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Reviewed, UniProtKB/Swiss-Prot Q6MJP9 (HUTI_BDEBA)

Last modified February 9, 2010. Version 35. 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

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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: Bd2721
OrganismBdellovibrio bacteriovorus [Complete proteome] [HAMAP]
Taxonomic identifier959 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio

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Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423Imidazolonepropionase HAMAP MF_00372
PRO_0000306439

Sites

Metal binding911Zinc or iron By similarity
Metal binding931Zinc or iron By similarity
Metal binding2571Zinc or iron By similarity
Metal binding3311Zinc or iron By similarity
Binding site1001Substrate By similarity
Binding site1131Substrate By similarity
Binding site1631Substrate By similarity
Binding site1931Substrate By similarity
Binding site2601Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q6MJP9-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 811E864E81340D00

FASTA42346,553
        10         20         30         40         50         60 
MGPMCLNRHM GILLKNISTL LTLQGAAAKQ GRRIKEEDLS LLQQAAVVIE KNKIVWVGPQ 

        70         80         90        100        110        120 
KKLPKEFARK KALRDYDMRG RTVLPGFVEC HTHLIFAGDR AAEFEMRNQG VSYQEIAAKG 

       130        140        150        160        170        180 
GGILSTMKKT RASSLNDLVK AGQRRLDHFV SQGVTTVEIK SGYALNLKDE LKMLQAAQKL 

       190        200        210        220        230        240 
SGIRTVNTFL GAHALPPEFK SYEDYLTFLA DEVLPVVAKK KLARRVDVFI EKGFFPPEAS 

       250        260        270        280        290        300 
EKYLRRAQEL GFEILIHADQ MSLSGGSEIA VRLGALSGDH LLQIEDKEIR KLAQSEVTGV 

       310        320        330        340        350        360 
LLPTADLYTK TKYPPARAMI DAGVRVALAT DFNPGTSPTQ NLNLVGLLAR LEMKMSLPEV 

       370        380        390        400        410        420 
IAAYTVGGAH ALNLQNEVGS LEVGKSADIL CIDQDWQTLF YSVGEASEKV VFSRGKKVFG 


TLK

« Hide

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References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / HD100 / DSM 50701 / NCIB 9529.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842653 Genomic DNA. Translation: CAE80511.1.
RefSeqNP_969518.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
SMRQ6MJP9. Positions 8-420.
ModBaseSearch...

Genome annotation databases

GeneID2736242.
KEGGbba:Bd2721.
NMPDRfig|264462.1.peg.2490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.

Enzyme and pathway databases

BioCycBBAC264462:BD2721-MONOMER.
BRENDA3.5.2.7. 3459.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameHUTI_BDEBA
AccessionPrimary (citable) accession number: Q6MJP9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 5, 2004
Last modified: February 9, 2010
This is version 35 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)

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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