Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q1Q9E4 (HUTH_PSYCK)

Last modified June 16, 2009. Version 25. 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: Pcryo_1932
OrganismPsychrobacter cryohalolentis (strain K5) [Complete proteome] [HAMAP]
Taxonomic identifier335284 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length520 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 – 520520Histidine ammonia-lyase HAMAP MF_00229
PRO_1000021567

Amino acid modifications

Modified residue14712,3-didehydroalanine (Ser) By similarity
Cross-link146 ↔ 1485-imidazolinone (Ala-Gly) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1Q9E4-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 1FD92E53A3EEF57E

FASTA52055,756
        10         20         30         40         50         60 
MTAIKKLTLQ PRQLSFEILR DIYEQPVILT LPDSAYEAID ASHEDVQTII RRDKSAYGIN 

        70         80         90        100        110        120 
TGFGLLAKTR ISDDQLELLQ RNLIVSHSVG TGEALPANVV RLIMVMKVTS LAQGVSGVRR 

       130        140        150        160        170        180 
AVVDSLLGLI NNQITPNIPA KGSVGASGDL APLSHMTLAM MGEGHVYVDG NKVLAADALA 

       190        200        210        220        230        240 
QHGLEPITLA AKEGLALING TQVSTALALR GYFLARDLLE TATIVGSLSI DAAKGSDAPF 

       250        260        270        280        290        300 
DARIHEVRGH HGQIEIAKAH RQLIKGSAIR ASHDGEQDDR VQDPYCLRCQ PQVMGACLDI 

       310        320        330        340        350        360 
INQAGKTLLI ESNAVTDNPL IFNNEDGPVA ISGGNFHAEP VAFAADILAL AIAEIGSMSE 

       370        380        390        400        410        420 
RRIALLIDAT LSGGLPPFLV DNAGVNSGFM IAHVTAAALA SENKSIAHPG SVDSIPTSAN 

       430        440        450        460        470        480 
QEDHVSMATY CARRLYEMAQ NTATIIGIEL LAAGQGIDFH RGLETSEPLT MAHQKLREQV 

       490        500        510        520 
TFYDKDRYLA PDIEAAKQLV LDGTLAEHWQ PLRSNWYDSK 

« Hide

References

[1]"Complete sequence of chromosome of Psychrobacter cryohalolentis K5."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Sims D.R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000323 Genomic DNA. Translation: ABE75709.1.
RefSeqYP_581193.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4034669.
GenomeReviewsGene locus Pcryo_1932 in contig CP000323_GR.
KEGGpcr:Pcryo_1932.
NMPDRfig|335284.3.peg.2412.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1Q9E4.
OMAQ1Q9E4. FAPDIEA.

Enzyme and pathway databases

BioCycPCRY335284:PCRYO_1932-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_PSYCK
AccessionPrimary (citable) accession number: Q1Q9E4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 25 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