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B2T2Y6 (HUTI_BURPP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:Bphyt_1534
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia

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_1000121540

Sites

Metal binding671Zinc or iron By similarity
Metal binding691Zinc or iron By similarity
Metal binding2371Zinc or iron By similarity
Metal binding3121Zinc or iron By similarity
Binding site761Substrate By similarity
Binding site891Substrate By similarity
Binding site1391Substrate By similarity
Binding site1721Substrate By similarity
Binding site2401Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B2T2Y6 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 0A07EA02248B0249

FASTA40744,113
        10         20         30         40         50         60 
MKQTVWHHLK LCPQGDPQNT LPDAAIAVEN GTIVWLGAAS SLPADYAAWP REDLHGAWVT 

        70         80         90        100        110        120 
PGLVDCHTHL VYGGQRADEF AQRLAGVSYE EIARQGGGIV STVRATRAAD EASLFRQSAA 

       130        140        150        160        170        180 
RLEPLLAEGV TTVEIKSGYG LDLASERKML RVARQLGERY PVTVYTTFLG AHALPPEFAG 

       190        200        210        220        230        240 
RADAYIDEVC NTMLPALADE GLVDAVDVFC ERIGFSLEQS ERVFNAAERY KLPVKMHAEQ 

       250        260        270        280        290        300 
LSNGGGTALA ARHRALSADH LEFLDEAGVA AMKEAGTVAV LLPGAYYFIR ETQLPPLELL 

       310        320        330        340        350        360 
RRYQVPVAIS TDSNPGTSPA TSLLLMMNMA TTLFRMTVPE VLQGVTSHAA RALGKADRHG 

       370        380        390        400 
SLEAGRAADF AVWSVDSLAE LAYWIGRPLC ARVVRAGETV YTRRELS

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001052 Genomic DNA. Translation: ACD15947.1.
RefSeqYP_001895171.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2T2Y6.
SMRB2T2Y6. Positions 17-400.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2T2Y6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6283578.
GenomeReviewsGene locus Bphyt_1534 in contig CP001052_GR.
KEGGbpy:Bphyt_1534.
PATRIC19213138. VBIBurPhy117947_5348.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

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_BURPP
AccessionPrimary (citable) accession number: B2T2Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 29 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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