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Q44185 (DCAS_RHIRD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-carbamoyl-D-amino acid hydrolase

EC=3.5.1.77
Alternative name(s):
D-N-alpha-carbamilase
OrganismRhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Taxonomic identifier358 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

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.

Subunit structure

Homotetramer.

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 304304N-carbamoyl-D-amino acid hydrolase
PRO_0000079801

Regions

Domain5 – 299295CN hydrolase

Sites

Active site471
Active site1271
Active site1721

Experimental info

Mutagenesis1291H → A, N or R: No activity. Ref.4
Mutagenesis1441H → A: 5% activity of wild-type. Ref.4
Mutagenesis2151H → A: 17% activity of wild-type. Ref.4
Sequence conflict2741V → L in AAB47607. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Q44185 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 02436D8CEF925211

FASTA30434,152
        10         20         30         40         50         60 
MTRQMILAVG QQGPIARAET REQVVGRLLD MLTNAASRGV NFIVFPELAL TTFFPRWHFT 

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

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

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

       250        260        270        280        290        300 
EGCMLLGHSC IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK AHRQPQHYGL 


IAEF 

« Hide

References

[1]"Identification, sequencing and mutagenesis of the gene for a D-carbamoylase from Agrobacterium radiobacter."
Buson A., Negro A., Grassato L., Tagliaro M., Basaglia M., Grandi C., Fontana A., Nuti M.P.
FEMS Microbiol. Lett. 145:55-62(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL B-11291.
[2]Grifantini R.
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NRRL B-11291.
[3]"Topological mapping of the cysteine residues of N-carbamyl-D-amino-acid amidohydrolase and their role in enzymatic activity."
Grifantini R., Pratesi C., Galli G., Grandi G.
J. Biol. Chem. 271:9326-9331(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Strain: NRRL B-11291.
[4]"Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft."
Wang W.-C., Hsu W.-H., Chien F.-T., Chen C.-Y.
J. Mol. Biol. 306:251-261(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), MUTAGENESIS OF HIS-129; HIS-144 AND HIS-215.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59376 Genomic DNA. Translation: AAB47607.1.
X91070 Genomic DNA. Translation: CAA62550.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FO6X-ray1.95A/B/C/D1-304[»]
2GGKX-ray2.30A/B/C/D1-304[»]
2GGLX-ray2.40A/B/C/D1-304[»]
ProteinModelPortalQ44185.
SMRQ44185. Positions 3-304.
ModBaseSearch...
MobiDBSearch...

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. SSF56317. 1 hit.
PROSITEPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ44185.

Entry information

Entry nameDCAS_RHIRD
AccessionPrimary (citable) accession number: Q44185
Secondary accession number(s): Q44203
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references