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Information on EC 2.3.1.37 - 5-aminolevulinate synthase and Organism(s) Rhodobacter capsulatus and UniProt Accession P18079

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EC Tree
     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.37 5-aminolevulinate synthase
IUBMB Comments
A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues.
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This record set is specific for:
Rhodobacter capsulatus
UNIPROT: P18079
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Word Map
The taxonomic range for the selected organisms is: Rhodobacter capsulatus
The enzyme appears in selected viruses and cellular organisms
Synonyms
alas2, ala synthase, 5-aminolevulinate synthase, ala-s, delta-aminolevulinate synthase, delta-aminolevulinic acid synthase, delta-aminolevulinic acid synthetase, 5-aminolevulinic acid synthase, aminolevulinate synthase, delta-aminolevulinate synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-aminolevulinate synthetase
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5-aminolevulinic acid synthase
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5-aminolevulinic acid synthetase
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ALA synthase
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ALA synthetase
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alpha-aminolevulinic acid synthase
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aminolevulinate synthase
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aminolevulinate synthetase
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aminolevulinic acid synthase
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aminolevulinic acid synthetase
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aminolevulinic synthetase
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delta-aminolevulinate synthase
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delta-aminolevulinate synthetase
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delta-aminolevulinic acid synthase
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delta-aminolevulinic acid synthetase
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delta-aminolevulinic synthetase
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synthase, aminolevulinate
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synthetase, aminolevulinate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
succinyl-CoA:glycine C-succinyltransferase (decarboxylating)
A pyridoxal-phosphate protein. The enzyme in erythrocytes is genetically distinct from that in other tissues.
CAS REGISTRY NUMBER
COMMENTARY hide
9037-14-3
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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
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
show the reaction diagram
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?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
show the reaction diagram
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?
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
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
show the reaction diagram
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-
?
succinyl-CoA + glycine
5-aminolevulinate + CoA + CO2
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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coexpression of the enzyme improves the heterologous production of cytochrome P450, CYP119, from Sulfolobus acidocaldarius in Escherichia coli
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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amino acid sequence alignment
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 43600, calculated from amino acid sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion, crystal structure of full-length homodimeric enzyme binding its cofactor pyridoxal 5'-phosphate at 2.1 A, and structures of the enzyme in complex with the substrates glycine or succinyl-coenzyme A at 2.7 A and 2.8 A, respectivel
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expressed in Escherichia coli Rosetta 2 (DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ferreira, G.C.; Gong, J.
5-Aminolevulinate synthase and the first step of heme biosynthesis
J. Bioenerg. Biomembr.
27
151-159
1995
Agrobacterium tumefaciens, Aspergillus nidulans, Bradyrhizobium japonicum, Saccharomyces cerevisiae, Gallus gallus, Euglena gracilis, Homo sapiens, Paracoccus denitrificans, Mus musculus, Rattus norvegicus, Sinorhizobium meliloti, Rhodobacter capsulatus, Cereibacter sphaeroides
Manually annotated by BRENDA team
Astner, I.; Schulze, J.O.; van den Heuvel, J.; Jahn, D.; Schubert, W.D.; Heinz, D.W.
Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans
EMBO J.
24
3166-3177
2005
Rhodobacter capsulatus (P18079), Rhodobacter capsulatus
Manually annotated by BRENDA team
Honda, Y.; Nanasawa, K.; Fujii, H.
Coexpression of 5-aminolevulinic acid synthase gene facilitates heterologous production of thermostable cytochrome P450, CYP119, in holo form in Escherichia coli
ChemBioChem
19
2156-2159
2018
Rhodobacter capsulatus
Manually annotated by BRENDA team
Na, I.; DeForte, S.; Stojanovski, B.M.; Ferreira, G.C.; Uversky, V.N.
Molecular dynamics analysis of the structural and dynamic properties of the functionally enhanced hepta-variant of mouse 5-aminolevulinate synthase
J. Biomol. Struct. Dyn.
36
152-165
2018
Mus musculus (P08680), Mus musculus, Rhodobacter capsulatus (P18079), Rhodobacter capsulatus, Rhodobacter capsulatus ATCC BAA-309 (P18079)
Manually annotated by BRENDA team