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B7GUU8 (HUTI_ACIB3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 23. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:ABBFA_000079
OrganismAcinetobacter baumannii (strain AB307-0294) [Complete proteome] [HAMAP]
Taxonomic identifier557600 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
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. 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.

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: 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 – 401401Imidazolonepropionase HAMAP MF_00372
PRO_1000121523

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

Sequences

Sequence LengthMass (Da)Tools
B7GUU8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: AB79F2F280F0491C

FASTA40144,060
        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 RVFKTAQSLG LPVKLHAEQL 

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

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

       370        380        390        400 
LEQGKVADFV AWDIEHPSEI VYWLGGDLPK RVVQHGQEVI F

« Hide

References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AB307-0294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001172 Genomic DNA. Translation: ACJ58828.1.
RefSeqYP_002324020.1. NC_011595.1.

3D structure databases

ProteinModelPortalB7GUU8.
ModBaseSearch...

Protein-protein interaction databases

STRINGB7GUU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7060101.
GenomeReviewsGene locus ABBFA_000079 in contig CP001172_GR.
KEGGabb:ABBFA_000079.
PATRIC20701689. VBIAciBau42682_0075.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

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_ACIB3
AccessionPrimary (citable) accession number: B7GUU8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 23 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

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