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Q8YD09 (HUTIH_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional imidazolonepropionase/histidine ammonia-lyase

Including the following 2 domains:

  1. Imidazolonepropionase
    EC=3.5.2.7
    Alternative name(s):
    Imidazolone-5-propionate hydrolase
  2. Histidine ammonia-lyase
    Short name=Histidase
    EC=4.3.1.3
Gene names
Name:hutIH
Ordered Locus Names:BMEII0368
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length925 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_00229

L-histidine = urocanate + NH3. HAMAP MF_00229

Cofactor

Binds 1 zinc or iron ion per subunit By similarity. HAMAP MF_00229

Pathway

Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 1/3. HAMAP MF_00229

Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 3/3.

Subcellular location

Cytoplasm Potential HAMAP MF_00229.

Post-translational modification

Contains an active site 4-methylidene-imidazol-5-one (MIO), which is formed autocatalytically by cyclization and dehydration of residues Ala-Ser-Gly By similarity. HAMAP MF_00229

Sequence similarities

In the N-terminal section; belongs to the HutI family.

In the C-terminal section; belongs to the PAL/histidase family.

Sequence caution

The sequence AAL53610.1 differs from that shown. Reason: Frameshift at position 696.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 925925Bifunctional imidazolonepropionase/histidine ammonia-lyase HAMAP MF_00229
PRO_0000160981

Regions

Region1 – 414414Imidazolonepropionase HAMAP MF_00229
Region415 – 925511Histidine ammonia-lyase HAMAP MF_00229

Sites

Metal binding731Zinc or iron By similarity
Metal binding751Zinc or iron By similarity
Metal binding2431Zinc or iron By similarity
Metal binding3181Zinc or iron By similarity
Binding site821Substrate By similarity
Binding site951Substrate By similarity
Binding site1451Substrate By similarity
Binding site1781Substrate By similarity
Binding site2461Substrate By similarity

Amino acid modifications

Modified residue55712,3-didehydroalanine (Ser) By similarity
Cross-link556 ↔ 5585-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YD09 [UniParc].

Last modified May 24, 2005. Version 2.
Checksum: 3D7D858028548835

FASTA92597,849
        10         20         30         40         50         60 
MTKNSSTVFT HARIATLEEK AANLGLIEEA ALVVKDARIV YAGPENKLPD EYASFEKIDC 

        70         80         90        100        110        120 
GNRLITPGLI DCHTHLVHAG NRAHEFELRL QGATYEEVAR AGGGIVSSVR NLRAASEDDL 

       130        140        150        160        170        180 
VRETLPRLDA LIAEGVTTVE VKSGYGLDRD SEIKSLKAAR RLGEERDVAI RTTFLGAHAL 

       190        200        210        220        230        240 
PPEMNGDKAA YIDRVINDML PAIAEQGLAD AVDGFCEGIA FLPDEIARVF DAAKAHDIPV 

       250        260        270        280        290        300 
KLHADQLSNL HGAALAASYG ALSADHLEYT DADGAAAMAS AGTVAVLLPG AYYFIRETQK 

       310        320        330        340        350        360 
PPVEAFRAAG TKMALATDNN PGTSPLTSLL LTMNMGATLF RMTVEECIAG VTREAARALG 

       370        380        390        400        410        420 
ILDQTGTLEI GKDADLAIWD IERPAELVYR IGFNPLWKRV FKGQIKPHVR MEPFMTIILK 

       430        440        450        460        470        480 
PGSVPLETLE KIYREGLPVR IDPAFHAGIE KAAARIAEIA AGDAPVYGIN TGFGKLASIR 

       490        500        510        520        530        540 
IAAGDVATLQ RNLILSHCCG VGEPLSENIV RLIMALKLVS LGRGASGVQL EVITLIEAML 

       550        560        570        580        590        600 
EKGVIPMIPE KGSVGASGDL APLAHMTAAM IGEGEAFYRG ERLSGAKALG KAGLKPVVLA 

       610        620        630        640        650        660 
AKEGLALING TQTSTALALA GLFRAHRAAR TALITGALST DAAMGSDAPF HEEIHQLRGH 

       670        680        690        700        710        720 
KGQIDAGRAL RTLLEGSAIR RSHLEGDQRV QDPYCXRCQP QVDGACLDIL RQAARTLEIE 

       730        740        750        760        770        780 
ANAVTDNPLV LSDGRAVSGG NFHAEPVAFA ADQIALAVCE IGAISQRRIA LLVDPSLSFG 

       790        800        810        820        830        840 
LPAFLARKPG LNSGLMIAEV TSAALMSENK QMAHPASVDS TPTSANQEDH VSMACHGARR 

       850        860        870        880        890        900 
LLQMTANLNA IIGIEALTGA LGVELRKPLT TSAELAKVIA ALRAKVATLE EDRYMADDLK 

       910        920 
AAAELVADGT LSGVISAGIL PDLEA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008918 Genomic DNA. Translation: AAL53610.1. Frameshift.
PIRAG3555.
RefSeqNP_541346.1. NC_003318.1.

3D structure databases

ProteinModelPortalQ8YD09.
SMRQ8YD09. Positions 5-404.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1198140.
GenomeReviewsGene locus BMEII0368 in contig AE008918_GR.
KEGGbme:BMEII0368.
PATRIC17800400. VBIBruMel146950_2532.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG365519.
PhylomeDBQ8YD09.

Enzyme and pathway databases

BioCycBMEL224914:BMEII0368-MONOMER.

Family and domain databases

HAMAPMF_00229. His_ammonia-lyase. Fused.
[Tree]
MF_00372. HutI. Fused.
[Tree]
InterProIPR013108. Amidohydro_3.
IPR005921. HutH.
IPR005920. HutI.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR011059. Metal-dep_hydrolase_composite.
IPR001106. Phe/His_NH3-lyase.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view]
Gene3DG3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KOK01468.
PfamPF07969. Amidohydro_3. 1 hit.
PF00221. PAL. 1 hit.
[Graphical view]
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
SSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR01225. HutH. 1 hit.
TIGR01224. HutI. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHUTIH_BRUME
AccessionPrimary (citable) accession number: Q8YD09
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: May 24, 2005
Last modified: January 25, 2012
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families