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A0KF84 (HUTI_AERHH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:AHA_0377
OrganismAeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]
Taxonomic identifier380703 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence caution

The sequence ABK39901.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHistidine metabolism
   Cellular componentCytoplasm
   LigandIron
Metal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Complete 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 – 411411Imidazolonepropionase HAMAP MF_00372
PRO_0000306422

Sites

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

Secondary structure

1 ........................................................................ 411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A0KF84 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 63D38DB562DC8EBF

FASTA41144,543
        10         20         30         40         50         60 
MNKELLNCER VWLNVTPATL RSDLADYGLL EPHALGVHEG RIHALVPMQD LKGPYPAHWQ 

        70         80         90        100        110        120 
DMKGKLVTPG LIDCHTHLIF AGSRAEEFEL RQKGVPYAEI ARKGGGIIST VRATRAACEE 

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

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

       250        260        270        280        290        300 
AVKGHMDQLS NLGGSTLAAN FGALSVDHLE YLDPEGIQAL AHRGVVATLL PTAFYFLKET 

       310        320        330        340        350        360 
KLPPVAALRK AGVPMAVSSD INPGTAPIVS LRMAMNMACT LFGLTPVEAM AGVTRHAARA 

       370        380        390        400        410 
LGEQEQLGQL RVGMLADFLV WNCGHPAELS YLIGVDQLVS RVINGEETLH G

« Hide

References

[1]"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades."
Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.
J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 7966 / NCIB 9240.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000462 Genomic DNA. Translation: ABK39901.1. Different initiation.
RefSeqYP_854906.1. NC_008570.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OOFX-ray2.20A6-411[»]
2Q09X-ray1.97A6-411[»]
ProteinModelPortalA0KF84.
SMRA0KF84. Positions 6-410.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0KF84.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4486961.
GenomeReviewsGene locus AHA_0377 in contig CP000462_GR.
KEGGaha:AHA_0377.
PATRIC20778238. VBIAerHyd135212_0364.
TIGRAHA_0377.

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHBG686142.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycAHYD196024:AHA_0377-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_AERHH
AccessionPrimary (citable) accession number: A0KF84
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: January 25, 2012
This is version 35 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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