalytic1
Metal bindingi284Zinc; catalytic1
Sitei323Transition state stabilizer1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14060.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetylpolyamine aminohydrolase
Gene namesi
Name:aphA
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 aminohydrolaseAdd BLAST341

Interactioni

Subunit structurei

Homodimer.1 Publication

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 159Substrate binding2

Sequence similaritiesi

Belongs to the histone deacetylase family.Curated

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 2 hits.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
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.

Cross-referencesi

Sequence databases

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

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...

Chemistry databases

BindingDBiQ48935.
ChEMBLiCHEMBL1795187.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14060.

Miscellaneous databases

EvolutionaryTraceiQ48935.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 2 hits.
PfamiPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PRINTSiPR01270. HDASUPER.
ProtoNetiSearch...

Entry informationi

Entry nameiAPHA_MYCRA
AccessioniPrimary (citable) accession number: Q48935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

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.