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Protein

Creatinine amidohydrolase

Gene

crnA

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

Functioni

Cyclic amidohydrolase that catalyzes the reversible conversion of creatinine to creatine. Is also active toward glycocyamidine, though the reaction rate is very low, but it is completely inert toward hydantoin and its derivatives.1 Publication

Catalytic activityi

Creatinine + H2O = creatine.2 Publications

Cofactori

Note: Binds 2 Zn2+ ions per subunit. The Zn2+ in the metal 1 binding site can be replaced with Mn2+; however, the second zinc in metal binding site 2 is much more tightly bound and cannot be replaced. The enzyme with one zinc and one manganese ion is more active than that with two zinc ions.2 Publications

Enzyme regulationi

Is markedly inactivated in vitro by heavy metal ions, N-bromosuccinimide, ethoxyformic anhydride, and dye-sensitized photooxidation.1 Publication

Kineticsi

  1. KM=26 mM for creatinine2 Publications
  2. KM=130 mM for creatine2 Publications
  3. KM=200 mM for glycocyamidine2 Publications
  1. Vmax=390 µmol/min/mg enzyme for the forward reaction (creatine formation)2 Publications
  2. Vmax=1510 µmol/min/mg enzyme for the reverse reaction (creatinine formation)2 Publications
  3. Vmax=3.7 µmol/min/mg enzyme with glycocyamidine as substrate2 Publications

pH dependencei

Optimum pH is 7-9 for the forward and reverse reactions.1 Publication

Temperature dependencei

Retains 75% of the activity after incubation at 75 degrees Celsius for 30 minutes.1 Publication

Pathwayi: creatinine degradation

This protein is involved in the pathway creatinine degradation, which is part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the pathway creatinine degradation and in Amine and polyamine degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi34Zinc or manganese 12 Publications1
Metal bindingi36Zinc 2; via tele nitrogen2 Publications1
Metal bindingi45Zinc 22 Publications1
Metal bindingi45Zinc or manganese 12 Publications1
Binding sitei78Substrate; via carbonyl oxygen1
Metal bindingi120Zinc or manganese 1; via pros nitrogen2 Publications1
Binding sitei121Substrate; via amide nitrogen1
Sitei122Coordinates a catalytic water molecule1
Metal bindingi183Zinc 22 Publications1

GO - Molecular functioni

  • creatininase activity Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • creatine biosynthetic process Source: UniProtKB
  • creatinine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10962.
BRENDAi3.5.2.10. 5092.
UniPathwayiUPA00274.

Names & Taxonomyi

Protein namesi
Recommended name:
Creatinine amidohydrolase (EC:3.5.2.10)
Alternative name(s):
Creatininase
Gene namesi
Name:crnA
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi121Y → A: 30-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi122E → Q: 700-fold decrease in catalytic efficiency. No ion in metal binding site 1. 1 Publication1
Mutagenesisi154W → A: Loss of activity. 1 Publication1
Mutagenesisi154W → F: 340-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi174W → A: Nearly no activity. 1 Publication1
Mutagenesisi174W → F: 2-fold decrease in catalytic efficiency. 1 Publication1
Mutagenesisi178H → A: Loss of activity. 1
Mutagenesisi183E → Q: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00004069342 – 260Creatinine amidohydrolaseAdd BLAST259

Interactioni

Subunit structurei

Homohexamer; trimer of dimers.3 Publications

Structurei

Secondary structure

1260
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 9Combined sources3
Helixi12 – 20Combined sources9
Beta strandi26 – 30Combined sources5
Beta strandi38 – 40Combined sources3
Helixi44 – 60Combined sources17
Helixi76 – 79Combined sources4
Beta strandi84 – 86Combined sources3
Helixi92 – 109Combined sources18
Beta strandi113 – 118Combined sources6
Helixi121 – 123Combined sources3
Helixi124 – 140Combined sources17
Beta strandi147 – 152Combined sources6
Helixi153 – 156Combined sources4
Helixi160 – 166Combined sources7
Helixi174 – 176Combined sources3
Beta strandi178 – 180Combined sources3
Helixi181 – 190Combined sources10
Helixi192 – 194Combined sources3
Helixi197 – 199Combined sources3
Beta strandi210 – 215Combined sources6
Helixi218 – 220Combined sources3
Helixi235 – 256Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J2TX-ray1.80A/B/C/D/E/F1-260[»]
1J2UX-ray1.85A/B/C/D/E/F1-260[»]
1Q3KX-ray2.10A/B/C/D/E/F2-260[»]
1V7ZX-ray1.60A/B/C/D/E/F1-260[»]
3A6DX-ray1.90A/B/C/D/E/F1-260[»]
3A6EX-ray2.00A/B/C/D/E/F1-260[»]
3A6FX-ray1.78A/B/C/D/E/F1-260[»]
3A6GX-ray2.00A/B/C/D/E/F1-260[»]
3A6HX-ray2.00A/B/C/D/E/F1-260[»]
3A6JX-ray2.00A/B/C/D/E/F1-260[»]
3A6KX-ray2.20A/B/C/D/E/F1-260[»]
3A6LX-ray2.00A/B/C/D/E/F1-260[»]
ProteinModelPortaliP83772.
SMRiP83772.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83772.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni174 – 178Substrate binding5

