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Reviewed, UniProtKB/Swiss-Prot Q11E18 (HUTH_MESSB)

Last modified June 16, 2009. Version 24. 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: Meso_2985
OrganismMesorhizobium sp. (strain BNC1) [Complete proteome] [HAMAP]
Taxonomic identifier266779 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length511 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 – 511511Histidine ammonia-lyase HAMAP MF_00229
PRO_1000021560

Amino acid modifications

Modified residue14312,3-didehydroalanine (Ser) By similarity
Cross-link142 ↔ 1445-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q11E18-1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: B80D982815C6102C

FASTA51153,243
        10         20         30         40         50         60 
MTIILHPGSV LLRDLATIYW TGVPARLDPS FDAGIVKAAD RIAEIAAGNA PVYGINTGFG 

        70         80         90        100        110        120 
KLASIKIDSA DVAALQRNLV LSHCCGVGEA LPENVVRLMM ALKLVSLGRG ASGVRLELVR 

       130        140        150        160        170        180 
LIEAMLARGV IPVIPEKGSV GASGDLAPLA HMAAVMMGHG EAFFGGERLN GATALLKAGL 

       190        200        210        220        230        240 
QPVELAAKEG LALINGTQTS TALALAGLFR AHRAAQSALI TGAMSTDAAM GSSAPFHPEI 

       250        260        270        280        290        300 
HTLRGHRGQI DTAEALRALL ENSPIRQSHI EGDERVQDPY CIRCQPQVDG ACLDLLRSVA 

       310        320        330        340        350        360 
RTLEIEANAV TDNPLVLSDN SVVAGGNFHA EPVAFAADQI VLAICEIGAI AQRRIALLVD 

       370        380        390        400        410        420 
PALSYGLPAF LAKKPGLNSG LMIAEVTSAA LMSENKQMSH PASVDSTPTS ANQEDHVSMA 

       430        440        450        460        470        480 
CHGARRLLPM TENLFAIIGI EALCAAQGVE LRAPLATSPE LTKAIAAIRN VVPSLEEDRY 

       490        500        510 
MANDLKAATV LIASGSLNES VSSGILPALE V 

« Hide

References

[1]"Complete sequence of chromosome of Mesorhizobium sp. BNC1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000390 Genomic DNA. Translation: ABG64357.1.
RefSeqYP_675522.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4181421.
GenomeReviewsGene locus Meso_2985 in contig CP000390_GR.
KEGGmes:Meso_2985.
NMPDRfig|266779.1.peg.1513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ11E18.
OMAQ11E18. AHMAAVM.

Enzyme and pathway databases

BioCycMSP266779:MESO_2985-MON.

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_MESSB
AccessionPrimary (citable) accession number: Q11E18
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: June 16, 2009
This is version 24 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