Skip Header

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

Q637I0 (HUTI_BACCZ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:BCE33L3352
OrganismBacillus cereus (strain ZK / E33L) [Complete proteome] [HAMAP]
Taxonomic identifier288681 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length423 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 – 423423Imidazolonepropionase HAMAP MF_00372
PRO_0000306431

Sites

Metal binding781Zinc or iron By similarity
Metal binding801Zinc or iron By similarity
Metal binding2471Zinc or iron By similarity
Metal binding3221Zinc or iron By similarity
Binding site871Substrate By similarity
Binding site1001Substrate By similarity
Binding site1501Substrate By similarity
Binding site1831Substrate By similarity
Binding site2501Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q637I0 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: AFD88B9714ED4F92

FASTA42346,199
        10         20         30         40         50         60 
MLDTLLINIG QLLTMDQEDG LLRREAMNTL PVIENGAVGI ENGVITFVGT VEEAKGLQAK 

        70         80         90        100        110        120 
EVIDCGGKMV SPGLVDPHTH LVFGGSRENE IALKLQGVPY LEILEKGGGI LSTVNATKQA 

       130        140        150        160        170        180 
SKEELVQKAK FHLDRMLSFG VTTVEAKSGY GLDDETEWKQ LEATAQLQKE HPIDLVSTFL 

       190        200        210        220        230        240 
GAHAVPKEYK GRSKEFLQWM LDLLPEMKEK QLAEFVDIFC ETGVFSVEES KDFLLKAKEL 

       250        260        270        280        290        300 
GFDVKIHADE IDPLGGAEAA AEIGAASADH LVGASDKGIE MLANSNTVAT LLPGTTFYLN 

       310        320        330        340        350        360 
KESFARGRKM IDEGVAVALA TDFNPGSCPT ENIQLIMSIA MLKLKMTPEE VWNAVTVNSS 

       370        380        390        400        410        420 
YAINRGEVAG KIRVGRKADL VLWDAYNYAY VPYHYGVSHV NTVWKNGNIA YTRGEQSWST 


ATI

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000001 Genomic DNA. Translation: AAU16911.1.
RefSeqYP_084937.1. NC_006274.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortalQ637I0.
SMRQ637I0. Positions 2-413.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ637I0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000040954; EBBACP00000039855; EBBACG00000040945.
GeneID3026762.
GenomeReviewsGene locus BCE33L3352 in contig CP000001_GR.
KEGGbcz:BCZK3352.
PATRIC18890428. VBIBacCer95304_3552.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1228.
GeneTreeEBGT00050000002251.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycBCER288681:BCE33L3352-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_BACCZ
AccessionPrimary (citable) accession number: Q637I0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 50 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents