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Q9HLJ0 (HUTI_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable imidazolonepropionase

EC=3.5.2.7
Alternative name(s):
Imidazolone-5-propionate hydrolase
Gene names
Name:hutI
Ordered Locus Names:Ta0238
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length410 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
Reference 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 – 410410Probable imidazolonepropionase HAMAP MF_00372
PRO_0000160979

Sites

Metal binding711Zinc or iron By similarity
Metal binding731Zinc or iron By similarity
Metal binding2351Zinc or iron By similarity
Metal binding3091Zinc or iron By similarity
Binding site801Substrate By similarity
Binding site931Substrate By similarity
Binding site1431Substrate By similarity
Binding site1751Substrate By similarity
Binding site2381Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HLJ0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6F381052AC3A0C01

FASTA41045,006
        10         20         30         40         50         60 
MRALTNLSQI ATGEGRSFLS GERQADVKVY ENHSILIHGG RIAEITRAVP PGVEEIDCGG 

        70         80         90        100        110        120 
GVAVPGFVDP HTHIAFAGNR VQEFYMRIRG TSYLDILRSG NGIYRTIRDT VNADENRIFK 

       130        140        150        160        170        180 
ETISRVWSAV RRGTTTMEMK TGYGLDQRGE EKILSAIEVI KNTGPISVVP TYLAHVVPQD 

       190        200        210        220        230        240 
VQENAYVEGI LETVKRNRQR ISYADIFCDA GAFSPEASRR FLEAAIAMGI PARIHTNEIE 

       250        260        270        280        290        300 
NVGCVKKTRG LPIVSYDHMI HFDDADLDIV KENGSSVTLL PITVFALNEA YPDARRIIDR 

       310        320        330        340        350        360 
GIPVSIATDI SPLNMNDDMI FAMHLAVRNN HMNAEEVLNA ATINPAASLG LAEKKGTIES 

       370        380        390        400        410 
GKDADLVVLS ARSYDEIPYL YGLDIVSMTI SRGNILYSRG DHGITDTSEA 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445063 Genomic DNA. Translation: CAC11383.1.
RefSeqNP_393718.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HLJ0.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1455872.
GenomeReviewsGene locus Ta0238 in contig AL139299_GR.
KEGGtac:Ta0238.
NMPDRfig|273075.1.peg.240.

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
PhylomeDBQ9HLJ0.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycTACI273075:TA0238-MONOMER.

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_THEAC
AccessionPrimary (citable) accession number: Q9HLJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 70 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