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Reviewed, UniProtKB/Swiss-Prot Q7P192 (HUTI_CHRVO)

Last modified June 16, 2009. Version 37. 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: CV_0321
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

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Protein attributes

Sequence length413 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

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 – 413413Imidazolonepropionase HAMAP MF_00372
PRO_0000306456

Sites

Metal binding771Zinc or iron By similarity
Metal binding791Zinc or iron By similarity
Metal binding2471Zinc or iron By similarity
Metal binding3221Zinc or iron By similarity
Binding site861Substrate By similarity
Binding site991Substrate By similarity
Binding site1491Substrate By similarity
Binding site1821Substrate By similarity
Binding site2501Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q7P192-1 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: FA4D8A5F69C02F5F

FASTA41343,634
        10         20         30         40         50         60 
MNVPHPHRPS LWLNARLATM DPAHGAPYGA LEGHALLLRD GHIEAVLPQA EADAAAFDGE 

        70         80         90        100        110        120 
VFDLQGRWVT PGFVDCHTHL VYGGSRAAEW EKRLTGVPYQ QIAAEGGGIV STVRATRWLD 

       130        140        150        160        170        180 
EEELALASLP RLKALMAEGV TTVEIKSGYG LTLADELKQL AAARRLQASL PVEVATTLLA 

       190        200        210        220        230        240 
AHAVPPEYAG DADGYVDLVV ESILPVAARA GLAEAVDAFC ESVGFSPAQT RRVFEAARAH 

       250        260        270        280        290        300 
GLKVKGHVEQ LSNLHGAELV AEFGGLSADH IEYLDDAGVA ALKRAGTVAV LLPGAFYFLR 

       310        320        330        340        350        360 
ETQKPPVDKL RAAGVPMAVS TDLNPGTSPF ASIRLAMNQA CVLFGLTPEE ALAGVTRHAA 

       370        380        390        400        410 
QALGRGATHG RLAAGCVADL LVWDIAHPAE LAYSVGVPLL KQRVFRGAAQ HID

« Hide

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References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131.

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Cross-references

Sequence databases

AE016825 Genomic DNA. Translation: AAQ58000.1.
RefSeqNP_899991.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2550792.
GenomeReviewsGene locus CV_0321 in contig AE016825_GR.
KEGGcvi:CV_0321.
NMPDRfig|243365.1.peg.321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ7P192.
OMAQ7P192. MNMACTL.

Enzyme and pathway databases

BioCycCVIO243365:CV_0321-MON.
BRENDA3.5.2.7. 415.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR005920. HutI.
[Graphical view]
PfamPF01979. Amidohydro_1. 2 hits.
[Graphical view]
ProDomPD001248. Amidohydro_like. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01224. hutI. 1 hit.
ProtoNetSearch...

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Entry information

Entry nameHUTI_CHRVO
AccessionPrimary (citable) accession number: Q7P192
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 15, 2003
Last modified: June 16, 2009
This is version 37 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