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Reviewed, UniProtKB/Swiss-Prot Q8U8Z6 (HUTI_AGRT5)

Last modified September 1, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: Atu3934
ORF Names: AGR_L_1824
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Complete proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

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Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. 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

Subunit structure

Monomer. Ref.3

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 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: 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 – 419419Imidazolonepropionase HAMAP MF_00372
PRO_0000160942

Regions

Region331 – 3333Substrate HAMAP MF_00372

Sites

Metal binding841Zinc or iron HAMAP MF_00372
Metal binding861Zinc or iron HAMAP MF_00372
Metal binding2541Zinc or iron HAMAP MF_00372
Metal binding3291Zinc or iron HAMAP MF_00372
Binding site931Substrate By similarity
Binding site1061Substrate By similarity
Binding site1561Substrate HAMAP MF_00372
Binding site1891Substrate By similarity
Binding site2571Substrate By similarity

Secondary structure

1 ........................................................................... 419
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q8U8Z6-1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 55D09461815693CF

FASTA41944,400
        10         20         30         40         50         60 
MPGNNSAKGT ATGNATALWR NAQLATLNPA MDGIGAVENA VIAVRNGRIA FAGPESDLPD 

        70         80         90        100        110        120 
DLSTADETTD CGGRWITPAL IDCHTHLVFG GNRAMEFEMR LNGATYEEIA KAGGGIVSSV 

       130        140        150        160        170        180 
RDTRALSDEV LVAQALPRLD TLLSEGVSTI EIKSGYGLDI ETELKMLRVA RRLETLRPVR 

       190        200        210        220        230        240 
IVTSYLAAHA TPADYKGRNA DYITDVVLPG LEKAHAEGLA DAVDGFCEGI AFSVKEIDRV 

       250        260        270        280        290        300 
FAAAQQRGLP VKLHAEQLSN LGGAELAASY NALSADHLEY LDETGAKALA KAGTVAVLLP 

       310        320        330        340        350        360 
GAFYALREKQ LPPVQALRDA GAEIALATDC NPGTSPLTSL LLTMNMGATL FRMTVEECLT 

       370        380        390        400        410 
ATTRNAAKAL GLLAETGTLE AGKSADFAIW DIERPAELVY RIGFNPLHAR IFKGQKVSP

« Hide

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References

« Hide 'large scale' references
[1]"The genome of the natural genetic engineer Agrobacterium tumefaciens C58."
Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P., Clendenning J. expand/collapse author list , Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., Nester E.W.
Science 294:2317-2323(2001) [PubMed: 11743193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Genome sequence of the plant pathogen and biotechnology agent Agrobacterium tumefaciens C58."
Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C. expand/collapse author list , Allinger M., Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.
Science 294:2323-2328(2001) [PubMed: 11743194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution."
Tyagi R., Kumaran D., Burley S.K., Swaminathan S.
Proteins 69:652-658(2007) [PubMed: 17640072] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) IN COMPLEX WITH PRODUCT AND IRON IONS, SUBUNIT.

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Cross-references

Sequence databases

AE007870 Genomic DNA. Translation: AAK89486.2.
PIRAH3040.
D98245.
RefSeqNP_356701.2.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2GOKX-ray1.87A/B2-419[»]
2PUZX-ray1.83A/B1-419[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8U8Z6.

Genome annotation databases

GeneID1135808.
GenomeReviewsGene locus Atu3934 in contig AE007870_GR.
KEGGatc:AGR_L_1824.
atu:Atu3934.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8U8Z6.

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_AGRT5
AccessionPrimary (citable) accession number: Q8U8Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2002
Last modified: September 1, 2009
This is version 51 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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