Sequence similaritiesi

Belongs to the creatininase superfamily.Curated

Family and domain databases

Gene3Di3.40.50.10310. 1 hit.
InterProiIPR031034. Creatininase.
IPR024087. Creatininase-like_dom.
IPR003785. Creatininase/forma_Hydrolase.
[Graphical view]
PfamiPF02633. Creatininase. 1 hit.
[Graphical view]
SUPFAMiSSF102215. SSF102215. 1 hit.
TIGRFAMsiTIGR04448. creatininase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P83772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSVFVGEL TWKEYEARVA AGDCVLMLPV GALEQHGHHM CMNVDVLLPT
60 70 80 90 100
AVCKRVAERI GALVMPGLQY GYKSQQKSGG GNHFPGTTSL DGATLTGTVQ
110 120 130 140 150
DIIRELARHG ARRLVLMNGH YENSMFIVEG IDLALRELRY AGIQDFKVVV
160 170 180 190 200
LSYWDFVKDP AVIQQLYPEG FLGWDIEHGG VFETSLMLAL YPDLVDLDRV
210 220 230 240 250
VDHPPATFPP YDVFPVDPAR TPAPGTLSSA KTASREKGEL ILEVCVQGIA
260
DAIREEFPPT
Length:260
Mass (Da):28,569
Last modified:March 15, 2004 - v1
Checksum:iE530A7513F57A762
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45424 Genomic DNA. Translation: BAA08265.1.
PIRiT48846.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45424 Genomic DNA. Translation: BAA08265.1.
PIRiT48846.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J2TX-ray1.80A/B/C/D/E/F1-260[»]
1J2UX-ray1.85A/B/C/D/E/F1-260[»]
1Q3KX-ray2.10A/B/C/D/E/F2-260[»]
1V7ZX-ray1.60A/B/C/D/E/F1-260[»]
3A6DX-ray1.90A/B/C/D/E/F1-260[»]
3A6EX-ray2.00A/B/C/D/E/F1-260[»]
3A6FX-ray1.78A/B/C/D/E/F1-260[»]
3A6GX-ray2.00A/B/C/D/E/F1-260[»]
3A6HX-ray2.00A/B/C/D/E/F1-260[»]
3A6JX-ray2.00A/B/C/D/E/F1-260[»]
3A6KX-ray2.20A/B/C/D/E/F1-260[»]
3A6LX-ray2.00A/B/C/D/E/F1-260[»]
ProteinModelPortaliP83772.
SMRiP83772.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00274.
BioCyciMetaCyc:MONOMER-10962.
BRENDAi3.5.2.10. 5092.

Miscellaneous databases

EvolutionaryTraceiP83772.

Family and domain databases

Gene3Di3.40.50.10310. 1 hit.
InterProiIPR031034. Creatininase.
IPR024087. Creatininase-like_dom.
IPR003785. Creatininase/forma_Hydrolase.
[Graphical view]
PfamiPF02633. Creatininase. 1 hit.
[Graphical view]
SUPFAMiSSF102215. SSF102215. 1 hit.
TIGRFAMsiTIGR04448. creatininase. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCRNA_PSEPU
AccessioniPrimary (citable) accession number: P83772
Secondary accession number(s): Q52548
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: March 15, 2004
Last modified: November 2, 2016
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The proposed catalytic mechanism involves two water molecules. The first molecule is a hydroxide ion that is bound as a bridge between the two metal ions and attacks the carbonyl carbon of the substrate. The second water molecule, that is bound to the carboxyl group of Glu-122 and to the metal 1, functions as a proton donor in catalysis.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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