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Reviewed, UniProtKB/Swiss-Prot Q12EQ4 (HUTI_POLSJ)

Last modified June 16, 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: Bpro_1035
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length425 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 – 425425Imidazolonepropionase HAMAP MF_00372
PRO_0000306481

Sites

Metal binding781Zinc or iron By similarity
Metal binding801Zinc or iron By similarity
Metal binding2481Zinc or iron By similarity
Metal binding3231Zinc 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
Q12EQ4-1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 1D52F947C74FA752

FASTA42544,819
        10         20         30         40         50         60 
MTTAPHPAAD GIWEHLRLMP GALADDSPVA TNTEAAIVVT EGRIRWIGAS AALPAGFSAL 

        70         80         90        100        110        120 
PRFDGGGALV TPGLVDCHTH LVYGGQRANE FAMRLAGASY EEVAKAGGGI VSSVRATRAA 

       130        140        150        160        170        180 
GEDELFAQAA PRLEQLLADG VCAIEIKSGY GLALEHERKQ LRVARRLGEA YGVTVRTTFL 

       190        200        210        220        230        240 
GAHALPPEYA GRSQDYIDLV CREMLPALAA EGLVDAVDVF CERIAFSLSE TEQVFQAAQR 

       250        260        270        280        290        300 
LGLPVKLHAE QLSDMGGAAL AARYGALSCD HIEHLSQAGI DAMRAAGTVA VLLPGAYYTL 

       310        320        330        340        350        360 
RDTHLPPIAA LREAGVPMAV STDHNPGTSP ALSLLLMANM ACTLFRLTVP EALAGITRHA 

       370        380        390        400        410        420 
ARALGLQDTH GALGVGRPAN FVLWQLNDSA ELAYWLGQQA PRTIVRQGRV ALDGLQIAPN 


ARITP 

« Hide

References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000316 Genomic DNA. Translation: ABE42988.1.
RefSeqYP_547886.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4012156.
GenomeReviewsGene locus Bpro_1035 in contig CP000316_GR.
KEGGpol:Bpro_1035.
NMPDRfig|296591.1.peg.3371.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ12EQ4.
OMAQ12EQ4. MNMACTL.

Enzyme and pathway databases

BioCycPSP296591:BPRO_1035-MON.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005920. HutI.
[Graphical view]
PfamPF07969. Amidohydro_3. 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_POLSJ
AccessionPrimary (citable) accession number: Q12EQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: August 22, 2006
Last modified: June 16, 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