DB code: D00103

CATH domain 3.90.1150.10 : Aspartate Aminotransferase, domain 1
3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
E.C. 2.6.1.13
CSA 2oat
M-CSA 2oat
MACiE

CATH domain Related DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00102 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Contains RefSeq Pfam
P04181 Ornithine aminotransferase, mitochondrial
EC 2.6.1.13
Ornithine--oxo-acid aminotransferase
Ornithine aminotransferase, hepatic form
Ornithine aminotransferase, renal form
NP_000265.1 (Protein)
NM_000274.3 (DNA/RNA sequence)
NP_001165285.1 (Protein)
NM_001171814.1 (DNA/RNA sequence)
PF00202 (Aminotran_3)
[Graphical View]

KEGG enzyme name
ornithine aminotransferase
ornithine delta-transaminase
L-ornithine:alpha-ketoglutarate delta-aminotransferase
OAT
L-ornithine 5-aminotransferase
L-ornithine aminotransferase
ornithine 5-aminotransferase
ornithine transaminase
ornithine-alpha-ketoglutarate aminotransferase
ornithine-2-oxoacid aminotransferase
ornithine-keto acid aminotransferase
ornithine-keto acid transaminase
ornithine-ketoglutarate aminotransferase
ornithine-oxo acid aminotransferase
ornithine:alpha-oxoglutarate transaminase
ornithine---oxo-acid transaminase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P04181 OAT_HUMAN L-ornithine + a 2-oxo acid = L-glutamate 5- semialdehyde + an L-amino acid. Homotetramer. Mitochondrion matrix. Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00330 Arginine and proline metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C00077 C00161 C01165 C00151
E.C.
Compound Pyridoxal phosphate L-Ornithine 2-Oxo acid L-Glutamate 5-semialdehyde L-Amino acid
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,amine group,lipid carbohydrate,carboxyl group amino acids,carbohydrate amino acids
ChEBI 18405
15729
17232
58066
PubChem 1051
6262
88747248
193305
49791979
1gbnA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gbnB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gbnC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1oatA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1oatB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1oatC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2canA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2canB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2canC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2oatA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2oatB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2oatC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1gbnA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:GBC-PLP
1gbnB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:GBC-PLP
1gbnC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:GBC-PLP
1oatA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Unbound
1oatB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Unbound
1oatC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Unbound
2canA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:CAN-PLP
2canB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:CAN-PLP
2canC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:CAN-PLP
2oatA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PFM Unbound Unbound Unbound Unbound Intermediate-analogue:PFM
2oatB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PFM Unbound Unbound Unbound Unbound Intermediate-analogue:PFM
2oatC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Analogue:PFM Unbound Unbound Unbound Unbound Intermediate-analogue:PFM

Reference for Active-site residues
resource references E.C.
Swiss-prot

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1gbnA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gbnB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gbnC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1oatA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1oatB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1oatC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2canA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2canB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2canC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2oatA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2oatB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2oatC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1gbnA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
1gbnB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
1gbnC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
1oatA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
1oatB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
1oatC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
2canA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
2canB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
2canC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
2oatA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
2oatB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)
2oatC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 292 LYS 292(PLP binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.91-92
[5]
p.304-306

References
[1]
Resource
Comments
Medline ID
PubMed ID 3803391
Journal Eur J Biochem
Year 1987
Volume 162
Pages 345-50
Authors Markovic-Housley Z, Kania M, Lustig A, Vincent MG, Jansonius JN, John RA
Title Quaternary structure of ornithine aminotransferase in solution and preliminary crystallographic data.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 7932736
Journal J Mol Biol
Year 1994
Volume 243
Pages 128-30
Authors Shen BW, Ramesh V, Mueller R, Hohenester E, Hennig M, Jansonius JN
Title Crystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID 97454792
PubMed ID 9309222
Journal Structure
Year 1997
Volume 5
Pages 1067-75
Authors Shah SA, Shen BW, Brunger AT
Title Human ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition.
Related PDB 2can 1gbn
Related UniProtKB P04181
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID 9818101
PubMed ID 9514741
Journal J Mol Biol
Year 1998
Volume 277
Pages 81-102
Authors Shen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T
Title Crystal structure of human recombinant ornithine aminotransferase.
Related PDB 1oat
Related UniProtKB P04181
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS)
Medline ID 99096924
PubMed ID 9878407
Journal J Mol Biol
Year 1999
Volume 285
Pages 297-309
Authors Storici P, Capitani G, Muller R, Schirmer T, Jansonius JN
Title Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine.
Related PDB 2oat
Related UniProtKB P04181

Comments
This enzyme catalyzes the following reactions:
(A) Formation of external aldimine (with amine group of the first substrate).
(B) Isomerization (change in the position of double-bond)
(C) Schiff-base deforming (by hydration), releasing the first product, and PMP.
(D) Schiff-base forming (of PMP with carbonyl group of the second substrate).
(E) Isomerization (change in the position of double-bond)
(F) Formation of internal aldimine, releasing the second product.

Created Updated
2004-03-17 2009-02-26