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Reviewed, UniProtKB/Swiss-Prot Q0BZK3 (HUTI_HYPNA)

Last modified June 16, 2009. Version 22. 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: HNE_2395
OrganismHyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]
Taxonomic identifier228405 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeHyphomonas

Protein attributes

Sequence length406 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 – 406406Imidazolonepropionase HAMAP MF_00372
PRO_0000306466

Sites

Metal binding751Zinc or iron By similarity
Metal binding771Zinc or iron By similarity
Metal binding2451Zinc or iron By similarity
Metal binding3201Zinc or iron By similarity
Binding site841Substrate By similarity
Binding site971Substrate By similarity
Binding site1471Substrate By similarity
Binding site1801Substrate By similarity
Binding site2481Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BZK3-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 7A65FA6FEF7D3823

FASTA40643,060
        10         20         30         40         50         60 
MQKKRIWTNA RLATMAAGLP GLGIVEDGLI AAEGDRITFA GLASDFPYTE GPSTQGYEVT 

        70         80         90        100        110        120 
DCGGRWILPG LIDCHTHLVW AGSRADEFER RLAGASYEEI ARSGGGIRST VSAVRAASEA 

       130        140        150        160        170        180 
ELVAESLPRL NALIGEGVTT IEIKSGYGLN IEDELKQLRA ARALGEVRPI DVETTLLAAH 

       190        200        210        220        230        240 
TLPPEYEGRA DAYIDLVCNE IIPAAAQAGL ASAVDAFCET IGFTPEQTGR VLSAARHHGL 

       250        260        270        280        290        300 
AVKLHADQLS NLQGGALAAR HNALSADHLE YLDEAGIAAM AQAGMVAVML PGAYYVLRET 

       310        320        330        340        350        360 
HPPPLEGLRR AGVSLAISTD CNPGTSPLTS ILLAMNMGAT LFRMTVEECL LGTTRHAARA 

       370        380        390        400 
LGLEKATGTL EAGKLCNLSI WDIDRPAELV NAMGLNPLHT RVWRGQ 

« Hide

References

[1]"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus."
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. expand/collapse author list , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L.
J. Bacteriol. 188:6841-6850(2006) [PubMed: 16980487] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000158 Genomic DNA. Translation: ABI76937.1.
RefSeqYP_761090.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4289897.
GenomeReviewsGene locus HNE_2395 in contig CP000158_GR.
KEGGhne:HNE_2395.
NMPDRfig|228405.5.peg.2309.
TIGRHNE_2395.

Phylogenomic databases

HOGENOMQ0BZK3.
OMAQ0BZK3. MNMACTL.

Enzyme and pathway databases

BioCycHNEP81032:HNE_2395-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_HYPNA
AccessionPrimary (citable) accession number: Q0BZK3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 22 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