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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.

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei177Nucleophile1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000793971 – 264N-carbamoylsarcosine amidaseAdd BLAST264

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

1264
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 33Combined sources25
Beta strandi43 – 51Combined sources9
Helixi54 – 57Combined sources4
Beta strandi58 – 61Combined sources4
Helixi68 – 84Combined sources17
Beta strandi89 – 94Combined sources6
Helixi109 – 113Combined sources5
Helixi117 – 119Combined sources3
Helixi125 – 127Combined sources3
Helixi131 – 133Combined sources3
Beta strandi140 – 150Combined sources11
Helixi155 – 161Combined sources7
Beta strandi166 – 172Combined sources7
Turni174 – 176Combined sources3
Helixi177 – 188Combined sources12
Beta strandi191 – 195Combined sources5
Helixi196 – 198Combined sources3
Beta strandi202 – 205Combined sources4
Helixi206 – 217Combined sources12
Beta strandi220 – 222Combined sources3
Helixi224 – 233Combined sources10
Helixi237 – 239Combined sources3

3D structure databases

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

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: November 2, 2016
This is version 69 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

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 one 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.