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 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591Proton acceptor1 Publication
Metal bindingi195 – 1951Zinc; catalytic
Metal bindingi197 – 1971Zinc; catalytic
Metal bindingi284 – 2841Zinc; catalytic
Sitei323 – 3231Transition state stabilizer

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi158 – 1581H → A: Reduces enzyme activity by 97%. 1 Publication
Mutagenesisi159 – 1591H → A: Abolishes enzyme activity.
Mutagenesisi323 – 3231Y → F: Reduces enzyme activity by 99%. 1 Publication

Chemistry

ChEMBLiCHEMBL1795187.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Acetylpolyamine aminohydrolasePRO_0000114737Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Chemistry

BindingDBiQ48935.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 43Combined sources
Helixi7 – 115Combined sources
Beta strandi17 – 193Combined sources
Beta strandi22 – 243Combined sources
Helixi31 – 4212Combined sources
Beta strandi47 – 493Combined sources
Helixi59 – 613Combined sources
Helixi65 – 8016Combined sources
Helixi105 – 1117Combined sources
Beta strandi113 – 1153Combined sources
Helixi124 – 14320Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi169 – 1713Combined sources
Helixi173 – 18311Combined sources
Beta strandi189 – 1935Combined sources
Beta strandi195 – 1973Combined sources
Helixi200 – 2067Combined sources
Beta strandi210 – 21910Combined sources
Helixi221 – 2233Combined sources
Helixi238 – 2403Combined sources
Beta strandi244 – 2496Combined sources
Helixi255 – 27218Combined sources
Beta strandi275 – 2817Combined sources
Beta strandi294 – 2963Combined sources
Helixi298 – 30912Combined sources
Beta strandi315 – 3195Combined sources
Helixi327 – 34014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ48935.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 1592Substrate binding

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
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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

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 11, 2015
This is version 61 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.