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Protein

Creatinase

Gene
N/A
Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Creatine + H2O = sarcosine + urea.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei232 – 2321

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Creatinase (EC:3.5.3.3)
Alternative name(s):
Creatine amidinohydrolase
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403CreatinasePRO_0000079344Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Helixi21 – 3717Combined sources
Beta strandi41 – 455Combined sources
Helixi48 – 558Combined sources
Beta strandi67 – 704Combined sources
Beta strandi75 – 806Combined sources
Helixi81 – 833Combined sources
Helixi86 – 905Combined sources
Beta strandi93 – 997Combined sources
Helixi106 – 1149Combined sources
Beta strandi119 – 1235Combined sources
Turni125 – 1273Combined sources
Helixi130 – 13910Combined sources
Beta strandi144 – 1474Combined sources
Helixi149 – 1568Combined sources
Helixi161 – 18424Combined sources
Helixi191 – 20919Combined sources
Beta strandi219 – 2246Combined sources
Helixi225 – 2295Combined sources
Beta strandi235 – 2373Combined sources
Beta strandi245 – 2517Combined sources
Beta strandi261 – 2688Combined sources
Helixi272 – 29120Combined sources
Helixi298 – 31114Combined sources
Helixi315 – 3173Combined sources
Beta strandi327 – 3304Combined sources
Beta strandi354 – 3574Combined sources
Beta strandi360 – 3634Combined sources
Beta strandi371 – 3744Combined sources
Beta strandi376 – 3827Combined sources
Beta strandi385 – 3884Combined sources
Helixi396 – 3994Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHMX-ray1.90A/B2-402[»]
ProteinModelPortaliP38488.
SMRiP38488. Positions 2-402.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38488.

Family & Domainsi

Domaini

Each monomer has two clearly defined domains. The small N-terminal domain (AA 1-161) and the large domain (AA 162-403). Each of the two active sites is made by residues of the large domain of one monomer and some residues of the small domain of the other monomer.

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000587. Creatinase_N.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.

Sequencei

Sequence statusi: Complete.

P38488-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQMPKTLRIR NGDKVRSTFS AQEYANRQAR LRAHLAAENI DAAIFTSYHN
60 70 80 90 100
INYYSDFLYC SFGRPYALVV TEDDVISISA NIDGGQPWRR TVGTDNIVYT
110 120 130 140 150
DWQRDNYFAA IQQALPKARR IGIEHDHLNL QNRDKLAARY PDAELVDVAA
160 170 180 190 200
ACMRMRMIKS AEEHVMIRHG ARIADIGGAA VVEALGDQVP EYEVALHATQ
210 220 230 240 250
AMVRAIADTF EDVELMDTWT WFQSGINTDG AHNPVTTRKV NKGDILSLNC
260 270 280 290 300
FPMIAGYYTA LERTLFLDHC SDDHLRLWQV NVEVHEAGLK LIKPGARCSD
310 320 330 340 350
IARELNEIFL KHDVLQYRTF GYGHSFGTLS HYYGREAGLE LREDIDTVLE
360 370 380 390 400
PGMVVSMEPM IMLPEGLPGA GGYREHDILI VNENGAENIT KFPYGPEKNI

IRK
Length:403
Mass (Da):45,537
Last modified:February 1, 1995 - v2
Checksum:i21C2CD808D017EE0
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CHMX-ray1.90A/B2-402[»]
ProteinModelPortaliP38488.
SMRiP38488. Positions 2-402.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP38488.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000587. Creatinase_N.
IPR000994. Pept_M24_structural-domain.
[Graphical view]
PfamiPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures."
    Coll M., Knof S.H., Ohga Y., Messerschmidt A., Huber R., Moellering H., Ruessmann L., Schumacher G.
    J. Mol. Biol. 214:597-610(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
  2. "Crystal structure determination, refinement and molecular model of creatine amidinohydrolase from Pseudomonas putida."
    Hoeffken H.W., Knof S.H., Bartlett P.A., Huber R., Moellering H., Schumacher G.
    J. Mol. Biol. 204:417-433(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Entry informationi

Entry nameiCREA_PSEPU
AccessioniPrimary (citable) accession number: P38488
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 1, 1995
Last modified: October 14, 2015
This is version 70 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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.