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34  structures 62  species 0  interactions 71  sequences 1  architecture

Family: HDC (PF02329)

Summary: Histidine carboxylase PI chain

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This is the Wikipedia entry entitled "Histidine decarboxylase". More...

Histidine decarboxylase Edit Wikipedia article

Histidine decarboxylase
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols HDC ; MGC163399
External IDs OMIM142704 MGI96062 HomoloGene20490 GeneCards: HDC Gene
EC number 4.1.1.22
Orthologs
Species Human Mouse
Entrez 3067 15186
Ensembl ENSG00000140287 ENSMUSG00000027360
UniProt P19113 P23738
RefSeq (mRNA) NM_002112 NM_008230
RefSeq (protein) NP_002103 NP_032256
Location (UCSC) Chr 15:
50.53 – 50.56 Mb
Chr 2:
126.59 – 126.62 Mb
PubMed search [1] [2]
histidine decarboxylase
Identifiers
EC number 4.1.1.22
CAS number 9024-61-7
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
Histidine carboxylase PI chain
PDB 1ibt EBI.jpg
structure of the d53,54n mutant of histidine decarboxylase at-170 c
Identifiers
Symbol HDC
Pfam PF02329
InterPro IPR003427
SCOP 1pya
SUPERFAMILY 1pya

Histidine decarboxylase (HDC) is the enzyme that catalyzes the reaction that produces histamine from histidine with the help of vitamin B6 as follows:[1][2][3]

Conversion of histidine to histamine by histidine decarboxylase

In humans, the histidine decarboxylase enzyme is encoded by the HDC gene.[4][5]

Function

The biogenic amine histamine is an important modulator of numerous physiologic processes, including neurotransmission, gastric acid secretion, and smooth muscle tone. The biosynthesis of histamine from histidine is catalyzed by the enzyme L-histidine decarboxylase. This homodimeric enzyme is a pyridoxal phosphate (PLP)-dependent decarboxylase and is highly specific for its histidine substrate.[4]

Biosynthesis

In bacteria, it is synthesised as a proenzyme, PI. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer, (alpha beta)6, by nonhydrolytic self-catalysis.[6]

Clinical significance

Known inhibitors of histidine decarboxylase : catechin, tritoqualine an atypical antihistaminic (Hypostamin©).

Mutations in the gene for this enzyme have been observed in one family with Tourette syndrome (TS) and are not thought to account for most cases of TS.[7]

See also

References

  1. ^ Epps HM (1945). "Studies on bacterial amino-acid decarboxylases: 4. l(-)-histidine decarboxylase from Cl. welchii Type A". Biochem. J. 39 (1): 42–6. PMC 1258146. PMID 16747851. 
  2. ^ Riley WD, Snell EE (October 1968). "Histidine decarboxylase of Lactobacillus 30a. IV. The presence of covalently bound pyruvate as the prosthetic group". Biochemistry 7 (10): 3520–8. doi:10.1021/bi00850a029. PMID 5681461. 
  3. ^ Rosenthaler J, Guirard BM, Chang GW, Snell EE (July 1965). "Purification and properties of histidine decarboxylase from Lactobacillus 30a". Proc. Natl. Acad. Sci. U.S.A. 54 (1): 152–8. doi:10.1073/pnas.54.1.152. PMC 285813. PMID 5216347. 
  4. ^ a b "Entrez Gene: histidine decarboxylase". 
  5. ^ Bruneau G, Nguyen VC, Gros F, Bernheim A, Thibault J (November 1992). "Preparation of a rat brain histidine decarboxylase (HDC) cDNA probe by PCR and assignment of the human HDC gene to chromosome 15". Hum. Genet. 90 (3): 235–8. doi:10.1007/bf00220068. PMID 1487235. 
  6. ^ Coton E, Rollan GC, Lonvaud-Funel A (1998). "Histidine carboxylase of Leuconostoc oenos 9204: purification, kinetic properties, cloning and nucleotide sequence of the hdc gene.". J Appl Microbiol 84 (2): 143–51. doi:10.1046/j.1365-2672.1998.00271.x. PMID 9633629. 
  7. ^ "Online Mendelian Inheritance in Man: histidine decarboxylase". 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Histidine carboxylase PI chain Provide feedback

Histidine carboxylase catalyses the formation of histamine from histidine. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta)6.

Literature references

  1. Coton E, Rollan GC, Lonvaud-Funel A; , J Appl Microbiol 1998;84:143-151.: Histidine carboxylase of Leuconostoc oenos 9204: purification, kinetic properties, cloning and nucleotide sequence of the hdc gene. PUBMED:9633629 EPMC:9633629


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003427

Histidine decarboxylase (EC) catalyses the formation of histamine from histidine [PUBMED:11243783]. It requires a pyruvoyl group for its activity. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta) 6 by nonhydrolytic self-catalysis.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

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Alignments

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(4)
Full
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Representative proteomes NCBI
(58)
Meta
(3)
RP15
(4)
RP35
(7)
RP55
(8)
RP75
(9)
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(4)
Full
(71)
Representative proteomes NCBI
(58)
Meta
(3)
RP15
(4)
RP35
(7)
RP55
(8)
RP75
(9)
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External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_19599 (release 5.2)
Previous IDs: none
Type: Domain
Author: Mian N, Bateman A
Number in seed: 4
Number in full: 71
Average length of the domain: 262.60 aa
Average identity of full alignment: 46 %
Average coverage of the sequence by the domain: 94.92 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 28.3 28.0
Noise cut-off 15.8 15.1
Model length: 306
Family (HMM) version: 11
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Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HDC domain has been found. There are 34 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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