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B6ERX5 (HUTI_ALISL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:VSAL_II0705
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio

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_1000121526

Sites

Metal binding721Zinc or iron By similarity
Metal binding741Zinc or iron By similarity
Metal binding2421Zinc or iron By similarity
Metal binding3171Zinc or iron By similarity
Binding site811Substrate By similarity
Binding site941Substrate By similarity
Binding site1441Substrate By similarity
Binding site1771Substrate By similarity
Binding site2451Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B6ERX5 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: DC961E9FBDDB9F67

FASTA40744,531
        10         20         30         40         50         60 
MDRIFTNLNL VTMKTDLSTP NDGYQIIQDA MIGVTNGKVE YVGHSCPEIF HGHPDVIDCG 

        70         80         90        100        110        120 
NALVTPGFID CHTHLIFAGN RANEFEQRLQ GVPYQDIARQ GGGILSTVNA TRQASEDELY 

       130        140        150        160        170        180 
HLAVQRLEGL KRDGVTTVEI KSGYGLTLYD ELKMLRVAKR IAKLPDMKVS STLLAAHALP 

       190        200        210        220        230        240 
PEYKDKPDDY ITLICDSIIP TVAEQKLADH VDVFCEGIGF SVEQCQRVFD AALTHELGIK 

       250        260        270        280        290        300 
GHTEQLSNLG GSALAASMGA DSVDHIEYLD EDGVKSLAKH NTVATLLPGA FYFLRETQLP 

       310        320        330        340        350        360 
PIDLLRKHHV PMAISTDFNP GTSPIASLRM MMNMACTLFR LTPEEALRGV TCNAAQALGL 

       370        380        390        400 
QSSRGQISVG MEADFALWQL DSPAELSYRL GVPDLIARVV DGDVFYN

« Hide

References

[1]"The complete genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238."
Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LFI1238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM178380 Genomic DNA. Translation: CAQ81459.1.
RefSeqYP_002265019.1. NC_011313.1.

3D structure databases

ProteinModelPortalB6ERX5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB6ERX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6962489.
GenomeReviewsGene locus VSAL_II0705 in contig FM178380_GR.
KEGGvsa:VSAL_II0705.
PATRIC20858204. VBIAliSal95923_4062.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR013108. Amidohydro_3.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
PF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_ALISL
AccessionPrimary (citable) accession number: B6ERX5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 25, 2008
Last modified: January 25, 2012
This is version 28 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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