Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A8MF65 (HUTI_ALKOO)

Last modified February 9, 2010. Version 17. 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: Clos_1188
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
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. 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 HAMAP MF_00372.

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 – 422422Imidazolonepropionase HAMAP MF_00372
PRO_1000059942

Sites

Metal binding821Zinc or iron By similarity
Metal binding841Zinc or iron By similarity
Metal binding2521Zinc or iron By similarity
Metal binding3271Zinc or iron By similarity
Binding site911Substrate By similarity
Binding site1041Substrate By similarity
Binding site1541Substrate By similarity
Binding site1871Substrate By similarity
Binding site2551Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8MF65-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: DE5043412735781B

FASTA42245,757
        10         20         30         40         50         60 
MNIDVWIKNI TQLVTVQAHG KPKKGKEMQD VGIIQDGWIA VAGDRIVGIG SGEISADFQV 

        70         80         90        100        110        120 
GENTVIISGE GKTVTPGLID PHTHLVHAGS RENELALKLK GVPYLEILKQ GGGILSTVNA 

       130        140        150        160        170        180 
TKKATMEELV AQSKKSLDRM LSYGVTTVEI KSGYGLELEA EIKQLEAIHR LQQQTPMDLV 

       190        200        210        220        230        240 
STFMGAHAIP KEYKENPEEF IDLIIEEMLP AIKEKNLAEF CDVFCEEGVF SVDQTRRILE 

       250        260        270        280        290        300 
AARSLGFKNK IHADEIVPLG GAELAAELQT ISAEHLMAAS ETGLKMMAES NVVPVALPGT 

       310        320        330        340        350        360 
SFNLATGKYA DARKMIEYGL PVALATDYNP GSCPTENIQL IMSIGCLYLK MTPEEVISAV 

       370        380        390        400        410        420 
TINAAAAIDR TQEIGSIEVG KKADITIFDA PNLYYIPYHF GVNHVDTVLK SGKIVVEKGN 


VI 

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000853 Genomic DNA. Translation: ABW18734.1.
RefSeqYP_001512730.1.

3D structure databases

SMRA8MF65. Positions 7-418.
ModBaseSearch...

Genome annotation databases

GeneID5676593.
GenomeReviewsGene locus Clos_1188 in contig CP000853_GR.
KEGGaoe:Clos_1188.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_ALKOO
AccessionPrimary (citable) accession number: A8MF65
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: February 9, 2010
This is version 17 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