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Q5WCP8 (HUTI_BACSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Imidazolonepropionase

EC=3.5.2.7
Alternative name(s):
Imidazolone-5-propionate hydrolase
Gene names
Name:hutI
Ordered Locus Names:ABC3329
OrganismBacillus clausii (strain KSM-K16) [Complete proteome] [HAMAP]
Taxonomic identifier66692 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O = N-formimidoyl-L-glutamate + H+. HAMAP MF_00372

Cofactor

Binds 1 zinc or iron ion per subunit By similarity. HAMAP MF_00372

Pathway

Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3. HAMAP MF_00372

Subcellular location

Cytoplasm Potential HAMAP MF_00372.

Sequence similarities

Belongs to the HutI family.

Ontologies

Keywords
   Biological processHistidine metabolism
   Cellular componentCytoplasm
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhistidine catabolic process to glutamate and formamide

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionimidazolonepropionase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Imidazolonepropionase HAMAP MF_00372
PRO_0000306432

Sites

Metal binding851Zinc or iron By similarity
Metal binding871Zinc or iron By similarity
Metal binding2551Zinc or iron By similarity
Metal binding3291Zinc or iron By similarity
Binding site941Substrate By similarity
Binding site1071Substrate By similarity
Binding site1571Substrate By similarity
Binding site1901Substrate By similarity
Binding site2581Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5WCP8 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: F54C70EE28632E3E

FASTA44747,914
        10         20         30         40         50         60 
MAELLYLKEA EQVVTVAGAS DKPKVGEDLS EIGVIERGSV IVEGEKIAFA GTDADARHYL 

        70         80         90        100        110        120 
QKRSGKVKTI EATGKILTPG LVDPHTHLVF AGSREQELTM RLKGKSYMSI LQAGGGILST 

       130        140        150        160        170        180 
TKSTRAATAD QLAHESRLRL DRFLQHGVTT VEAKSGYGLA TDAELKQLRV AQQLNNDHPV 

       190        200        210        220        230        240 
DVVSTFMGAH AIPPEWKQDP NGFVQLVAEE MIPQVAAENL AEFCDVFCEE GVFTVAQSQY 

       250        260        270        280        290        300 
ILEEGKKHGL KPKIHADELV SFGGAELAAK VGAVSADHLL KASPTGIEQM AEAGVIAVLL 

       310        320        330        340        350        360 
PGTAFFLMTE PANARAMIEA GVPVALSTDR NPGSSPTESL PFIMNLACLT MKMTPEEVLA 

       370        380        390        400        410        420 
ASTINAAHAI GRAKDIGSIE AGKNADLVLF DAPNYQTLQY NYAVNRVDTV MKAGKIVVEG 

       430        440 
GVLLEKTDNQ RCSLATEDRG TRPIWQK 

« Hide

References

[1]"The complete genome sequence of the alkaliphilic Bacillus clausii KSM-K16."
Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., Kawai S., Ito S., Horikoshi K.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KSM-K16.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006627 Genomic DNA. Translation: BAD65862.1.
RefSeqYP_176823.1. NC_006582.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortalQ5WCP8.
SMRQ5WCP8. Positions 10-419.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WCP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000045998; EBBACP00000044759; EBBACG00000045989.
GeneID3201303.
GenomeReviewsGene locus ABC3329 in contig AP006627_GR.
KEGGbcl:ABC3329.
NMPDRfig|66692.3.peg.3344.
PATRIC18926390. VBIBacCla58185_3543.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1228.
GeneTreeEBGT00050000002251.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycBCLA66692:ABC3329-MONOMER.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_BACSK
AccessionPrimary (citable) accession number: Q5WCP8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: November 23, 2004
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families