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P32400

- CSH_ARTSP

UniProt

P32400 - CSH_ARTSP

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

Functioni

Catalytic activityi

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

Cofactori

Binds 1 sulfate ion per subunit.

Pathwayi

Sites

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

GO - Molecular functioni

  1. N-carbamoylsarcosine amidase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. creatinine catabolic process Source: UniProtKB-UniPathway
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 lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264N-carbamoylsarcosine amidase
PRO_0000079397Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

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

3D structure databases

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

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

MTETSGTFND IEARLAAVLE EAFEAGTSIY NERGFKRRIG YGNRPAVIHI    50
DLANAWTQPG HPFSCPGMET IIPNVQRINE AARAKGVPVF YTTNVYRNRD 100
ASSGTNDMGL WYSKIPTETL PADSYWAQID DRIAPADGEV VIEKNRASAF 150
PGTNLELFLT SNRIDTLIVT GATAAGCVRH TVEDAIAKGF RPIIPRETIG 200
DRVPGVVQWN LYDIDNKFGD VESTDSVVQY LDALPQFEDT VPKTLSDPQP 250
EVEAPADPVF AEQH 264
Length:264
Mass (Da):29,057
Last modified:October 1, 1993 - v1
Checksum:i8A213B555EA5DCDC
GO

Sequence databases

PIRiS28969.

Cross-referencesi

Sequence databases

PIRi S28969.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NBA X-ray 2.00 A/B/C/D 1-264 [» ]
ProteinModelPortali P32400.
SMRi P32400. Positions 7-259.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00274 ; UER00397 .
BioCyci MetaCyc:MONOMER-11021.

Miscellaneous databases

EvolutionaryTracei P32400.

Family and domain databases

Gene3Di 3.40.50.850. 1 hit.
InterProi IPR000868. Isochorismatase-like.
[Graphical view ]
Pfami PF00857. Isochorismatase. 1 hit.
[Graphical view ]
SUPFAMi SSF52499. SSF52499. 1 hit.
ProtoNeti Search...

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: October 16, 2013
This is version 63 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

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