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B2SD97 (HUTI_BRUA1) 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
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:BAbS19_II02900
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP]
Taxonomic identifier430066 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length405 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 – 405405Imidazolonepropionase HAMAP MF_00372
PRO_1000121534

Sites

Metal binding731Zinc or iron By similarity
Metal binding751Zinc or iron By similarity
Metal binding2431Zinc or iron By similarity
Metal binding3181Zinc or iron By similarity
Binding site821Substrate By similarity
Binding site951Substrate By similarity
Binding site1451Substrate By similarity
Binding site1781Substrate By similarity
Binding site2461Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2SD97 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: A55470DFB24E994E

FASTA40543,520
        10         20         30         40         50         60 
MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPD EYASFEKIDC 

        70         80         90        100        110        120 
GNRLITPGLI DCHTHLVHAG NRAHEFELRL QGATYEEVAR AGGGIVSSVR NLRAASEDDL 

       130        140        150        160        170        180 
VRETLPRLDA LIAEGVTTVE VKSGYGLDRD SEIKSLKAAR RLGEERDVAI RTTFLGAHAL 

       190        200        210        220        230        240 
PPEMNGDKAA YIDRVINDML PAIAEQGLAD AVDGFCEGIA FLPDEIARVF DAAKAHDIPV 

       250        260        270        280        290        300 
KLHADQLSNL HGAALAASYG ALSADHLEYT DADGAAAMAS AGTVAVLLPG AYYFIRETQK 

       310        320        330        340        350        360 
PPVEAFRAAG TKMALATDNN PGTSPLTSLL LTMNMGATLF RMTVEECIAG VTREAARALG 

       370        380        390        400 
ILDQTGTLEI GKDADLAIWD IERPAELVYR IGFNPLWKRV FKGQI 

« Hide

References

[1]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed: 18478107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000888 Genomic DNA. Translation: ACD73801.1.
RefSeqYP_001932247.1. NC_010740.1.

3D structure databases

ProteinModelPortalB2SD97.
SMRB2SD97. Positions 5-404.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2SD97.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6326040.
GenomeReviewsGene locus BAbS19_II02900 in contig CP000888_GR.
KEGGbmc:BAbS19_II02900.
PATRIC17815029. VBIBruAbo38055_0324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_BRUA1
AccessionPrimary (citable) accession number: B2SD97
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 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