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Reviewed, UniProtKB/Swiss-Prot Q891P9 (HUTI_CLOTE)

Last modified June 16, 2009. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: CTC_02320
OrganismClostridium tetani [Complete proteome] [HAMAP]
Taxonomic identifier1513 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

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Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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.

Sequence similarities

Belongs to the hutI family.

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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: HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Imidazolonepropionase HAMAP MF_00372
PRO_0000306457

Sites

Metal binding821Zinc or iron By similarity
Metal binding841Zinc or iron By similarity
Metal binding2521Zinc or iron By similarity
Metal binding3261Zinc or iron By similarity
Binding site911Substrate By similarity
Binding site1041Substrate By similarity
Binding site1541Substrate By similarity
Binding site1871Substrate By similarity
Binding site2551Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q891P9-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FDC85F6E21E3E146

FASTA41946,125
        10         20         30         40         50         60 
MKKGNVIIKN ASQVITCSGF EGKFGKDMNN INVIENASVV VEDGIIKEIG SLEDILKKYN 

        70         80         90        100        110        120 
EKHFEIVDAS NKAVLPGFVD SHTHFVFGGF RAEEFSWRLN GESYMDIMNK GGGIVNSVRG 

       130        140        150        160        170        180 
TREATEDELY ESAKKRLDSM IHFGVTTVEG KSGYGLDYET ELKQLRVMDR LQKDHSIDIC 

       190        200        210        220        230        240 
KTFMGAHATP EEYRGRNEEY INFIIEDVLP KVAEEKLAEF CDVFCEEGVF SVEESRKILL 

       250        260        270        280        290        300 
KAKELGMKIK LHADEIVQLG GAELAAELGA TSADHLLHAS DEGIKAMADK KVIATLLPTT 

       310        320        330        340        350        360 
AFCLKEPFAR ARMMIDKGGA VALGTDFNPG SGFTNSIPLM FALATIYMDM SIEEAISAMT 

       370        380        390        400        410 
INGAAAIGRA ETIGSIDKGK KGDLVILEYP SYKFLPYNTG VNIVETVIKD GNIVYKKSY

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References

[1]"The genome sequence of Clostridium tetani, the causative agent of tetanus disease."
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed: 12552129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Massachusetts / E88.

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Cross-references

Sequence databases

AE015927 Genomic DNA. Translation: AAO36796.1.
RefSeqNP_782859.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1058694.
GenomeReviewsGene locus CTC_02320 in contig AE015927_GR.
KEGGctc:CTC02320.
NMPDRfig|212717.1.peg.2081.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ891P9.
OMAQ891P9. MNMACTL.

Enzyme and pathway databases

BioCycCTET212717:CTC_02320-MON.
BRENDA3.5.2.7. 2082.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
ProDomPD001248. Amidohydro_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameHUTI_CLOTE
AccessionPrimary (citable) accession number: Q891P9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents