DB code: D00279

CATH domain 3.90.1150.10 : Aspartate Aminotransferase, domain 1
3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
E.C. 5.4.3.8
CSA 2gsa
M-CSA 2gsa
MACiE M0195

CATH domain Related DB codes (homologues)
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P24630 Glutamate-1-semialdehyde 2,1-aminomutase
GSA
EC 5.4.3.8
Glutamate-1-semialdehyde aminotransferase
GSA-AT
YP_171591.2 (Protein)
NC_006576.1 (DNA/RNA sequence)
PF00202 (Aminotran_3)
[Graphical View]

KEGG enzyme name
glutamate-1-semialdehyde 2,1-aminomutase
glutamate-1-semialdehyde aminotransferase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P24630 GSA_SYNP6 (S)-4-amino-5-oxopentanoate = 5- aminolevulinate. Homodimer. Cytoplasm (Potential). Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00860 Porphyrin and chlorophyll metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00647 C03741 C00430 C00018 I00003
E.C. (initial stage:PMP-GSA)
(PMP-GSA)
(PLP-GSA)
(PLP-DAV)
(PMP-DAV)
(final stage:PMP-DAV)
Compound Pyridoxamine 5'-phosphate (S)-4-Amino-5-oxopentanoate 5-Aminolevulinate Ketimine intermediate-1 Quinonoid intermediate-1 External aldimine intermediate-1 Internal aldimine intermediate (PLP) 4,5-diaminovalerate (DAV) External aldimine intermediate-2 Quinonoid intermediate-2 Ketimine intermediate-2
Type amine group,aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,carbohydrate amino acids,carbohydrate
ChEBI 18335
57501
15757
356416
17549
PubChem 1053
25244684
129297
7048523
137
2gsaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2gsaB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3gsaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3gsaB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3gsbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3gsbB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
4gsaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
4gsaB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
2gsaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PMP Unbound Unbound Unbound Unbound
2gsaB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PLP Unbound Unbound Intermediate-bound:PLP Unbound
3gsaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PLP Unbound Unbound Intermediate-bound:PLP Intermediate-analogue:GAB
3gsaB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PLP Unbound Unbound Unbound Unbound
3gsbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PMP Analogue:GAB Unbound Unbound Unbound
3gsbB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PMP Unbound Unbound Unbound Unbound
4gsaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PLP Unbound Unbound Intermediate-bound:PLP Unbound
4gsaB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PLP Unbound Unbound Intermediate-bound:PLP Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P24630 & literature [7], [13]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2gsaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2gsaB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3gsaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3gsaB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3gsbA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3gsbB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
4gsaA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
4gsaB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2gsaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
2gsaB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
3gsaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
3gsaB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
3gsbA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
3gsbB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
4gsaA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)
4gsaB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 245;LYS 273 LYS 273(PLP binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Scheme I
[3]
Scheme 2, p.1588
[4]
Scheme 1
[6]
Fig.5
[7]
Fig.1, p.4870-4871
[8]
Scheme 1
[11]
FIG.1

