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Reviewed, UniProtKB/Swiss-Prot Q5FRS2 (HUTI_GLUOX)

Last modified November 3, 2009. Version 27. 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: GOX1163
OrganismGluconobacter oxydans (Gluconobacter suboxydans) [Complete proteome] [HAMAP]
Taxonomic identifier442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconobacter

Protein attributes

Sequence length412 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 – 412412Imidazolonepropionase HAMAP MF_00372
PRO_0000306463

Sites

Metal binding761Zinc or iron By similarity
Metal binding781Zinc or iron By similarity
Metal binding2461Zinc or iron By similarity
Metal binding3211Zinc or iron By similarity
Binding site851Substrate By similarity
Binding site981Substrate By similarity
Binding site1481Substrate By similarity
Binding site1811Substrate By similarity
Binding site2491Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5FRS2-1 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 04873235E2A0DC4C

FASTA41245,076
        10         20         30         40         50         60 
MWDTLWTDIH VATADPALIS DQDGYGCIHN AAIGIENGRI SWIGAARDLP DAPQNLAHKI 

        70         80         90        100        110        120 
HSGNGLWMTP GLVDAHTHVI YAGDRSLEFA ERLNGVSYEE IARKGGGIIS TVNATRHVSE 

       130        140        150        160        170        180 
DELFDVTARR VRRMIAEGTT TLEMKSGYGL TLQDELKQLR VARAIGTALP VRVHATFLGA 

       190        200        210        220        230        240 
HALPSEFKDR QDDYVSHLIT DILPQAVEEK LIDSIDGFCE NIAFTPDQIE RLFIAANDLK 

       250        260        270        280        290        300 
IPVRLHSEQL SNSGGTKLAA RYGALSTDHL EYVVEDDVID LAHAGTVAML LPGAFYFIRE 

       310        320        330        340        350        360 
TRMPPVDLFR KHNVPMGLAT DCNPGTSPSV SLTGIMNMAC TLFRMTPEET FSAVTRIGAQ 

       370        380        390        400        410 
ALGLQNVTGS LTTGQTADML LWDLAGPHEL SYWIGGRRPV QRVFDGKLNP VI 

« Hide

References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

CP000009 Genomic DNA. Translation: AAW60924.1.
RefSeqYP_191580.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3249738.
GenomeReviewsGene locus GOX1163 in contig CP000009_GR.
KEGGgox:GOX1163.
NMPDRfig|290633.1.peg.1125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5FRS2.
OMAMNMACTL.

Enzyme and pathway databases

BioCycGOXY290633:GOX1163-MON.
BRENDA3.5.2.7. 3050.

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...

Entry information

Entry nameHUTI_GLUOX
AccessionPrimary (citable) accession number: Q5FRS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2005
Last modified: November 3, 2009
This is version 27 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