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Q2IIV4 (HUTH_ANADE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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:
Histidine ammonia-lyase

Short name=Histidase
EC=4.3.1.3
Gene names
Name:hutH
Ordered Locus Names:Adeh_1814
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
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 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

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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhistidine ammonia-lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Histidine ammonia-lyase HAMAP MF_00229
PRO_0000336582

Amino acid modifications

Modified residue14412,3-didehydroalanine (Ser) By similarity
Cross-link143 ↔ 1455-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IIV4 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 52FF0095D52F0AD5

FASTA50853,101
        10         20         30         40         50         60 
METLLLDGET LTLEQVRAVA TGAARAALAP AARERVRRSR ALVDARLEDG EAHYGINTGF 

        70         80         90        100        110        120 
GTLAEVRIPR ADLERLQRNL VLSHAAGVGA PLPLAEARAL VLLRANVLAK GVSGIRERTL 

       130        140        150        160        170        180 
ELLLAMLERG VVPVVPERGS VGASGDLAPL AHLALVLIGD GEAFLAPPGA AAPPERLPGG 

       190        200        210        220        230        240 
EALRRAGLEP VVLQPKEGLA LVNGTQAMAA VGTLALLRAE RLAALADLAG AMTLEGLLGS 

       250        260        270        280        290        300 
HRPFAPEIQA ARGQPGQIEA AAHLRALLAG SELNASHQGP GCHKVQDPYS LRCMPQVHGA 

       310        320        330        340        350        360 
ARDGIGFCRG VLAREVNAAT DNPLVFPDTG EIVSGGNFHG QPVALALDVL AVAASHLAAI 

       370        380        390        400        410        420 
SERRVEQLVN PSLSGLPPFL APQHGLNSGF MIAQVTSAAL VSENKVLCHP ASVDSIPSSA 

       430        440        450        460        470        480 
GREDHVSMGM TAALKARQVV ENVRTCLAIE LLVAAQALDL RAPLRPAQRV ADAHARLRER 

       490        500 
VPHLSEDRAL YRDIEAVSRL VDEGALEL 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-C.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC81586.1.
RefSeqYP_465023.1. NC_007760.1.

3D structure databases

ProteinModelPortalQ2IIV4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IIV4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3887396.
GenomeReviewsGene locus Adeh_1814 in contig CP000251_GR.
KEGGade:Adeh_1814.
PATRIC20919793. VBIAnaDeh31384_1878.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2986.
HOGENOMHBG510887.
OMAQKGQIDS.
PhylomeDBQ2IIV4.
ProtClustDBPRK09367.

Enzyme and pathway databases

BioCycADEH290397:ADEH_1814-MONOMER.

Family and domain databases

HAMAPMF_00229. His_ammonia-lyase.
[Tree]
InterProIPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
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.
KOK01745.
PfamPF00221. PAL. 1 hit.
[Graphical view]
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR01225. HutH. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHUTH_ANADE
AccessionPrimary (citable) accession number: Q2IIV4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 46 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