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Reviewed, UniProtKB/Swiss-Prot Q0AP92 (HUTH_MARMM)

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: Mmar10_1603
OrganismMaricaulis maris (strain MCS10) [Complete proteome] [HAMAP]
Taxonomic identifier394221 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeMaricaulis

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_0000336585

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
Q0AP92-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: BB3F77F890CA662E

FASTA50752,202
        10         20         30         40         50         60 
MTTVTIKPGA MVLADWADIW RGATIRIDPE AKAGVDAAAA TVDRLIASGE AVYGLNTGFG 

        70         80         90        100        110        120 
KLAQTRIADD ELATLQERLV LSHAAGIGEA LDSRIVRLVM ALKLASLGRG ASGVRWTTIA 

       130        140        150        160        170        180 
AMQALLDADV LPVIPSQGSV GASGDLAPLA HMSAALIGAG EATWQGQRMP ASDALAKAGL 

       190        200        210        220        230        240 
KPVQLGPKEG LALLNGTQTS TALALAGLFE VEAGFQAALV SGALSVDAAK GSVAPFDPRI 

       250        260        270        280        290        300 
HSLRGHPGQI DVAAALRGLL DGSGILSSHE GCEKIQDPYC LRCQPQVMGA VLDLLRQAGA 

       310        320        330        340        350        360 
VLEREANAVT DNPLIFTDTD EAISGGNFHA EPVAFAADQI AMAACEIGSI CERRIALLTD 

       370        380        390        400        410        420 
PAVSGLPAFL TPNPGINSGF MIAHVTAAAL VSENKQKAYP ASVDSIPTSA NQEDHVSMAT 

       430        440        450        460        470        480 
HGAFRLLKMA ENLHVVVGIE LLCGAQGTDF HAGLTSSPTL ETAKATLRKQ VPAYGDDRYF 

       490        500 
ATDIANARDL VTGRGLVADA GTLPGIA 

« Hide

References

[1]"Complete sequence of Maricaulis maris MCS10."
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., Saunders E., 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., Viollier P., Stephens C., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000449 Genomic DNA. Translation: ABI65895.1.
RefSeqYP_756833.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4283925.
GenomeReviewsGene locus Mmar10_1603 in contig CP000449_GR.
KEGGmmr:Mmar10_1603.
NMPDRfig|394221.5.peg.1566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0AP92.
OMAQ0AP92. 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_MARMM
AccessionPrimary (citable) accession number: Q0AP92
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 17, 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