References
[1]
Resource
Comments
Medline ID
PubMed ID 1643048
Journal Biochemistry
Year 1992
Volume 31
Pages 7143-51
Authors Ilag LL, Jahn D
Title Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1445864
Journal Biochemistry
Year 1992
Volume 31
Pages 11249-54
Authors Smith MA, Kannangara CG, Grimm B
Title Glutamate 1-semialdehyde aminotransferase: anomalous enantiomeric reaction and enzyme mechanism.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1730703
Journal J Biol Chem
Year 1992
Volume 267
Pages 1584-8
Authors Pugh CE, Harwood JL, John RA
Title Mechanism of glutamate semialdehyde aminotransferase. Roles of diamino- and dioxo-intermediates in the synthesis of aminolevulinate.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 8352736
Journal Biochem J
Year 1993
Volume 293
Pages 697-701
Authors Tyacke RJ, Harwood JL, John RA
Title Properties of the pyridoxaldimine form of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1-aminomutase) and analysis of its role as an intermediate in the formation of aminolaevulinate.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7932714
Journal J Mol Biol
Year 1994
Volume 242
Pages 591-4
Authors Hennig M, Grimm B, Jenny M, Muller R, Jansonius JN
Title Crystallization and preliminary X-ray analysis of wild-type and K272A mutant glutamate 1-semialdehyde aminotransferase from Synechococcus.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8519748
Journal Biochemistry
Year 1995
Volume 34
Pages 15918-24
Authors Brody S, Andersen JS, Kannangara CG, Meldgaard M, Roepstorff P, von Wettstein D
Title Characterization of the different spectral forms of glutamate 1-semialdehyde aminotransferase by mass spectrometry.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 97289685
PubMed ID 9144156
Journal Proc Natl Acad Sci U S A
Year 1997
Volume 94
Pages 4866-71
Authors Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN
Title Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity.
Related PDB 2gsa 3gsa 3gsa 4gsa
Related UniProtKB P24630
[8]
Resource
Comments
Medline ID
PubMed ID 10660540
Journal J Biol Chem
Year 2000
Volume 275
Pages 3879-86
Authors Contestabile R, Angelaccio S, Maytum R, Bossa F, John RA
Title The contribution of a conformationally mobile, active site loop to the reaction catalyzed by glutamate semialdehyde aminomutase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11726494
Journal EMBO J
Year 2001
Volume 20
Pages 6583-90
Authors Moser J, Schubert WD, Beier V, Bringemeier I, Jahn D, Heinz DW
Title V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12459457
Journal FEBS Lett
Year 2002
Volume 532
Pages 27-30
Authors Meskauskiene R, Apel K
Title Interaction of FLU, a negative regulator of tetrapyrrole biosynthesis, with the glutamyl-tRNA reductase requires the tetratricopeptide repeat domain of FLU.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 12878592
Journal J Biol Chem
Year 2003
Volume 278
Pages 40521-6
Authors D'Aguanno S, Gonzales IN, Simmaco M, Contestabile R, John RA
Title Stereochemistry of the reactions of glutamate-1-semialdehyde aminomutase with 4,5-diaminovalerate.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 15498941
Journal Protein Sci
Year 2004
Volume 13
Pages 2992-3005
Authors Paiardini A, Bossa F, Pascarella S
Title Evolutionarily conserved regions and hydrophobic contacts at the superfamily level: The case of the fold-type I, pyridoxal-5'-phosphate-dependent enzymes.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 16564539
Journal J Mol Biol
Year 2006
Volume [Epub ahead of print]
Pages [Epub ahead of print]
Authors Schulze JO, Schubert WD, Moser J, Jahn D, Heinz DW
Title Evolutionary Relationship between Initial Enzymes of Tetrapyrrole Biosynthesis.
Related PDB
Related UniProtKB

Comments
Since the reaction starts and ends with the cofactor in the pyridoxamine phosphate form (PMP), PMP (C00647) is annotated as cofactor in this entry.
This enzyme catalyzes intramolecular transamination, which is similar to other transaminases (E.C. 2.6.1.-), such as aspartate aminotransferase (D00101 in EzCatDB), except that the reaction starts and ends with the cofactor in the PMP form, instead of PLP form.
(A) Schiff-base formation of PMP with carbonyl group of the substrate, (S)-4-Amino-5-oxopentanoate (GSA), leading to a ketimine intermediate:
(B) Isomerization (change in the position of double-bond), leading to external aldimine (PLP-GSA):
(C) Formation of internal aldimine, leading to the elimination of an intermediate, 4,5-diamiovalerate (DAV), from PLP:
(D) Formation of external aldimine (with another amine group of DAV):
(B) Isomerization (change in the position of double-bond), leading to a ketimine intermediate:
(C) Schiff-base deformation, releasing the product, 5-Aminolevulinate, and PMP:

Created Updated
2004-04-05 2009-02-26