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B4RW95 (HUTI_ALTMD) 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

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:MADE_1004495
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

Protein attributes

Sequence length419 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 – 419419Imidazolonepropionase HAMAP MF_00372
PRO_1000121527

Sites

Metal binding871Zinc or iron By similarity
Metal binding891Zinc or iron By similarity
Metal binding2571Zinc or iron By similarity
Metal binding3321Zinc or iron By similarity
Binding site961Substrate By similarity
Binding site1091Substrate By similarity
Binding site1591Substrate By similarity
Binding site1921Substrate By similarity
Binding site2601Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RW95 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 250D5FB21BD60771

FASTA41945,544
        10         20         30         40         50         60 
MDSKYDTLIY NVRIASMQHN GMPYGELPPT AIAIKEGHIV ALLSCDEQLN DALQQTSTVI 

        70         80         90        100        110        120 
DGSRLIPCNE NEQPTLPWLL PGFIDCHTHL VYGGNRAEEF EMRLQGASYV EIAERGGGIK 

       130        140        150        160        170        180 
GTVKKTRQAD EQTLLNTAIK RAMRLCEEGV TTIEVKSGYG LDVDTEIRML SVAKSLEKHL 

       190        200        210        220        230        240 
PVTIQTTYLG AHALPNEFNH DADAYIDFIC RDALPQIASL GLADAVDVFC ETIGFSLQQT 

       250        260        270        280        290        300 
ERVFSCAKQY GLPVKAHVEQ LSDSKGAVLA AKYGALSVDH IEYLVDSDIP SLVKSETVAV 

       310        320        330        340        350        360 
LLPGAFYYLS EVQKPPVEAL RAHNVPIAVA TDFNPGSSPL ASLLTALNMS CVLFKLTPEE 

       370        380        390        400        410 
ALRGATEHAA SALGLNDRGV VDIGNVADLT LWDIETPAEL VYCINGHRPI AVFKDGKHV 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEA97045.1.
RefSeqYP_004426043.1. NC_011138.2.

3D structure databases

ProteinModelPortalB4RW95.
ModBaseSearch...

Protein-protein interaction databases

STRINGB4RW95.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID10556240.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Family and domain databases

HAMAPMF_00372. HutI.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
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_ALTMD
AccessionPrimary (citable) accession number: B4RW95
Secondary accession number(s): F2GB04
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
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