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Protein

Aminoacylase-1B

Gene

Acy1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).1 Publication

Catalytic activityi

An N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.
An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi80Zinc 1By similarity1
Active sitei82By similarity1
Metal bindingi113Zinc 1By similarity1
Metal bindingi113Zinc 2By similarity1
Active sitei147Proton acceptorBy similarity1
Metal bindingi148Zinc 2By similarity1
Metal bindingi175Zinc 1By similarity1
Metal bindingi373Zinc 2By similarity1

GO - Molecular functioni

  • aminoacylase activity Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • metallopeptidase activity Source: InterPro

GO - Biological processi

  • cellular amino acid metabolic process Source: InterPro
  • protein catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacylase-1B (EC:3.5.1.14)
Short name:
ACY-1B
Alternative name(s):
ACY IB
N-acyl-L-amino-acid amidohydrolase
Gene namesi
Name:Acy1b
Synonyms:Acy1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2030. Acy1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002740101 – 408Aminoacylase-1BAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei408PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ6PTT0.

PTM databases

iPTMnetiQ6PTT0.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6PTT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Phylogenomic databases

HOVERGENiHBG000982.
PhylomeDBiQ6PTT0.

Family and domain databases

CDDicd05646. M20_AcylaseI_like. 1 hit.
Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF036696. ACY-1. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6PTT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ
60 70 80 90 100
KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK
110 120 130 140 150
DSEGYIYTRG AQDMKCVSIQ YLEAVKRLKV EGHRFPRTIH MTFVPDEEVG
160 170 180 190 200
GHQGMELFVQ RHEFHALRAG FALDEGLANP TDAFTVFYSE RSPWWVRVTS
210 220 230 240 250
TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS
260 270 280 290 300
VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEEQL QSWCQEAGEG
310 320 330 340 350
VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMTLTLEP EIFPAATDSR
360 370 380 390 400
YIRAVGIPAL GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS

VPALPGES
Length:408
Mass (Da):45,823
Last modified:July 5, 2004 - v1
Checksum:iF335317AF2574927
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY580165 mRNA. Translation: AAS90691.1.
UniGeneiRn.3679.

Genome annotation databases

UCSCiRGD:2030. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY580165 mRNA. Translation: AAS90691.1.
UniGeneiRn.3679.

3D structure databases

ProteinModelPortaliQ6PTT0.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ6PTT0.

Proteomic databases

PRIDEiQ6PTT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2030. rat.

Organism-specific databases

RGDi2030. Acy1.

Phylogenomic databases

HOVERGENiHBG000982.
PhylomeDBiQ6PTT0.

Family and domain databases

CDDicd05646. M20_AcylaseI_like. 1 hit.
Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF036696. ACY-1. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACY1B_RAT
AccessioniPrimary (citable) accession number: Q6PTT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: October 5, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  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.