Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0JUI7 (HUTI_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Arth_1313
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length400 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

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 – 400400Imidazolonepropionase HAMAP MF_00372
PRO_0000306426

Sites

Metal binding641Zinc or iron By similarity
Metal binding661Zinc or iron By similarity
Metal binding2191Zinc or iron By similarity
Metal binding3031Zinc or iron By similarity
Binding site731Substrate By similarity
Binding site861Substrate By similarity
Binding site1311Substrate By similarity
Binding site1581Substrate By similarity
Binding site2221Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JUI7 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 4626C3E7F1919D60

FASTA40041,829
        10         20         30         40         50         60 
MSTLITNIAE LMTQDAEHRV LKDAAVVIEG ERISWIGPSS AAPAADDEVD AGGRALLPGW 

        70         80         90        100        110        120 
VDSHTHLIFA GDRTAEFEAR MAGESYSAGG IAVTTGATRG TSDFDLTRLA LGRVAEAVSQ 

       130        140        150        160        170        180 
GTTYLETKTG YGLDVENETR SARIASTVAD EVTYLGAHLV PAGADADEYT DLVCGPMLAA 

       190        200        210        220        230        240 
VRPYVSWADV FCEQGAFNEQ QSRRVLQACK DAGMGLRVHG NQLGEGPGVR LAVEFGAASV 

       250        260        270        280        290        300 
DHVNYLSAAD VEALAGSWSG WQGAGTRGTV ATCLPACDLS TRQPLAPGRE LLDAGVPIAL 

       310        320        330        340        350        360 
ASNCNPGTSY TSSMAFCVTT AVLQMRLSVH EAVRAATYGG ALALRREAGN DVDGERAVGS 

       370        380        390        400 
VAIGHRADLH LLNAPSATHL AYRPGIPLTH AVWRAGVRAR

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000454 Genomic DNA. Translation: ABK02707.1.
RefSeqYP_830807.1. NC_008541.1.

3D structure databases

ProteinModelPortalA0JUI7.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JUI7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4446202.
GenomeReviewsGene locus Arth_1313 in contig CP000454_GR.
KEGGart:Arth_1313.
PATRIC20997911. VBIArtSp72239_1668.
TIGRArth_1313.

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK14085.

Enzyme and pathway databases

BioCycASP1667:ARTH_1313-MONOMER.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_ARTS2
AccessionPrimary (citable) accession number: A0JUI7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 34 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents