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Reviewed, UniProtKB/Swiss-Prot B2I2C1 (HUTI_ACIBC)

Last modified November 3, 2009. Version 12. 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

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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: ACICU_03599
OrganismAcinetobacter baumannii (strain ACICU) [Complete proteome] [HAMAP]
Taxonomic identifier405416 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Imidazolonepropionase HAMAP MF_00372
PRO_1000121525

Sites

Metal binding661Zinc or iron By similarity
Metal binding681Zinc or iron By similarity
Metal binding2361Zinc or iron By similarity
Metal binding3111Zinc or iron By similarity
Binding site751Substrate By similarity
Binding site881Substrate By similarity
Binding site1381Substrate By similarity
Binding site1711Substrate By similarity
Binding site2391Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
B2I2C1-1 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: A21C50868EFD4E0A

FASTA40144,018
        10         20         30         40         50         60 
MKKLWQNCHI ATMQNGQYSY IEDAAIVTEG HLIHWIGKQQ QLPTDTYSET VDLNGAWVTP 

        70         80         90        100        110        120 
GFIDCHTHSV FGGNRSVEFE KRLQGVSYAE IAASGGGIAS TVRATREASE EQLLNSALKR 

       130        140        150        160        170        180 
IRCMQQDGVT TIEIKSGYGL NYENERKMLR VIRQIGEKLP MTVKSTCLAA HALPPEYKDQ 

       190        200        210        220        230        240 
SDAYIEHICT EMLPKLHAEG LVDAVDAFCE HLAFSPAQVE RVFKTAQSLG LPVKLHAEQL 

       250        260        270        280        290        300 
SSLGGSSLAA RYHALSADHL EYMTEDDVKA MAASGTVAVL LPGAFYLLRE TQYPPIESLI 

       310        320        330        340        350        360 
KHGVRIALSS DLNPGTSPAL SLRLMLNMGS TLFRLTPEQA LAGVTIHAAQ ALGLEQTHGS 

       370        380        390        400 
LEQGKVADFV AWDIEHPSEI VYWLGGDLPK RVVQHGQEVI F

« Hide

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References

[1]"Whole-genome pyrosequencing of an epidemic multidrug-resistant Acinetobacter baumannii strain belonging to the European clone II group."
Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J., Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.
Antimicrob. Agents Chemother. 52:2616-2625(2008) [PubMed: 18411315] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000863 Genomic DNA. Translation: ACC58908.1.
RefSeqYP_001848255.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6235944.
GenomeReviewsGene locus ACICU_03599 in contig CP000863_GR.
KEGGabc:ACICU_03599.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMNMACTL.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameHUTI_ACIBC
AccessionPrimary (citable) accession number: B2I2C1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: June 10, 2008
Last modified: November 3, 2009
This is version 12 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)

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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