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Reviewed, UniProtKB/Swiss-Prot A6KX92 (HUTI_BACV8)

Last modified November 3, 2009. Version 18. 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

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: BVU_0336
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Imidazolonepropionase HAMAP MF_00372
PRO_0000306438

Sites

Metal binding771Zinc or iron By similarity
Metal binding791Zinc or iron By similarity
Metal binding2491Zinc or iron By similarity
Metal binding3231Zinc or iron By similarity
Binding site861Substrate By similarity
Binding site991Substrate By similarity
Binding site1491Substrate By similarity
Binding site1841Substrate By similarity
Binding site2521Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A6KX92-1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 3E16F3366E2C6F93

FASTA41444,945
        10         20         30         40         50         60 
MSNNLIIINA HIVTPQGRTA RKGEAMNELL NIPCGTVRVT DGIITYVGEN RISHEKPGYK 

        70         80         90        100        110        120 
VLDARGNVLL PGFVDSHTHL VFGGFRPDEF IWRLNGDSYM SIMERGGGII NTVRATREAS 

       130        140        150        160        170        180 
FEELKHKAEW FLDTMSRMGV TTVEGKSGYG LDRDTELKQL SIMQAINECP DRKVDIATTF 

       190        200        210        220        230        240 
LGAHALPEEY KGRSDAYIDF LINEMLPMIH QKQLAENCDI FCEKGVFTVE QSRKLLKAAQ 

       250        260        270        280        290        300 
ALGFGTKLHA DEIVSFGGAE LAGELKALSA DHLLQASDEG IKALAQNNVV ATLLPLTAFT 

       310        320        330        340        350        360 
LKEPYARGRK MIDSGCAVAL ATDLNPGSCF SGSIPLTFAL ACIYMKLTVA EAITAITLNG 

       370        380        390        400        410 
AAALGRADRI GSIEAGKQGD FVLLGTDNPH ILPYYTGMNA VKLTIKGGRI LHSN 

« Hide

References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000139 Genomic DNA. Translation: ABR38056.1.
RefSeqYP_001297678.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6KX92.

Genome annotation databases

GeneID5301305.
GenomeReviewsGene locus BVU_0336 in contig CP000139_GR.
KEGGbvu:BVU_0336.
NMPDRfig|435590.6.peg.324.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMNMACTL.

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...

Entry information

Entry nameHUTI_BACV8
AccessionPrimary (citable) accession number: A6KX92
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 24, 2007
Last modified: November 3, 2009
This is version 18 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)

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