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Reviewed, UniProtKB/Swiss-Prot P42084 (HUTI_BACSU)

Last modified November 3, 2009. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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: BSU39370
ORF Names: EE57B
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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. 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

Subunit structure

Homodimer. Ref.3

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 term3D-structure
Complete 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 – 421421Imidazolonepropionase HAMAP MF_00372
PRO_0000160944

Sites

Metal binding801Zinc or iron HAMAP MF_00372
Metal binding821Zinc or iron HAMAP MF_00372
Metal binding2491Zinc or iron HAMAP MF_00372
Metal binding3241Zinc or iron HAMAP MF_00372
Binding site891Substrate HAMAP MF_00372
Binding site1021Substrate HAMAP MF_00372
Binding site1521Substrate HAMAP MF_00372
Binding site1851Substrate HAMAP MF_00372
Binding site2521Substrate HAMAP MF_00372

Secondary structure

1 ............................................................................ 421
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P42084-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A0E1893961745771

FASTA42145,564
        10         20         30         40         50         60 
MPKQIDTILI NIGQLLTMES SGPRAGKSMQ DLHVIEDAVV GIHEQKIVFA GQKGAEAGYE 

        70         80         90        100        110        120 
ADEIIDCSGR LVTPGLVDPH THLVFGGSRE KEMNLKLQGI SYLDILAQGG GILSTVKDTR 

       130        140        150        160        170        180 
AASEEELLQK AHFHLQRMLS YGTTTAEVKS GYGLEKETEL KQLRVAKKLH ESQPVDLVST 

       190        200        210        220        230        240 
FMGAHAIPPE YQNDPDDFLD QMLSLLPEIK EQELASFADI FTETGVFTVS QSRRYLQKAA 

       250        260        270        280        290        300 
EAGFGLKIHA DEIDPLGGAE LAGKLKAVSA DHLVGTSDEG IKKLAEAGTI AVLLPGTTFY 

       310        320        330        340        350        360 
LGKSTYARAR AMIDEGVCVS LATDFNPGSS PTENIQLIMS IAALHLKMTA EEIWHAVTVN 

       370        380        390        400        410        420 
AAYAIGKGEE AGQLKAGRSA DLVIWQAPNY MYIPYHYGVN HVHQVMKNGT IVVNREGAIL 


G

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome containing the hut and wapA loci."
Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.
Microbiology 141:337-343(1995) [PubMed: 7704263] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / BGSC1A1.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis."
Yu Y., Liang Y.-H., Brostromer E., Quan J.-M., Panjikar S., Dong Y.-H., Su X.-D.
J. Biol. Chem. 281:36929-36936(2006) [PubMed: 16990261] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, SUBUNIT.

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Cross-references

Sequence databases

D31856 Genomic DNA. Translation: BAA06642.1.
AL009126 Genomic DNA. Translation: CAB15973.1.
PIRD69643.
RefSeqNP_391816.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2BB0X-ray2.00A/B1-421[»]
2G3FX-ray2.00A/B1-421[»]
ModBaseSearch...

Genome annotation databases

GeneID937531.
GenomeReviewsGene locus BSU39370 in contig AL009126_GR.
KEGGbsu:BSU39370.
NMPDRfig|224308.1.peg.3942.

Organism-specific databases

SubtiListBG11100. hutI. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP42084.
OMAMNMACTL.

Enzyme and pathway databases

BioCycBSUB224308:BSU3933-MON.
MetaCyc:HUTIBACSU-MON.
BRENDA3.5.2.7. 150.

Family and domain databases

HAMAPMF_00372.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005920. HutI.
[Graphical view]
PfamPF07969. Amidohydro_3. 1 hit.
[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_BACSU
AccessionPrimary (citable) accession number: P42084
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 3, 2009
This is version 74 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

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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