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Information on EC 4.1.1.22 - histidine decarboxylase and Organism(s) Pseudomonas fluorescens and UniProt Accession P95477

for references in articles please use BRENDA:EC4.1.1.22
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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.22 histidine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
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This record set is specific for:
Pseudomonas fluorescens
UNIPROT: P95477
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Word Map
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The taxonomic range for the selected organisms is: Pseudomonas fluorescens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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L-histidine
=
histamine
+
CO2
=
+
Synonyms
hdc, histidine decarboxylase, l-histidine decarboxylase, histamine-forming enzyme, hisdcase, pyruvoyl-dependent histidine decarboxylase, pyruvoyl-dependent decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Decarboxylase, histidine
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HDC
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-
-
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HisDCase
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-
-
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L-Histidine decarboxylase
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-
-
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TOM92
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
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SYSTEMATIC NAME
IUBMB Comments
L-histidine carboxy-lyase (histamine-forming)
A pyridoxal-phosphate protein (in animal tissues). The bacterial enzyme has a pyruvoyl residue as prosthetic group.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-61-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-histidine
histamine + CO2
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-histidine
histamine + CO2
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, binding structure involving a Schiff base, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DCHS_PSEFL
405
0
45727
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
structure-function relationship, molecular modeling, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence analysis and comparison, intron-exon relationships, phylogenetic analysis, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Okigami, H.; Ueno, H.
Bioinformatic study on histidine decarboxylase
J. Biol. Macromol.
6
11-27
2006
Morganella morganii (P05034), Rattus norvegicus (P16453), Homo sapiens (P19113), Klebsiella aerogenes (P28577), Raoultella planticola (P28578), Solanum lycopersicum (P54772), Pseudomonas fluorescens (P95477), Drosophila melanogaster (Q05733), Vibrio anguillarum (Q56581), Vibrio anguillarum (Q79JY8), Gloeobacter violaceus (Q7NIG4), Mus musculus (Q7TMW5), Photobacterium phosphoreum (Q846V2), Aplysia californica (Q86BW8), Clostridium tetani (Q894Q7), Oryza sativa (Q8RV06), Mesorhizobium loti (Q98A07), Arabidopsis thaliana (Q9MA74)
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Manually annotated by BRENDA team