Reviewed, UniProtKB/Swiss-Prot P37112 (AMAA_BACST)

Names and origin

Protein names

Recommended name:
    N-acyl-L-amino acid amidohydrolase
      Short name=L-aminoacylase
    EC=3.5.1.14

Gene names

Name:	amaA
Synonyms:	ama

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes most efficiently N-acetyl derivatives of aromatic amino acids but is also active on other amino acids. L-stereospecific.
Catalytic activity	An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid.
Cofactor	Cobalt.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the peptidase M20 family.

Ontologies

Keywords
Ligand	Cobalt
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	aminoacylase activity Inferred from electronic annotation. Source: EC cobalt ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: InterPro protein dimerization 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 – 370	370	N-acyl-L-amino acid amidohydrolase		PRO_0000061949

Sequences

	Sequence		Length	Mass (Da)
	P37112-1 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 479AF1559DB527FB	FASTA	370	41,676
	10 20 30 40 50 60 MTKEEIKRLV DEVKTDVIAW RRHLHAHPEL SFQEEKTAQF VYETLQSFGH LELSRPTKTS 70 80 90 100 110 120 VMARLIGQQP GRVVAIRADM DALPIQEENT FEFASKNPGV MHACGHDGHT AMLLGTAKIF 130 140 150 160 170 180 SQLRDDIRGE IRFLFQHAEE LFPGGAEEMV QAGVMDGVDV VIGTHLWSPL ERGKIGIVYG 190 200 210 220 230 240 PMMAAPDRFF IRIIGKGGHG AMPHQTIDAI AIGAQVVTNL QHIVSRYVDP LEPLVLSVTQ 250 260 270 280 290 300 FVAGTAHNVL PGEVEIQGTV RTFDETLRRT VPQWMERIVK GITEAHGASY EFRFDYGYRP 310 320 330 340 350 360 VINYDEGDPR HGGNGVRAVR RRGSGPLETE HGRRRFLRLF AKSARQLFLR RRGQCRKRHR 370 LPAPPPALYD

References

[1]

"Gene cloning, sequence analysis, purification, and characterization of a thermostable aminoacylase from Bacillus stearothermophilus." Sakanyan V., Desmarez L., Legrain C., Charlier D.R.M., Mett I., Kochikyan A., Savchenko A., Boyen A., Falmagne P., Pirard A., Glansdorff N. Appl. Environ. Microbiol. 59:3878-3888(1993) [PubMed: 8285691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION. Strain: NCIB 8224 / CCM 2186.

[2]

"Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus." Batisse N., Weigel P., Lecocq M., Sakanyan V. Appl. Environ. Microbiol. 63:763-766(1997) [PubMed: 9023955] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCIB 8224 / CCM 2186.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X74289 Genomic DNA. Translation: CAA52342.1. Y08753 Genomic DNA. Translation: CAA70000.1.
PIR	I40358.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.1.14. 266715.
Family and domain databases
InterPro	IPR017439. Pept_M20D_AA028/carboxypep-Ss1. IPR010168. Pept_M20D_amidohydro. IPR002933. Peptidase_M20. IPR011650. Peptidase_M20_dimer. [Graphical view]
Pfam	PF07687. M20_dimer. 1 hit. PF01546. Peptidase_M20. 1 hit. [Graphical view]
PIRSF	PIRSF005962. Pept_M20D_amidohydro. 1 hit.
TIGRFAMs	TIGR01891. amidohydrolases. 1 hit.
ProtoNet	Search...

Entry information

Entry name

AMAA_BACST

Accession

Primary (citable) accession number: P37112

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)