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P32400 (CSH_ARTSP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 62. 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-carbamoylsarcosine amidase
EC=3.5.1.59
Alternative name(s):
N-carbamoylsarcosine amidohydrolase
Short name=CSHase
OrganismArthrobacter sp.
Taxonomic identifier1667 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

N-carbamoylsarcosine + H2O = sarcosine + CO2 + NH3.

Cofactor

Binds 1 sulfate ion per subunit.

Pathway

Amine and polyamine degradation; creatinine degradation; sarcosine from creatinine: step 3/3.

Subunit structure

Homotetramer.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processcreatinine catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionN-carbamoylsarcosine amidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 264264N-carbamoylsarcosine amidase
PRO_0000079397

Sites

Active site1771Nucleophile

Secondary structure

1 ......................................... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32400 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 8A213B555EA5DCDC

FASTA26429,057
        10         20         30         40         50         60 
MTETSGTFND IEARLAAVLE EAFEAGTSIY NERGFKRRIG YGNRPAVIHI DLANAWTQPG 

        70         80         90        100        110        120 
HPFSCPGMET IIPNVQRINE AARAKGVPVF YTTNVYRNRD ASSGTNDMGL WYSKIPTETL 

       130        140        150        160        170        180 
PADSYWAQID DRIAPADGEV VIEKNRASAF PGTNLELFLT SNRIDTLIVT GATAAGCVRH 

       190        200        210        220        230        240 
TVEDAIAKGF RPIIPRETIG DRVPGVVQWN LYDIDNKFGD VESTDSVVQY LDALPQFEDT 

       250        260 
VPKTLSDPQP EVEAPADPVF AEQH

« Hide

References

[1]"Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0-A resolution."
Romao M.J., Turk D., Gomis-Rueth F.-X., Huber R.
J. Mol. Biol. 226:1111-1130(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 184 AND 232.
[2]"Crystallographic and fluorescence studies of ligand binding to N-carbamoylsarcosine amidohydrolase from Arthrobacter sp."
Zajc A., Romao M.J., Turk D., Huber R.
J. Mol. Biol. 263:269-283(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF COMPLEX WITH INHIBITORS.

Cross-references

Sequence databases

PIRS28969.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NBAX-ray2.00A/B/C/D1-264[»]
ProteinModelPortalP32400.
SMRP32400. Positions 7-259.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11021.
UniPathwayUPA00274; UER00397.

Family and domain databases

Gene3D3.40.50.850. 1 hit.
InterProIPR000868. Isochorismatase-like.
[Graphical view]
PfamPF00857. Isochorismatase. 1 hit.
[Graphical view]
SUPFAMSSF52499. Iscrsm_hydrolase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP32400.

Entry information

Entry nameCSH_ARTSP
AccessionPrimary (citable) accession number: P32400
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 3, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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