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Protein

N-carbamoylsarcosine amidase

Gene
N/A
Organism
Arthrobacter sp.
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

sulfateNote: Binds 1 sulfate ion per subunit.

Pathway: creatinine degradation

This protein is involved in step 3 of the subpathway that synthesizes sarcosine from creatinine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. N-carbamoylsarcosine amidase
This subpathway is part of the pathway creatinine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes sarcosine from creatinine, the pathway creatinine degradation and in Amine and polyamine degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei177 – 1771Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11021.
UniPathwayiUPA00274; UER00397.

Names & Taxonomyi

Protein namesi
Recommended name:
N-carbamoylsarcosine amidase (EC:3.5.1.59)
Alternative name(s):
N-carbamoylsarcosine amidohydrolase
Short name:
CSHase
OrganismiArthrobacter sp.
Taxonomic identifieri1667 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264N-carbamoylsarcosine amidasePRO_0000079397Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 3325Combined sources
Beta strandi43 – 519Combined sources
Helixi54 – 574Combined sources
Beta strandi58 – 614Combined sources
Helixi68 – 8417Combined sources
Beta strandi89 – 946Combined sources
Helixi109 – 1135Combined sources
Helixi117 – 1193Combined sources
Helixi125 – 1273Combined sources
Helixi131 – 1333Combined sources
Beta strandi140 – 15011Combined sources
Helixi155 – 1617Combined sources
Beta strandi166 – 1727Combined sources
Turni174 – 1763Combined sources
Helixi177 – 18812Combined sources
Beta strandi191 – 1955Combined sources
Helixi196 – 1983Combined sources
Beta strandi202 – 2054Combined sources
Helixi206 – 21712Combined sources
Beta strandi220 – 2223Combined sources
Helixi224 – 23310Combined sources
Helixi237 – 2393Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NBAX-ray2.00A/B/C/D1-264[»]
ProteinModelPortaliP32400.
SMRiP32400. Positions 7-259.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32400.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.850. 1 hit.
InterProiIPR000868. Isochorismatase-like.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
[Graphical view]
SUPFAMiSSF52499. SSF52499. 1 hit.

Sequencei

Sequence statusi: Complete.

P32400-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTETSGTFND IEARLAAVLE EAFEAGTSIY NERGFKRRIG YGNRPAVIHI
60 70 80 90 100
DLANAWTQPG HPFSCPGMET IIPNVQRINE AARAKGVPVF YTTNVYRNRD
110 120 130 140 150
ASSGTNDMGL WYSKIPTETL PADSYWAQID DRIAPADGEV VIEKNRASAF
160 170 180 190 200
PGTNLELFLT SNRIDTLIVT GATAAGCVRH TVEDAIAKGF RPIIPRETIG
210 220 230 240 250
DRVPGVVQWN LYDIDNKFGD VESTDSVVQY LDALPQFEDT VPKTLSDPQP
260
EVEAPADPVF AEQH
Length:264
Mass (Da):29,057
Last modified:October 1, 1993 - v1
Checksum:i8A213B555EA5DCDC
GO

Sequence databases

PIRiS28969.

Cross-referencesi

Sequence databases

PIRiS28969.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NBAX-ray2.00A/B/C/D1-264[»]
ProteinModelPortaliP32400.
SMRiP32400. Positions 7-259.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00274; UER00397.
BioCyciMetaCyc:MONOMER-11021.

Miscellaneous databases

EvolutionaryTraceiP32400.

Family and domain databases

Gene3Di3.40.50.850. 1 hit.
InterProiIPR000868. Isochorismatase-like.
[Graphical view]
PfamiPF00857. Isochorismatase. 1 hit.
[Graphical view]
SUPFAMiSSF52499. SSF52499. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCSH_ARTSP
AccessioniPrimary (citable) accession number: P32400
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.