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A5FZB8 (HUTI_ACICJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. 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:Acry_1746
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

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_1000007139

Sites

Metal binding701Zinc or iron By similarity
Metal binding721Zinc or iron By similarity
Metal binding2381Zinc or iron By similarity
Metal binding3131Zinc or iron By similarity
Binding site791Substrate By similarity
Binding site921Substrate By similarity
Binding site1421Substrate By similarity
Binding site1751Substrate By similarity
Binding site2411Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5FZB8 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 0EA63B04479255F1

FASTA40141,759
        10         20         30         40         50         60 
MRCDRLWRNA RLATCAPDRP GLGVVEGGAV ASRDGRIVWA GPEAEMPSLE AAETIDCAGR 

        70         80         90        100        110        120 
WITPGLVDCH THLIFGGDRS GEFARRLAGE SYESIAREGG GIRATMRATR ALDEAAMRAG 

       130        140        150        160        170        180 
AEARLAAWAA EGVTTVEIKS GYGLDEATEL AMLRAARAIG RAGRFRVAAT YLGAHTMPPE 

       190        200        210        220        230        240 
MDRAAYLDLV CRRMIPAIAE AGLADAVDAF CEEIAFGAGE VAAVFAAARA AGLAVKLHAD 

       250        260        270        280        290        300 
QRAEGGGAAL AARFGALSAD HLEYASAEGI AAMARAGSVA VLLPGAYYVL REAKRPDVAA 

       310        320        330        340        350        360 
MRAAGCRMAV ATDCNPGTSP IASLRLSAQM ACVFFGLSFE EAWLGITRHA ADALGLGGEC 

       370        380        390        400 
GAIDAGRSCD LAIWSVDSLD QVLAWVGPAP LERRVLKGVD A

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000697 Genomic DNA. Translation: ABQ30950.1.
RefSeqYP_001234869.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5FZB8.
SMRA5FZB8. Positions 4-398.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5FZB8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5161989.
GenomeReviewsGene locus Acry_1746 in contig CP000697_GR.
KEGGacr:Acry_1746.
PATRIC20648532. VBIAciCry6074_2246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHBG686142.
OMAMNMACTL.

Enzyme and pathway databases

BioCycACRY349163:ACRY_1746-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_ACICJ
AccessionPrimary (citable) accession number: A5FZB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 31 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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