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P60327 (DCAS_AGRSK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
N-carbamoyl-D-amino acid hydrolase
EC=3.5.1.77
Alternative name(s):
D-N-alpha-carbamilase
OrganismAgrobacterium sp. (strain KNK712)
Taxonomic identifier252128 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length304 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme.

Catalytic activity

N-carbamoyl-D-amino acid + H2O = D-amino acid + NH3 + CO2.

Sequence similarities

Contains 1 CN hydrolase domain.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processnitrogen compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionN-carbamoyl-D-amino acid hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304N-carbamoyl-D-amino acid hydrolase
PRO_0000079800

Regions

Domain5 – 299295CN hydrolase

Sites

Active site471
Active site1271
Active site1721

Secondary structure

1 .............................................................. 304
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60327 [UniParc].

Last modified February 2, 2004. Version 1.
Checksum: C64290139C1C7E61

FASTA30434,285
        10         20         30         40         50         60 
MTRQMILAVG QQGPIARAET REQVVVRLLD MLTKAASRGA NFIVFPELAL TTFFPRWHFT 

        70         80         90        100        110        120 
DEAELDSFYE TEMPGPVVRP LFEKAAELGI GFNLGYAELV VEGGVKRRFN TSILVDKSGK 

       130        140        150        160        170        180 
IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF EPGDLGFPVY DVDAAKMGMF ICNDRRWPEA 

       190        200        210        220        230        240 
WRVMGLRGAE IICGGYNTPT HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME 

       250        260        270        280        290        300 
ENCMLLGHSC IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK QHRQPQHYGL 


IAEL

« Hide

References

[1]"Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme."
Nanba H., Ikenaka Y., Yamada Y., Yajima K., Takano M., Takahashi S.
Biosci. Biotechnol. Biochem. 62:875-881(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases."
Nakai T., Hasegawa T., Yamashita E., Yamamoto M., Kumasaka T., Ueki T., Nanba H., Ikenaka Y., Takahashi S., Sato M., Tsukihara T.
Structure 8:729-737(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB007368 Genomic DNA. Translation: BAD00007.1.
PIRJW0082.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ERZX-ray1.70A/B2-304[»]
1UF4X-ray2.15A/B2-304[»]
1UF5X-ray1.60A/B2-304[»]
1UF7X-ray1.90A/B2-304[»]
1UF8X-ray1.80A/B2-304[»]
ProteinModelPortalP60327.
SMRP60327. Positions 2-304.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.60.110.10. 1 hit.
InterProIPR003010. C-N_Hydrolase.
[Graphical view]
PfamPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMSSF56317. Ntlse/CNhydtse. 1 hit.
PROSITEPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP60327.

Entry information

Entry nameDCAS_AGRSK
AccessionPrimary (citable) accession number: P60327
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: April 3, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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