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B0SYU7 (HUTI_CAUSK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:Caul_1298
OrganismCaulobacter sp. (strain K31) [Complete proteome] [HAMAP]
Taxonomic identifier366602 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length401 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 – 401401Imidazolonepropionase HAMAP MF_00372
PRO_1000079821

Sites

Metal binding701Zinc or iron By similarity
Metal binding721Zinc or iron By similarity
Metal binding2401Zinc or iron By similarity
Metal binding3151Zinc or iron By similarity
Binding site791Substrate By similarity
Binding site921Substrate By similarity
Binding site1421Substrate By similarity
Binding site1751Substrate By similarity
Binding site2431Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B0SYU7 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: FEFFCF6033706BB3

FASTA40142,469
        10         20         30         40         50         60 
MRCDRVWSKA RLATFAAGRP GIGVVEDGVV ASLSGRIVYA GPATEAPAFE ALETLDCEGR 

        70         80         90        100        110        120 
WITPGLIDPH THLVFGGDRA REFELRLAGA TYEEIARAGG GIVSTMKATR AASEGELVAS 

       130        140        150        160        170        180 
ALPRLDALIA EGLTTIEIKS GYGLSLDDEL KSLRAARALA DVRKVSVTTT FLGAHALPPE 

       190        200        210        220        230        240 
YEGDPDGYID HVCYQMIPAV AAEGLADAVD AFCEGIGFSR AQTRRVFQAA RERGLPVKLH 

       250        260        270        280        290        300 
AEQLSNLDGA ALAAEFGALS ADHLEHLDGA GIAAMAQAGT TAVLLPGAFY FVRETRLPPI 

       310        320        330        340        350        360 
QALRAAGVPL ALATDCNPGT SPLTSLLLTL NMAATLFRMT VDECLAGVTR EAARAIGRLD 

       370        380        390        400 
HIGTLEAGKS CDLAIWDIER PAQLVYRMGF NPLHARVWKG L

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References

[1]"Complete sequence of chromosome of Caulobacter sp. K31."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Bruce D., Goodwin L., Thompson L.S., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Stephens C., Richardson P.
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K31.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000927 Genomic DNA. Translation: ABZ70428.1.
RefSeqYP_001682926.1. NC_010338.1.

3D structure databases

ProteinModelPortalB0SYU7.
SMRB0SYU7. Positions 6-400.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0SYU7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5898753.
GenomeReviewsGene locus Caul_1298 in contig CP000927_GR.
KEGGcak:Caul_1298.
PATRIC21315606. VBICauSp18104_1669.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycCSP78:CAUL_1298-MONOMER.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF07969. Amidohydro_3. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_CAUSK
AccessionPrimary (citable) accession number: B0SYU7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 27 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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