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B4UEL6 (HUTI_ANASK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:AnaeK_2360
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length421 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: EC

metal 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_1000121528

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
B4UEL6 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: C027508A521444CD

FASTA42143,645
        10         20         30         40         50         60 
MSRPTATLVL RNAVVATCDR GPSDAGLLPG AAVAVEGRRV AWVGRDRDLE AEVNAGGAQV 

        70         80         90        100        110        120 
IDARGGLVTP GLVDSHTHLV FAGERAGEFA LRCAGRSYLQ VALSGGGIAV TTRATRAAPD 

       130        140        150        160        170        180 
EQLLADAAAR ARRLIAQGVT TIEVKSGYGL DAPEELRLLR IVHRLGDALG GDATILPTLL 

       190        200        210        220        230        240 
FHAVPPEQVG DRAGFVREAC ASLIPQVARE RLAGFCDVFV EDGAFAPDEA RLLLQAAKDR 

       250        260        270        280        290        300 
GLVPRVHAEQ LTAGGGARLA AELGCSSADH LEELDDAGVA ALAEARVVAG LLPLSTLFLG 

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

       370        380        390        400        410        420 
RALRQPDLGR IARGADADLV LWGCGSPEHL AWHMAVNHAL AVVKHGRVVH QAPAVAMVDC 


R

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References

[1]"Complete sequence of Anaeromyxobacter sp. K."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001131 Genomic DNA. Translation: ACG73587.1.
RefSeqYP_002134716.1. NC_011145.1.

3D structure databases

ProteinModelPortalB4UEL6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4UEL6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6783950.
GenomeReviewsGene locus AnaeK_2360 in contig CP001131_GR.
KEGGank:AnaeK_2360.
PATRIC20939375. VBIAnaSp90767_2378.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01468.
PANTHERPTHR22642. PTHR22642. 1 hit.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01224. HutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_ANASK
AccessionPrimary (citable) accession number: B4UEL6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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