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Q8A4B1 (HUTI_BACTN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. 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:BT_2692
OrganismBacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Taxonomic identifier226186 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length417 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
Reference 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 – 417417Imidazolonepropionase HAMAP MF_00372
PRO_0000306437

Sites

Metal binding801Zinc or iron By similarity
Metal binding821Zinc or iron By similarity
Metal binding2521Zinc or iron By similarity
Metal binding3261Zinc or iron By similarity
Binding site891Substrate By similarity
Binding site1021Substrate By similarity
Binding site1521Substrate By similarity
Binding site1871Substrate By similarity
Binding site2551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A4B1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1BAA8B0CDF56DEF6

FASTA41745,700
        10         20         30         40         50         60 
MSENLIIFNA RIVTPTGTSA RKGAEMGQLR IIENGTVEVT KGIITYVGES RGEDRDGYYQ 

        70         80         90        100        110        120 
HYWHYNARGH CLLPGFVDSH THFVFGGERS EEFSWRLKGE SYMSIMERGG GIASTVKATR 

       130        140        150        160        170        180 
QMNFLKLRSA AEGFLKKMSA MGVTTVEGKS GYGLDRETEL LQLKIMRSLN NDEHKRIDIV 

       190        200        210        220        230        240 
STFLGAHALP EEYKGRGDEY IDFLIREMLP VIRENELAEC CDVFCEQGVF SVEQSRRLLQ 

       250        260        270        280        290        300 
AAKEQGFLLK LHADEIVSFG GAELAAELGA LSADHLLQAS DAGIRAMADA GVVATLLPLT 

       310        320        330        340        350        360 
AFALKEPYAR GREMIDAGCA VALATDLNPG SCFSGSIPLT IALACIYMKL SIEETITALT 

       370        380        390        400        410 
LNGAAALHRA DRIGSIEVGK QGDFVILNSD NYHILPYYVG MNCVIMTIKG GMLYPVN

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References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE015928 Genomic DNA. Translation: AAO77798.1.
RefSeqNP_811604.1. NC_004663.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortalQ8A4B1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1072571.
GenomeReviewsGene locus BT_2692 in contig AE015928_GR.
KEGGbth:BT_2692.
NMPDRfig|226186.1.peg.2691.
PATRIC21060323. VBIBacThe70966_2733.

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
PhylomeDBQ8A4B1.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycBTHE226186:BT_2692-MONOMER.

Family and domain databases

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

Entry information

Entry nameHUTI_BACTN
AccessionPrimary (citable) accession number: Q8A4B1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: January 25, 2012
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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