Skip Header

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

A3NX99 (HUTI_BURP0) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:BURPS1106A_2719
OrganismBurkholderia pseudomallei (strain 1106a) [Complete proteome] [HAMAP]
Taxonomic identifier357348 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length407 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 – 407407Imidazolonepropionase HAMAP MF_00372
PRO_0000306451

Sites

Metal binding681Zinc or iron By similarity
Metal binding701Zinc or iron By similarity
Metal binding2381Zinc or iron By similarity
Metal binding3131Zinc or iron By similarity
Binding site771Substrate By similarity
Binding site901Substrate By similarity
Binding site1401Substrate By similarity
Binding site1731Substrate By similarity
Binding site2411Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3NX99 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 0FA4A3A98DB8E369

FASTA40743,777
        10         20         30         40         50         60 
MKSILWHNLK LCAHGDPNDT IADAAIAVNG DGTIAWTGRA SDVPAGYVHW PREDLRGAWV 

        70         80         90        100        110        120 
TPGLVDCHTH LVYGGQRADE FAQRLAGASY EEIAQRGGGI VSTVRATRDA SEAALFEQAC 

       130        140        150        160        170        180 
ARLRPLLAEG VTAIEIKSGY GLELASERRM LRVARQLGER FPVSVYTTFL GAHALPPEYA 

       190        200        210        220        230        240 
GRADEYIDEV CERMLPALAD EGLVDAVDVF CERIGFTLAQ SERVFEAAAR RGLPVKMHAE 

       250        260        270        280        290        300 
QLSNGGGSAL AARYRALSAD HLEYLDAAGV AAMRASGTTA VLLPGAYYFI RETKLPPIDL 

       310        320        330        340        350        360 
LRRHGVPIAL ATDHNPGTSP LTSLLLTMNM GCTVFKLTVQ EALLGVTRHA AAALGASDRH 

       370        380        390        400 
GSLAPGRQAD FAVWSVSTLA ELAYWFGRPL CERVVKGGVT VFTRDAR

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1106a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000572 Genomic DNA. Translation: ABN89106.1.
RefSeqYP_001066970.1. NC_009076.1.

3D structure databases

ProteinModelPortalA3NX99.
SMRA3NX99. Positions 3-401.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3NX99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4903048.
GenomeReviewsGene locus BURPS1106A_2719 in contig CP000572_GR.
KEGGbpl:BURPS1106A_2719.
PATRIC19223826. VBIBurPse14980_2569.
TIGRBURPS1106A_2719.

Phylogenomic databases

eggNOGCOG1228.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

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_BURP0
AccessionPrimary (citable) accession number: A3NX99
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 33 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