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Q9HQD6 (HUTI_HALSA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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

Names and origin

Protein namesRecommended name:
Probable imidazolonepropionase

EC=3.5.2.7
Alternative name(s):
Imidazolone-5-propionate hydrolase
Gene names
Name:hutI
Ordered Locus Names:VNG_1211G
OrganismHalobacterium salinarium (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium)
Taxonomic identifier64091 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium

Protein attributes

Sequence length417 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
Reference 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 – 417417Probable imidazolonepropionase HAMAP MF_00372
PRO_0000160978

Sites

Metal binding771Zinc or iron By similarity
Metal binding791Zinc or iron By similarity
Metal binding2441Zinc or iron By similarity
Metal binding3231Zinc or iron By similarity
Binding site861Substrate By similarity
Binding site991Substrate By similarity
Binding site1491Substrate By similarity
Binding site1821Substrate By similarity
Binding site2471Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HQD6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 3D2EF2B8918D3CF1

FASTA41742,297
        10         20         30         40         50         60 
MSSLDAVVHG ARELVVGPAA GGDTLETHAD GAVAVVDGAV AAVGDTADVL AAYPAENATT 

        70         80         90        100        110        120 
AIDATGKTVL PGFVDPHTHA LFAGDRSDEF AAKLRGKPYQ EILAEGGGIL RTVDAVRAAS 

       130        140        150        160        170        180 
DAALVANLTA QLDVMLAHGT TTAEVKTGYG LDTETECRML DAIAAAAAEH PVDVVTTFLG 

       190        200        210        220        230        240 
AHAVPDDTDA DAYVDAVIDD QLPAAANGPA RFCDVFCEAD VFTVEQSRRI LDAGREHGLA 

       250        260        270        280        290        300 
PKLHAEEFTR LGGAQLAADL GATSADHLLH ATPEDAAALA DAGVTPVLLP ATAFVLDEAY 

       310        320        330        340        350        360 
ADPQQFLAAA DNRTGAPVAL GTDLNPNCYT HSMGFVVSLA CNGMRMAPAD AVLAATAWAA 

       370        380        390        400        410 
SALDRGRDGT GTLREGTDGD VLVVDAPSHV HLPYNPGVNN VEAVLTDGTV AVGGGGA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004437 Genomic DNA. Translation: AAG19579.1.
PIRG84276.
RefSeqNP_280099.1. NC_002607.1.

3D structure databases

ProteinModelPortalQ9HQD6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1447878.
GenomeReviewsGene locus VNG_1211G in contig AE004437_GR.
KEGGhal:VNG1211G.
NMPDRfig|64091.1.peg.1118.

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycHSP64091:VNG1211G-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_HALSA
AccessionPrimary (citable) accession number: Q9HQD6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 69 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