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A0K8U2 (HUTI_BURCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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:Bcen2424_2168
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length407 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 – 407407Imidazolonepropionase HAMAP MF_00372
PRO_0000306447

Sites

Metal binding681Zinc or iron By similarity
Metal binding701Zinc or iron By similarity
Metal binding2381Zinc or iron By similarity
Metal binding3131Zinc or iron By similarity
Binding site771Substrate By similarity
Binding site901Substrate By similarity
Binding site1401Substrate By similarity
Binding site1731Substrate By similarity
Binding site2411Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0K8U2 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 4957FACB2984A362

FASTA40744,092
        10         20         30         40         50         60 
MKPTVWHHLR LCPHGHPDET IDDAAIAVDE TGTIAWLGAL SALPHGYAHW QREDLHGAWV 

        70         80         90        100        110        120 
TPGLVDCHTH LVYGGTRADE FAQRLAGVSY EEIARQGGGI VSTVRATRAA DETTLFVQAA 

       130        140        150        160        170        180 
ARLQPLLAEG VTAIEIKSGY GLDLASERKM LRVARQLGER FPVTVYTTFL GAHALPPEYA 

       190        200        210        220        230        240 
GRADEYIDEV CDRMLPTLAD EGLVDAVDVF CERIGFSLAQ TERVFEAATR RGLPVKLHAE 

       250        260        270        280        290        300 
QLSNAGGTAL AARYRALSAD HLEFLDEAGI EAMKAAGTVA VLLPGAYYFI RETQLPPIDL 

       310        320        330        340        350        360 
LRKHGVPIAL ATDHNPGTSP LESLLLTLNM GCTLFRMTVP EVLQGVTRHA AAALGRADRH 

       370        380        390        400 
GALEVGRQAD FAAWSVGSLA ELAYWIGRPL CEQVVRGGTP VFRRMNG 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI2424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000458 Genomic DNA. Translation: ABK08919.1.
RefSeqYP_835812.1. NC_008542.1.

3D structure databases

ProteinModelPortalA0K8U2.
SMRA0K8U2. Positions 4-401.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0K8U2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4449985.
GenomeReviewsGene locus Bcen2424_2168 in contig CP000458_GR.
KEGGbch:Bcen2424_2168.
PATRIC19061715. VBIBurCen15205_2207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycBCEN331272:BCEN2424_2168-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_BURCH
AccessionPrimary (citable) accession number: A0K8U2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 34 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