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Q81Y47 (HUTI_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. 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:BA_3710, GBAA_3710, BAS3440
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length423 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
Reference 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 – 423423Imidazolonepropionase HAMAP MF_00372
PRO_0000306428

Sites

Metal binding781Zinc or iron By similarity
Metal binding801Zinc or iron By similarity
Metal binding2471Zinc or iron By similarity
Metal binding3221Zinc or iron By similarity
Binding site871Substrate By similarity
Binding site1001Substrate By similarity
Binding site1501Substrate By similarity
Binding site1831Substrate By similarity
Binding site2501Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81Y47 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: AAD4333AEBFF34BD

FASTA42346,171
        10         20         30         40         50         60 
MLDTLLINIG QLLTMDQEDG LLRREAMNTL PVIENGAVGI ENGVITFVGT AEEAKGLQAK 

        70         80         90        100        110        120 
EVIDCGGKMV SPGLVDPHTH LVFGGSRENE IALKLQGVPY LEILEQGGGI LSTVNATKQA 

       130        140        150        160        170        180 
SKEELVQKAK FHLDRMLSFG VTTVEAKSGY GLDDETEWKQ LEATAQLQKE HPIDLVSTFL 

       190        200        210        220        230        240 
GAHAVPKEYK GRSKEFLQWM LDLLPEMKEK QLAEFVDIFC ETGVFSVEES KEFLLKAKEL 

       250        260        270        280        290        300 
GFDVKIHADE IDPLGGAEAA AEIGAASADH LVGASDKGIE MLANSNTVAT LLPGTTFYLN 

       310        320        330        340        350        360 
KESFARGRKM IDEGVAVALA TDFNPGSCPT ENIQLIMSIA MLKLKMTPEE VWNAVTVNSS 

       370        380        390        400        410        420 
YAINRGDVAG KIRVGRKADL VLWDAYNYAY VPYHYGVSHV NTVWKNGNIA YTRGEQSWST 


ATI

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.
[3]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016879 Genomic DNA. Translation: AAP27459.1.
AE017334 Genomic DNA. Translation: AAT32818.1.
AE017225 Genomic DNA. Translation: AAT55747.1.
RefSeqNP_845973.1. NC_003997.3.
YP_020343.1. NC_007530.2.
YP_029696.1. NC_005945.1.

3D structure databases

HSSPHSSP built from PDB template 2GOK based on UniProtKB Q8U8Z6.
ProteinModelPortalQ81Y47.
SMRQ81Y47. Positions 2-413.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000008252; EBBACP00000008008; EBBACG00000008244.
EBBACT00000014179; EBBACP00000013800; EBBACG00000014171.
EBBACT00000024152; EBBACP00000023637; EBBACG00000024143.
GeneID1086228.
2818284.
2851420.
GenomeReviewsGene locus BA_3710 in contig AE016879_GR.
Gene locus BAS3440 in contig AE017225_GR.
Gene locus GBAA_3710 in contig AE017334_GR.
KEGGban:BA_3710.
bar:GBAA_3710.
bat:BAS3440.
TIGRBA_3710.
GBAA_3710.

Phylogenomic databases

GeneTreeEBGT00050000002251.
HOGENOMHBG686142.
OMAMNMACTL.
ProtClustDBPRK09356.

Enzyme and pathway databases

BioCycBANT260799:BAS3440-MONOMER.
BANT261594:GBAA3710-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_BACAN
AccessionPrimary (citable) accession number: Q81Y47
Secondary accession number(s): Q6HVE2, Q6KPL1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 69 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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