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Reviewed, UniProtKB/Swiss-Prot Q0BDK6 (HUTH_BURCM)

Last modified June 16, 2009. Version 22. 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

Names and origin

Protein namesRecommended name:
    Histidine ammonia-lyase
      Short name=Histidase
    EC=4.3.1.3
Gene names
Name: hutH
Ordered Locus Names: Bamb_2211
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

L-histidine = urocanate + NH3. 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

Subcellular location

Cytoplasm Potential.

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.

Sequence similarities

Belongs to the PAL/histidase family.

Ontologies

Keywords
   Biological processHistidine metabolism
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processbiosynthetic process

Inferred from electronic annotation. Source: InterPro

histidine catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionammonia ligase activity

Inferred from electronic annotation. Source: InterPro

histidine ammonia-lyase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507Histidine ammonia-lyase HAMAP MF_00229
PRO_1000021549

Amino acid modifications

Modified residue14212,3-didehydroalanine (Ser) By similarity
Cross-link141 ↔ 1435-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BDK6-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 77E97E1B72B5549B

FASTA50753,309
        10         20         30         40         50         60 
MITLTPGHLT LPQLRKIARE SVQLTLDPAS FAKIDAGAKA VADIAAKGEP AYGINTGFGR 

        70         80         90        100        110        120 
LASTHIPHDQ LELLQKNLVL SHAVGVGEPM ARSSVRLLMA LKLSSLGRGH SGIRREVMDA 

       130        140        150        160        170        180 
LITLFNADVL PLIPVKGSVG ASGDLAPLAH MSAVLLGVGE VFIRGERASA LDGLRVAGLA 

       190        200        210        220        230        240 
PLTLQAKEGL ALLNGTQAST ALALDNMFSI EDLYRTALVA GALSVDAAAG SVKPFDARIH 

       250        260        270        280        290        300 
ELRGHRGQID AAAAYRDLLD GSPINQSHRD CDKVQDPYSL RCQPQVMGAC LDQMRHAADV 

       310        320        330        340        350        360 
LLIEANAVSD NPLIFPDTGE VLSGGNFHAE PVAFAADNLA LAAAEIGALA ERRIALLIDA 

       370        380        390        400        410        420 
TLSGLPPFLV KDGGVNSGFM IAHVTAAALA SENKTLAHPA SVDSLPTSAN QEDHVSMATF 

       430        440        450        460        470        480 
AARKLADIAD NTKYILAIEL LAAAQGVDLR APYHTSPKLA PVMETIRGHV AHYELDHYFA 

       490        500 
PDIAVIAKLV SERAFAKVAP FSFASEQ 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000440 Genomic DNA. Translation: ABI87767.1.
RefSeqYP_774101.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4310117.
GenomeReviewsGene locus Bamb_2211 in contig CP000440_GR.
KEGGbam:Bamb_2211.
NMPDRfig|339670.3.peg.3796.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ0BDK6. FAPDIEA.

Family and domain databases

HAMAPMF_00229.
[Tree]
InterProIPR005921. HutH.
IPR001106. Phe/His_NH3-lyase.
[Graphical view]
PfamPF00221. PAL. 1 hit.
[Graphical view]
TIGRFAMsTIGR01225. hutH. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHUTH_BURCM
AccessionPrimary (citable) accession number: Q0BDK6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 22 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)

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