Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A1TRE0 (HUTI_ACIAC)

Last modified November 3, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Aave_2961
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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: HAMAP

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Imidazolonepropionase HAMAP MF_00372
PRO_0000306420

Sites

Metal binding811Zinc or iron By similarity
Metal binding831Zinc or iron By similarity
Metal binding2511Zinc or iron By similarity
Metal binding3261Zinc or iron By similarity
Binding site901Substrate By similarity
Binding site1031Substrate By similarity
Binding site1531Substrate By similarity
Binding site1861Substrate By similarity
Binding site2541Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TRE0-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 872B70434FD98717

FASTA41643,898
        10         20         30         40         50         60 
MQPTPFSSLS SADGCWTGLR LAQGLFIPDV AVPDDALSCV VVQGGTVRWV GPVAAVPPAF 

        70         80         90        100        110        120 
AALPRHAGGG ALATPGLVDC HTHLVYGGHR ANEFAMRLAG ASYEEVARAG GGIVSSVKAT 

       130        140        150        160        170        180 
RAASEDELFA QALPRLQALL DEGVCAIEIK SGYGLALEHE RKQLRAARRL GEACGVTVRT 

       190        200        210        220        230        240 
TFLGAHALPP EYAGRSQDYI DLVCREMLPA LAEEGLVDAV DVFCERIAFS LAETEQVFQA 

       250        260        270        280        290        300 
AQALGLPVKL HAEQLSDMDG ARLAARYGAL SCDHIEHLSA EGIAAMKAAG TVAVLLPGAY 

       310        320        330        340        350        360 
YTLRDTHLPP IQALREAGVP MAVSTDHNPG TSPALSLRLM ANMACTLFRL TVPEALAGIT 

       370        380        390        400        410 
THAARALGLQ DTHGLIAAGR PADFVLWPFA EAAELAYWFG HQPPQAIVRQ GRVVQR 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM33528.1.
RefSeqYP_971302.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TRE0.

Genome annotation databases

GeneID4668440.
GenomeReviewsGene locus Aave_2961 in contig CP000512_GR.
KEGGaav:Aave_2961.
NMPDRfig|397945.5.peg.2520.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMNMACTL.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005920. HutI.
[Graphical view]
PfamPF07969. Amidohydro_3. 1 hit.
[Graphical view]
ProDomPD001248. Amidohydro_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_ACIAC
AccessionPrimary (citable) accession number: A1TRE0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents