Q6PTT0 (ACY1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aminoacylase-1B
Short name=ACY-1B
EC=3.5.1.14

Alternative name(s):
ACY IB
N-acyl-L-amino-acid amidohydrolase

Gene names

Name:	Acy1b
Synonyms:	Acy1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). Ref.1
Catalytic activity	An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the peptidase M20A family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro protein catabolic process Traceable author statement Ref.1. Source: RGD proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Inferred from direct assay Ref.1. Source: RGD
Molecular function	aminoacylase activity Inferred from direct assay Ref.1. Source: RGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 408	408	Aminoacylase-1B		PRO_0000274010
Sites
	Active site	82	1	By similarity
	Active site	147	1	Proton acceptor By similarity
	Metal binding	80	1	Zinc 1 By similarity
	Metal binding	113	1	Zinc 1 By similarity
	Metal binding	113	1	Zinc 2 By similarity
	Metal binding	148	1	Zinc 2 By similarity
	Metal binding	175	1	Zinc 1 By similarity
	Metal binding	373	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6PTT0 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: F335317AF2574927	FASTA	408	45,823
	10 20 30 40 50 60 MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV 70 80 90 100 110 120 TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYTRG AQDMKCVSIQ 130 140 150 160 170 180 YLEAVKRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RHEFHALRAG FALDEGLANP 190 200 210 220 230 240 TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN 250 260 270 280 290 300 PHLKEGSVTS VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEEQL QSWCQEAGEG 310 320 330 340 350 360 VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMTLTLEP EIFPAATDSR YIRAVGIPAL 370 380 390 400 GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS VPALPGES

References

[1]	"The rat kidney acylase I, characterization and molecular cloning. Differences with other acylases I." Giardina T., Perrier J., Puigserver A. Eur. J. Biochem. 267:6249-6255(2000) [PubMed: 11012679] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 161-178, FUNCTION. Strain: Wistar. Tissue: Kidney.
[2]	"The rat kidney acylase 1. Evidence for a new cDNA form and comparisons with the porcine intestinal enzyme." Perrier J., Durand A., Giardina T., Puigserver A. Comp. Biochem. Physiol. 138B:277-283(2004) [PubMed: 15253876] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Wistar.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY580165 mRNA. Translation: AAS90691.1.
IPI	IPI00454539.
UniGene	Rn.3679.
3D structure databases
HSSP	HSSP built from PDB template 1Q7L based on UniProtKB Q03154.
ProteinModelPortal	Q6PTT0.
SMR	Q6PTT0. Positions 7-198, 321-408.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6PTT0.
Proteomic databases
PRIDE	Q6PTT0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
RGD	2030. Acy1.
Phylogenomic databases
GeneTree	ENSGT00530000063360.
HOVERGEN	HBG000982.
InParanoid	Q6PTT0.
Gene expression databases
ArrayExpress	Q6PTT0.
Genevestigator	Q6PTT0.
Family and domain databases
InterPro	IPR001261. ArgE/DapE_CS. IPR010159. N-acyl_aa_amidohydrolase. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF036696. ACY-1. 1 hit.
SUPFAM	SSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMs	TIGR01880. Ac-peptdase-euk. 1 hit.
PROSITE	PS00758. ARGE_DAPE_CPG2_1. 1 hit. PS00759. ARGE_DAPE_CPG2_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACY1B_RAT

Accession

Primary (citable) accession number: Q6PTT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	July 5, 2004
Last modified:	September 21, 2011
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program