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Q6AKP5 (HUTI_DESPS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:DP2351
OrganismDesulfotalea psychrophila [Complete proteome] [HAMAP]
Taxonomic identifier84980 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfobacterales › Desulfobulbaceae › Desulfotalea

Protein attributes

Sequence length414 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 – 414414Imidazolonepropionase HAMAP MF_00372
PRO_0000306459

Sites

Metal binding811Zinc or iron By similarity
Metal binding831Zinc or iron By similarity
Metal binding2511Zinc or iron By similarity
Metal binding3251Zinc or iron By similarity
Binding site901Substrate By similarity
Binding site1031Substrate By similarity
Binding site1531Substrate By similarity
Binding site1861Substrate By similarity
Binding site2541Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6AKP5 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: EED6E2ED896746FB

FASTA41443,833
        10         20         30         40         50         60 
MSHQLFRNTR IYSPMDSGQP SAGKAQGKLA HFPNGALLVA DGLIVAMGDE EAVLAVAKGG 

        70         80         90        100        110        120 
AEVEEVDCGG RCMIPGFVDP HTHMCFAAPR EAEFAQRIAG TSYLQILSEG GGILSSVRAV 

       130        140        150        160        170        180 
ALAGEDELYK STLHRVQTAL SFGTTSLEIK SGYGLDTDNE LKMLRVIGRV AVDSCLDIVA 

       190        200        210        220        230        240 
TFLGAHAIPG QYKTDADAFI TMIVEEMLPR VREQGIARFC DVFCERGVFS IEQSRILLKA 

       250        260        270        280        290        300 
ARAMGLGLKI HADEVTDLGG AGLAAELGAC SADHLLAASD TNIRAMSQAG VIATLLPATA 

       310        320        330        340        350        360 
YSLRKDYARA RVMIENRVAV ALATDCNPGS SFTESMQFVI GLAVLNMEMT PAEALTGASL 

       370        380        390        400        410 
NSAYALNMAD RVGSLDRGKQ ADFLLLEGET PAVLAYHAGV SSVASVYKRG EKVH

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References

[1]"The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from permanently cold Arctic sediments."
Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.
Environ. Microbiol. 6:887-902(2004) [PubMed: 15305914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LSv54 / DSM 12343.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR522870 Genomic DNA. Translation: CAG37080.1.
RefSeqYP_066087.1. NC_006138.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortalQ6AKP5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2946341.
GenomeReviewsGene locus DP2351 in contig CR522870_GR.
KEGGdps:DP2351.
NMPDRfig|177439.1.peg.2351.
PATRIC21714746. VBIDesPsy67261_2563.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycDPSY177439:DP2351-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_DESPS
AccessionPrimary (citable) accession number: Q6AKP5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: September 13, 2004
Last modified: January 25, 2012
This is version 45 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

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