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UniProtKB/Swiss-Prot entry Q891P9

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name HUTI_CLOTE
Primary accession number Q891P9
Secondary accession numbers None
Integrated into Swiss-Prot on October 2, 2007
Sequence was last modified on June 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 34)
Name and origin of the protein
Protein name Imidazolonepropionase
Synonyms EC 3.5.2.7
Imidazolone-5-propionate hydrolase
Gene name
Name: hutI
OrderedLocusNames: CTC_02320
From
Clostridium tetani [TaxID: 1513] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 3: Inferred from homology;
References
[1]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Massachusetts / E88;
DOI=10.1073/pnas.0335853100; PubMed=12552129 [NCBI, ExPASy, EBI, Israel, Japan]
Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
"The genome sequence of Clostridium tetani, the causative agent of tetanus disease.";
Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AE015927; AAO36796.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_782859.1; -.
3D structure databases
ModBase Q891P9.
Enzyme and pathway databases
BioCyc CTET212717:CTC_02320-MON; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0050480; Molecular function: imidazolonepropionase activity (inferred from electronic annotation from HAMAP).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0019556; Biological process: histidine catabolic process to glutamate and formamide (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
HAMAP MF_00372; -; 1.
PBIL [Tree]
InterPro IPR006680; Amidohydro_1.
IPR005920; HutI.
Graphical view of domain structure.
Pfam PF01979; Amidohydro_1; 1.
Pfam graphical view of domain structure.
ProDom PD001248; Amidohydro_like; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01224; hutI; 1.
BLOCKS Q891P9.
ProtoNet Q891P9.
Genome annotation databases
GeneID 1058694; -.
GenomeReviews AE015927_GR; CTC_02320.
KEGG ctc:CTC02320; -.
NMPDR fig|212717.1.peg.2081; -.
Phylogenomic databases
HOGENOM Q891P9; -.
Genome annotation databases
CMR Q891P9; CTC_02320.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Histidine metabolism; Hydrolase; Iron; Metal-binding; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   419  419     Imidazolonepropionase. PRO_0000306457
METAL   82    82        Zinc or iron (By similarity). 
METAL   84    84        Zinc or iron (By similarity). 
METAL   252   252        Zinc or iron (By similarity). 
METAL   326   326        Zinc or iron (By similarity). 
BINDING   91    91        Substrate (By similarity). 
BINDING   104   104        Substrate (By similarity). 
BINDING   154   154        Substrate (By similarity). 
BINDING   187   187        Substrate (By similarity). 
BINDING   255   255        Substrate (By similarity). 
Sequence information
Length: 419 AA [This is the length of the unprocessed precursor] Molecular weight: 46125 Da [This is the MW of the unprocessed precursor] CRC64: FDC85F6E21E3E146 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKKGNVIIKN ASQVITCSGF EGKFGKDMNN INVIENASVV VEDGIIKEIG SLEDILKKYN 

        70         80         90        100        110        120 
EKHFEIVDAS NKAVLPGFVD SHTHFVFGGF RAEEFSWRLN GESYMDIMNK GGGIVNSVRG 

       130        140        150        160        170        180 
TREATEDELY ESAKKRLDSM IHFGVTTVEG KSGYGLDYET ELKQLRVMDR LQKDHSIDIC 

       190        200        210        220        230        240 
KTFMGAHATP EEYRGRNEEY INFIIEDVLP KVAEEKLAEF CDVFCEEGVF SVEESRKILL 

       250        260        270        280        290        300 
KAKELGMKIK LHADEIVQLG GAELAAELGA TSADHLLHAS DEGIKAMADK KVIATLLPTT 

       310        320        330        340        350        360 
AFCLKEPFAR ARMMIDKGGA VALGTDFNPG SGFTNSIPLM FALATIYMDM SIEEAISAMT 

       370        380        390        400        410 
INGAAAIGRA ETIGSIDKGK KGDLVILEYP SYKFLPYNTG VNIVETVIKD GNIVYKKSY
Q891P9 in FASTA format

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