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Reviewed, UniProtKB/Swiss-Prot A0LZE0 (HUTI_GRAFK)

Last modified November 3, 2009. Version 21. 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: GFO_0758
OrganismGramella forsetii (strain KT0803) [Complete proteome] [HAMAP]
Taxonomic identifier411154 [NCBI]
Taxonomic lineageBacteriaBacteroidetesFlavobacteriaFlavobacterialesFlavobacteriaceaeGramella

Protein attributes

Sequence length411 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 – 411411Imidazolonepropionase HAMAP MF_00372
PRO_0000306464

Sites

Metal binding781Zinc or iron By similarity
Metal binding801Zinc or iron By similarity
Metal binding2481Zinc or iron By similarity
Metal binding3221Zinc or iron By similarity
Binding site871Substrate By similarity
Binding site1001Substrate By similarity
Binding site1501Substrate By similarity
Binding site1831Substrate By similarity
Binding site2511Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LZE0-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 798349CC3C8A97F0

FASTA41145,460
        10         20         30         40         50         60 
MTLLVTNIKE LLQVREQNIL KVSGSEMKEL PTIKNAWLLI ENDKIADFGT MKNMPKITAD 

        70         80         90        100        110        120 
QTIDATGKIV LPTWCDSHTH IVYAGNREQE FADRINGLSY EEIANRGGGI LNSVKTLQDT 

       130        140        150        160        170        180 
SEEEVYEQSA KRLKEVMKLG TGAVEIKSGY GLTEKAELKM LRVIKKLREN YDLPVKSTFL 

       190        200        210        220        230        240 
GAHAIPKEYK NDPDAYMDLV INEILPKVAK EGLAEYIDIF CEKGYFSIKD THRLLSAAKE 

       250        260        270        280        290        300 
HGLKPKIHVN QFNSIGGVKV GVEHEALSVD HLEVMNDEDI EVLKGTRTMP VALPSCSLFL 

       310        320        330        340        350        360 
SIPYTPARKI LDAELPLALA TDFNPGSTPS GNMNLVVSLA CIKMKMTPEE AINAATINGA 

       370        380        390        400        410 
YAMDLSETHG SITKGKMANF MITKEIPSFT FLPYAFGTNS IDSVYINGKL I 

« Hide

References

[1]"Whole genome analysis of the marine Bacteroidetes'Gramella forsetii' reveals adaptations to degradation of polymeric organic matter."
Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E., Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K., Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I., Gloeckner F.O.
Environ. Microbiol. 8:2201-2213(2006) [PubMed: 17107561] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CU207366 Genomic DNA. Translation: CAL65735.1.
RefSeqYP_860802.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA0LZE0.

Genome annotation databases

GeneID4652556.
GenomeReviewsGene locus GFO_0758 in contig CU207366_GR.
KEGGgfo:GFO_0758.
NMPDRfig|411154.5.peg.722.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAMNMACTL.

Family and domain databases

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

Entry information

Entry nameHUTI_GRAFK
AccessionPrimary (citable) accession number: A0LZE0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 12, 2006
Last modified: November 3, 2009
This is version 21 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