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P21310 (HUTH_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histidine ammonia-lyase

Short name=Histidase
EC=4.3.1.3
Gene names
Name:hutH
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-histidine = urocanate + NH3. Ref.2 Ref.3 Ref.4 Ref.5

Pathway

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

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00229.

Induction

By histidine and urocanate. HAMAP-Rule 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. HAMAP-Rule MF_00229

Sequence similarities

Belongs to the PAL/histidase family.

Ontologies

Keywords
   Biological processHistidine metabolism
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processbiosynthetic process

Inferred from electronic annotation. Source: InterPro

histidine catabolic process to glutamate and formamide

Inferred from electronic annotation. Source: UniProtKB-UniPathway

histidine catabolic process to glutamate and formate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistidine ammonia-lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 510509Histidine ammonia-lyase HAMAP-Rule MF_00229
PRO_0000161017

Amino acid modifications

Modified residue14412,3-didehydroalanine (Ser) HAMAP-Rule MF_00229
Cross-link143 ↔ 1455-imidazolinone (Ala-Gly) HAMAP-Rule MF_00229

Experimental info

Mutagenesis1131S → A: No loss of activity.
Mutagenesis1441S → A or T: Complete loss of activity. Ref.3 Ref.4 Ref.5
Mutagenesis1441S → C: No effect. Ref.3 Ref.4 Ref.5
Mutagenesis3941S → A: No loss of activity.
Mutagenesis4191S → A: No loss of activity.
Sequence conflict1521H → T in AAA25840. Ref.1
Sequence conflict4391L → P in AAA25840. Ref.1

Secondary structure

................................................................................... 510
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21310 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7D80C7E64B0C4F57

FASTA51053,761
        10         20         30         40         50         60 
MTELTLKPGT LTLAQLRAIH AAPVRLQLDA SAAPAIDASV ACVEQIIAED RTAYGINTGF 

        70         80         90        100        110        120 
GLLASTRIAS HDLENLQRSL VLSHAAGIGA PLDDDLVRLI MVLKINSLSR GFSGIRRKVI 

       130        140        150        160        170        180 
DALIALVNAE VYPHIPLKGS VGASGDLAPL AHMSLVLLGE GKARYKGQWL SATEALAVAG 

       190        200        210        220        230        240 
LEPLTLAAKE GLALLNGTQA STAYALRGLF YAEDLYAAAI ACGGLSVEAV LGSRSPFDAR 

       250        260        270        280        290        300 
IHEARGQRGQ IDTAACFRDL LGDSSEVSLS HKNCDKVQDP YSLRCQPQVM GACLTQLRQA 

       310        320        330        340        350        360 
AEVLGIEANA VSDNPLVFAA EGDVISGGNF HAEPVAMAAD NLALAIAEIG SLSERRISLM 

       370        380        390        400        410        420 
MDKHMSQLPP FLVENGGVNS GFMIAQVTAA ALASENKALS HPHSVDSLPT SANQEDHVSM 

       430        440        450        460        470        480 
APAAGKRLWE MAENTRGVLA IEWLGACQGL DLRKGLKTSA KLEKARQALR SEVAHYDRDR 

       490        500        510 
FFAPDIEKAV ELLAKGSLTG LLPAGVLPSL 

« Hide

References

[1]"Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida."
Consevage M.W., Phillips A.T.
J. Bacteriol. 172:2224-2229(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13.
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
[2]"Identification of Ser143 as the site of modification in the active site of histidine ammonia-lyase."
Hernandez D., Stroh J.G., Phillips A.T.
Arch. Biochem. Biophys. 307:126-132(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, MASS SPECTROMETRY.
[3]"Ser-143 is an essential active site residue in histidine ammonia-lyase of Pseudomonas putida."
Hernandez D., Phillips A.T.
Biochem. Biophys. Res. Commun. 201:1433-1438(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INHIBITION BY CHEMICAL MODIFICATION, MUTAGENESIS OF SER-144.
[4]"Identification of serine-143 as the most likely precursor of dehydroalanine in the active site of histidine ammonia-lyase. A study of the overexpressed enzyme by site-directed mutagenesis."
Langer M., Reck G., Reed J., Retey J.
Biochemistry 33:6462-6467(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, DEHYDROALANINE FORMATION, MUTAGENESIS OF SER-144.
[5]"Histidine ammonia-lyase mutant S143C is posttranslationally converted into fully active wild-type enzyme. Evidence for serine 143 to be the precursor of active site dehydroalanine."
Langer M., Lieber A., Retey J.
Biochemistry 33:14034-14038(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, ENZYME MECHANISM, MUTAGENESIS OF SER-144.
[6]"Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile."
Schwede T.F., Retey J., Schulz G.E.
Biochemistry 38:5355-5361(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SEQUENCE REVISION TO 152 AND 439.
Strain: ATCC 12633 / DSM 291 / JCM 13063 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M35140 Genomic DNA. Translation: AAA25840.1.
PIRA35251.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B8FX-ray2.10A2-510[»]
1EB4X-ray2.00A2-510[»]
1GK2X-ray1.90A/B/C/D2-510[»]
1GK3X-ray2.25A2-510[»]
1GKJX-ray1.70A2-510[»]
1GKMX-ray1.00A2-510[»]
ProteinModelPortalP21310.
SMRP21310. Positions 2-510.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11608.
UniPathwayUPA00379; UER00549.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00229. His_ammonia_lyase.
InterProIPR001106. Aromatic_Lyase.
IPR024083. Fumarase/histidase_N.
IPR005921. HutH.
IPR008948. L-Aspartase-like.
IPR022313. Phe/His_NH3-lyase_AS.
[Graphical view]
PfamPF00221. Lyase_aromatic. 1 hit.
[Graphical view]
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR01225. hutH. 1 hit.
PROSITEPS00488. PAL_HISTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21310.

Entry information

Entry nameHUTH_PSEPU
AccessionPrimary (citable) accession number: P21310
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways