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Reviewed, UniProtKB/Swiss-Prot Q0AP91 (HUTI_MARMM)

Last modified June 16, 2009. Version 20. 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: Mmar10_1604
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

Protein attributes

Sequence length402 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 – 402402Imidazolonepropionase HAMAP MF_00372
PRO_0000306472

Sites

Metal binding691Zinc or iron By similarity
Metal binding711Zinc or iron By similarity
Metal binding2391Zinc or iron By similarity
Metal binding3141Zinc or iron By similarity
Binding site781Substrate By similarity
Binding site911Substrate By similarity
Binding site1411Substrate By similarity
Binding site1741Substrate By similarity
Binding site2421Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AP91-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 7EFC49E6950AA33D

FASTA40242,417
        10         20         30         40         50         60 
MQFDRLLTEA RLATMVAGDD GYGVIEKAAL GIKDGRIAWI GPMSEIPGEA RETERLASRW 

        70         80         90        100        110        120 
VTPALIDCHT HLVFAGDRSD EFERRLGGES YESISRSGGG IARSVEATRA AGAAELAAGA 

       130        140        150        160        170        180 
LTRIDALAQE GVGTVEIKSG YGLTRESERT MLRAARGVER ASGMRVSATL LAAHAVPPEY 

       190        200        210        220        230        240 
KGESGRYIDE ICIPLIREAA REGLADAVDA YCEGIGFSPE ETRRLFIAAK AAGLPVKLHA 

       250        260        270        280        290        300 
DQLSDTGGAR LVAEFGGLSA DHIEYTNAEG IAAMAKAGTV GVLLPGAFYA LNETKKPPVE 

       310        320        330        340        350        360 
AMRAAGVDMA VATDANPGTS PLVSLLTAAN MACILFGLTL PEAFAGMTRN AARALGLHGE 

       370        380        390        400 
IGTLEVGKAA DLAIWDVERP AEIIQWIGRR PLHGRILAGE WQ 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000449 Genomic DNA. Translation: ABI65896.1.
RefSeqYP_756834.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4283926.
GenomeReviewsGene locus Mmar10_1604 in contig CP000449_GR.
KEGGmmr:Mmar10_1604.
NMPDRfig|394221.5.peg.1567.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0AP91.
OMAQ0AP91. MNMACTL.

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_MARMM
AccessionPrimary (citable) accession number: Q0AP91
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 20 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