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Reviewed, UniProtKB/Swiss-Prot Q81AC8 (HUTI_BACCR)

Last modified November 3, 2009. Version 39. 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: BC_3650
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 423423Imidazolonepropionase HAMAP MF_00372
PRO_0000306430

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
Q81AC8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FFA030EBD0CD8AE7

FASTA42346,211
        10         20         30         40         50         60 
MLDTLLINIG QLLTMDQEDG LLRREAMNTL PVIENGVVGI ENGVITFVGT AEEAKGLQAK 

        70         80         90        100        110        120 
EVIDSGGKMV SPGLVDPHTH LVFGGSRENE IALKLQGVPY LEILEQGGGI LSTVNATKQA 

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

       190        200        210        220        230        240 
GAHAVPKEYK GRSKEFLQWM LDLLPEMKEK QLVEFVDIFC ETGVFSVEES KEFLLKAKEL 

       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 
YAINRGDVAG KIRVGRKADL VLWDAYNYAY VPYHYGVSHV NTVWKNGNIA YTRGEQSWST 


ATI 

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References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE016877 Genomic DNA. Translation: AAP10579.1.
RefSeqNP_833378.1.

3D structure databases

SMRQ81AC8. Positions 2-413.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81AC8.

Genome annotation databases

GeneID1205995.
GenomeReviewsGene locus BC_3650 in contig AE016877_GR.
KEGGbce:BC3650.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ81AC8.
OMAMNMACTL.

Enzyme and pathway databases

BioCycBCER226900:BC_3650-MON.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
ProDomPD001248. Amidohydro_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHUTI_BACCR
AccessionPrimary (citable) accession number: Q81AC8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: November 3, 2009
This is version 39 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