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Reviewed, UniProtKB/Swiss-Prot A4SSN5 (HUTI_AERS4)

Last modified November 3, 2009. Version 17. 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: ASA_3955
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length411 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 – 411411Imidazolonepropionase HAMAP MF_00372
PRO_0000306423

Sites

Metal binding751Zinc or iron By similarity
Metal binding771Zinc or iron By similarity
Metal binding2451Zinc or iron By similarity
Metal binding3201Zinc or iron By similarity
Binding site841Substrate By similarity
Binding site971Substrate By similarity
Binding site1471Substrate By similarity
Binding site1801Substrate By similarity
Binding site2481Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SSN5-1 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 821EDD22C8AA6D1F

FASTA41144,527
        10         20         30         40         50         60 
MNKELLNCER VWLNVTPATL RPDLADYGLL EPHALGVHEG KIHALVPMQD LKGPYPAHWQ 

        70         80         90        100        110        120 
DMKGKLATPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI ARKGGGILST VRATRAASEE 

       130        140        150        160        170        180 
QLFTLAAARI KSLIREGVTT VEIKSGYGLT LEDELKMLRV ARRLGEALPI RVKTTLLAAH 

       190        200        210        220        230        240 
AVPPEYRDDP DSWVETICQE IIPAAAEAGL ADAVDVFCEH IGFSLAQTEQ VYLAADQYGL 

       250        260        270        280        290        300 
PVKGHMEQLS NLGGSALAAN FGALSVDHLE HLDQEGIQAL AHRGVVATLL PTAFYFLKET 

       310        320        330        340        350        360 
KLPPVAALRK AHVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM VGVTRNAARA 

       370        380        390        400        410 
LGEQERLGQL RVGMLADFLV WNCAHPAELS YLIGVDQLVS RVVNGEETLH G 

« Hide

References

[1]"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449."
Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000644 Genomic DNA. Translation: ABO91907.1.
RefSeqYP_001143655.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA4SSN5.

Genome annotation databases

GeneID4996312.
GenomeReviewsGene locus ASA_3955 in contig CP000644_GR.
KEGGasa:ASA_3955.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMNMACTL.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
PfamPF01979. Amidohydro_1. 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_AERS4
AccessionPrimary (citable) accession number: A4SSN5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 15, 2007
Last modified: November 3, 2009
This is version 17 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