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Reviewed, UniProtKB/Swiss-Prot A3MA48 (HUTI_ACIBT)

Last modified September 1, 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

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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: A1S_3403
OrganismAcinetobacter baumannii (strain ATCC 17978 / NCDC KC 755) [Complete proteome] [HAMAP]
Taxonomic identifier400667 [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_0000306421

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
A3MA48-1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 574D1B36BB792641

FASTA40144,045
        10         20         30         40         50         60 
MKKLWQNCHI ATMQNGQYSY IEDAAIVTEG HLIHWIGKQQ QLPADTYSET 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 RVFKTAQSLN 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]"New insights into Acinetobacter baumannii pathogenesis revealed by high-density pyrosequencing and transposon mutagenesis."
Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N., Gerstein M., Snyder M.
Genes Dev. 21:601-614(2007) [PubMed: 17344419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000521 Genomic DNA. Translation: ABO13792.2.
RefSeqYP_001086394.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA3MA48.

Genome annotation databases

GeneID4917745.
GenomeReviewsGene locus A1S_3403 in contig CP000521_GR.
KEGGacb:A1S_3403.
NMPDRfig|400667.4.peg.3510.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
ProDomPD001248. Amidohydro_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameHUTI_ACIBT
AccessionPrimary (citable) accession number: A3MA48
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: September 1, 2009
This is version 19 of the entry and version 2 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