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Q9HLI6 (HUTH_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 69. 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:
Probable histidine ammonia-lyase
Short name=Histidase
EC=4.3.1.3
Gene names
Name:hutH
Ordered Locus Names:Ta0242
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma

Protein attributes

Sequence length496 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
Reference 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 – 496496Probable histidine ammonia-lyase HAMAP MF_00229
PRO_0000161056

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q9HLI6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: D5F0BF275477CA23

FASTA49654,149
        10         20         30         40         50         60 
MIEIDGRSLR VEDVYAVAVE YDRVSISDDT LKAVEEKHEA FLKLINSGKT VYGVNTGFGS 

        70         80         90        100        110        120 
LLNVHIERDQ EIELQKNLIR SHSSGVGDYL ENRYVRAIMA VRLNSLAAGY SAVSADLLNM 

       130        140        150        160        170        180 
MVEMLNRDVI PAVPKYGSVG ASGDLAPLAH IGLAMMGEGK AFFEGRLMDS ARALEKAGLK 

       190        200        210        220        230        240 
PYQFKEKEGV ALINGTSFMS GILSIAVMDA HDILENAIRS ALLSFEALGG TSKAFTPWIL 

       250        260        270        280        290        300 
GARPHLGQVA IGNRFREYLT GSDIVKRADS VKVQDAYTLR CIPQVYGSVA DVIDYVENVL 

       310        320        330        340        350        360 
SVEINSATDN PLFNGEEVVS GGNFHGEPVA LAADFLAIAL TDLGNMVERR IARLVDTNLS 

       370        380        390        400        410        420 
GLPPFLTPDS GLNSGYMIPQ YTAAALCNRN KVLAYPSSAD TIPTSANQED HVSMGATGSL 

       430        440        450        460        470        480 
KLLEIIDNVR YIIAIEYLLG SQALEFTDKG MSPSTRKIYE KIREKVEKLD HDRPPSFDIE 

       490 
TIRKMMDKKE FISALP

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed: 11029001] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL445063 Genomic DNA. Translation: CAC11387.1.
RefSeqNP_393722.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HLI6.
ModBaseSearch...

Proteomic databases

PRIDEQ9HLI6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1455875.
GenomeReviewsGene locus Ta0242 in contig AL139299_GR.
KEGGtac:Ta0242.
NMPDRfig|273075.1.peg.244.

Phylogenomic databases

HOGENOMHBG510887.
OMANAPVYGI.
PhylomeDBQ9HLI6.
ProtClustDBPRK09367.

Enzyme and pathway databases

BioCycTACI273075:TA0242-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_THEAC
AccessionPrimary (citable) accession number: Q9HLI6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 1, 2001
Last modified: December 14, 2011
This is version 69 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

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