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B3R6A3 (HUTI_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:RALTA_A2489
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length417 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 – 417417Imidazolonepropionase HAMAP MF_00372
PRO_1000121541

Sites

Metal binding771Zinc or iron By similarity
Metal binding791Zinc or iron By similarity
Metal binding2471Zinc or iron By similarity
Metal binding3221Zinc or iron By similarity
Binding site861Substrate By similarity
Binding site991Substrate By similarity
Binding site1491Substrate By similarity
Binding site1821Substrate By similarity
Binding site2501Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R6A3 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 459AA490044F9714

FASTA41744,261
        10         20         30         40         50         60 
MTPNSLLSAP SADGVWHHCH LLPDADPARA IRDGALVVEH GRIAWLGAAA DLPEAWRGAP 

        70         80         90        100        110        120 
RHDANGAWIT PGLVDCHTHL VYGGQRADEF AMRLAGAGYE EIARAGGGIV STVRATRGAD 

       130        140        150        160        170        180 
EDTLFAQAAA RLQPLLAEGV TAIEIKSGYG LNLESERKQL RVARRLGEHF GISVYTTFLG 

       190        200        210        220        230        240 
AHALPPEYAD RADDYIELVC NTMLPALADE GLVDAVDAFC ESIGFSIAQT ERVFDAAARH 

       250        260        270        280        290        300 
GLRVKLHAEQ LSNLGGAALA ARHRALSADH LEHLDEAGVA AMAEAGTVAV LLPGAYYFLR 

       310        320        330        340        350        360 
DTNLPPIALL RQYGVPMAIS TDHNPGTSPV TSLLLMMNMA CTLFRLTVPE ALAGVTAHAA 

       370        380        390        400        410 
RALGADDRHG RLAVGRVADF ALWRIDSPAE LAYWFGRNPV ATVVRQGRVH AGAGAAA

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAQ70421.1.
RefSeqYP_002006482.1. NC_010528.1.

3D structure databases

ProteinModelPortalB3R6A3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3R6A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6454617.
GenomeReviewsGene locus RALTA_A2489 in contig CU633749_GR.
KEGGcti:RALTA_A2489.
PATRIC21531620. VBICupTai42494_2449.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_CUPTR
AccessionPrimary (citable) accession number: B3R6A3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 30 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

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