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Reviewed, UniProtKB/Swiss-Prot Q2IHZ6 (HUTI_ANADE)

Last modified June 16, 2009. Version 22. 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: Adeh_1507
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length421 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

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 – 421421Imidazolonepropionase HAMAP MF_00372
PRO_0000306424

Sites

Metal binding761Zinc or iron By similarity
Metal binding781Zinc or iron By similarity
Metal binding2471Zinc or iron By similarity
Metal binding3221Zinc or iron By similarity
Binding site851Substrate By similarity
Binding site981Substrate By similarity
Binding site1481Substrate By similarity
Binding site1821Substrate By similarity
Binding site2501Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IHZ6-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 89EA666B75B8992F

FASTA42143,894
        10         20         30         40         50         60 
MSRPAATLVL RNAVVATCDR GPSDAGLLPG AAVAVEGRRV AWVGRERDVE AEVNLAGAQV 

        70         80         90        100        110        120 
IDARGGLVTP GLVDSHTHLV FAGERAGEFA LRCAGRTYLQ VALSGGGIAV TTRETRAAPD 

       130        140        150        160        170        180 
EQLLAAAAAR ARRLIAQGVT TLEVKSGYGL DAPEELRLLR IVHQLGRALG GDATILPTLL 

       190        200        210        220        230        240 
FHAVPPEQVG DRAGFVRDAC ASLIPQVARE RLAQFCDVFV EDGAFAPDEA RLLLQAAKDR 

       250        260        270        280        290        300 
GLVPRVHAEQ LTAGGGARLA AELGCSSADH LEELDDAGIA ALAQARVVAG LLPLSTLFLG 

       310        320        330        340        350        360 
SERYAPARRL LEAGVPVSLA TNMNPGSAMS ENVGLTLSLA CLKLRLTPAE ALVAFTAGGA 

       370        380        390        400        410        420 
RALRQPDLGR VARGADADLV LWGCGSPEHL AWHMAVNHAL VVVKHGRVVH EAPPAAMVDC 


R 

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References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000251 Genomic DNA. Translation: ABC81280.1.
RefSeqYP_464717.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3887917.
GenomeReviewsGene locus Adeh_1507 in contig CP000251_GR.
KEGGade:Adeh_1507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2IHZ6.
OMAQ2IHZ6. MNMACTL.

Enzyme and pathway databases

BioCycADEH290397:ADEH_1507-MON.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005920. HutI.
[Graphical view]
PfamPF07969. Amidohydro_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_ANADE
AccessionPrimary (citable) accession number: Q2IHZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 7, 2006
Last modified: June 16, 2009
This is version 22 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