NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
Nakagawa S.;
"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025;
DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan]
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.";
J. Biotechnol. 104:5-25(2003).

Comments

CATALYTIC ACTIVITY: An acylphosphate + H₂O = a carboxylate + phosphate.
SIMILARITY: Belongs to the acylphosphatase family.
SIMILARITY: Contains 1 acylphosphatase-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000036; BAB99459.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927154; CAF20403.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_694659.1; -.
YP_226304.1; -.

3D structure databases

HSSP

P30131; 1GXU. [HSSP ENTRY / PDB]

ModBase

Q8NNW4.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG2266-MON; -.

Ontologies

GO:0003998;	Molecular function: acylphosphatase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_01450; -; 1.
PBIL [Tree]

InterPro

IPR001792; Acylphosphatase.
Graphical view of domain structure.

PANTHER

PTHR10029; Acylphosphatase; 1.

Pfam

PF00708; Acylphosphatase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00112; ACYLPHPHTASE.

ProDom

PD001884; Acylphosphatase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00150; ACYLPHOSPHATASE_1; 1.
PS00151; ACYLPHOSPHATASE_2; FALSE_NEG.
PS51160; ACYLPHOSPHATASE_3; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q8NNW4.

Genome annotation databases

GeneID

1020019; -.
3343100; -.

GenomeReviews

BX927147_GR; cg2266.
BA000036_GR; Cgl2066.

KEGG

cgb:cg2266; -.
cgl:NCgl1987; -.

Phylogenomic databases

HOGENOM

Q8NNW4; -.

Genome annotation databases

CMR

Q8NNW4; Cgl2066.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 94`	`94`	`Acylphosphatase.`	`PRO_0000326691`
`DOMAIN`	`5 94`	`90`	`Acylphosphatase-like.`
`ACT_SITE`	`20 20`		`By similarity.`
`ACT_SITE`	`38 38`		`By similarity.`

Sequence information

Length: 94 AA [This is the length of the unprocessed precursor]

Molecular weight: 10663 Da [This is the MW of the unprocessed precursor]

CRC64: AD5EBB6DCBCD4EC7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEKVRLTAFV HGHVQGVGFR WWTTSQAREL KLAGSASNLS DGRVCVVAEG PQTQCEELLR 

        70         80         90 
RLKENPSSYR RPGHVDTVIE QWGEPRDVEG FVER

Q8NNW4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools