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Q579E7 (HUTI_BRUAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BruAb2_0304
OrganismBrucella abortus biovar 1 (strain 9-941) [Complete proteome] [HAMAP]
Taxonomic identifier262698 [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-Rule MF_00372

Cofactor

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

Pathway

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

Subcellular location

Cytoplasm Potential HAMAP-Rule 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: UniProtKB-UniPathway

histidine catabolic process to glutamate and formate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionimidazolonepropionase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Imidazolonepropionase HAMAP-Rule MF_00372
PRO_0000306443

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
Q579E7 [UniParc].

Last modified May 10, 2005. 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]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017224 Genomic DNA. Translation: AAX75737.1.
RefSeqYP_223098.1. NC_006933.1.

3D structure databases

ProteinModelPortalQ579E7.
SMRQ579E7. Positions 5-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262698.BruAb2_0304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAX75737; AAX75737; BruAb2_0304.
GeneID3341633.
KEGGbmb:BruAb2_0304.
PATRIC17826844. VBIBruAbo15061_2605.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHOG000218461.
KOK01468.
OMAGRADDYI.
OrthoDBEOG63C0XD.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycBABO262698:GJC2-2513-MONOMER.
UniPathwayUPA00379; UER00551.

Family and domain databases

Gene3D2.30.40.10. 1 hit.
HAMAPMF_00372. HutI.
InterProIPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
SUPFAMSSF51338. SSF51338. 2 hits.
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_BRUAB
AccessionPrimary (citable) accession number: Q579E7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 10, 2005
Last modified: April 16, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names