Skip Header

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

Q5RFB0

- ACY1_PONAB

UniProt

Q5RFB0 - ACY1_PONAB

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Aminoacylase-1

Gene

ACY1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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

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 Zn(2+) ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Zinc 1By similarity
Active sitei82 – 821By similarity
Metal bindingi113 – 1131Zinc 1By similarity
Metal bindingi113 – 1131Zinc 2By similarity
Active sitei147 – 1471Proton acceptorBy similarity
Metal bindingi148 – 1481Zinc 2By similarity
Metal bindingi175 – 1751Zinc 1By similarity
Metal bindingi373 – 3731Zinc 2By similarity

GO - Molecular functioni

  1. aminoacylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacylase-1 (EC:3.5.1.14)
Short name:
ACY-1
Alternative name(s):
N-acyl-L-amino-acid amidohydrolase
Gene namesi
Name:ACY1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 408407Aminoacylase-1PRO_0000274008Add
BLAST

Interactioni

Subunit structurei

Homodimer. Interacts with SPHK1.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5RFB0.
SMRiQ5RFB0. Positions 7-198, 321-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Phylogenomic databases

HOVERGENiHBG000982.
InParanoidiQ5RFB0.
KOiK14677.

Family and domain databases

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RFB0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE RARQLGLGCQ
60 70 80 90 100
KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK
110 120 130 140 150
DSEGYIYARG AQDMKCISIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG
160 170 180 190 200
GHQGMELFVQ RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS
210 220 230 240 250
TGRPGHASRF MEDTAAEKLH KVVSSILAFR EKEWQRLQSN PHLKEGSVTS
260 270 280 290 300
VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG
310 320 330 340 350
VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMKLTLEP EIMPAATDNR
360 370 380 390 400
YIRAVGIPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS

VPALPSES
Length:408
Mass (Da):45,969
Last modified:January 23, 2007 - v2
Checksum:iDA5F3D6468261C84
GO

Sequence cautioni

The sequence CAH89547.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857251 mRNA. Translation: CAH89547.1. Different initiation.
RefSeqiNP_001124673.1. NM_001131201.2.

Genome annotation databases

GeneIDi100171519.
KEGGipon:100171519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857251 mRNA. Translation: CAH89547.1 . Different initiation.
RefSeqi NP_001124673.1. NM_001131201.2.

3D structure databases

ProteinModelPortali Q5RFB0.
SMRi Q5RFB0. Positions 7-198, 321-408.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100171519.
KEGGi pon:100171519.

Organism-specific databases

CTDi 95.

Phylogenomic databases

HOVERGENi HBG000982.
InParanoidi Q5RFB0.
KOi K14677.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036696. ACY-1. 1 hit.
SUPFAMi SSF55031. SSF55031. 1 hit.
TIGRFAMsi TIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.

Entry informationi

Entry nameiACY1_PONAB
AccessioniPrimary (citable) accession number: Q5RFB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3