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 18405 |
15729 15729 |
17232 58066 17232 58066 |
||||||||
| PubChem |
1051 1051 |
6262 88747248 6262 88747248 |
193305 49791979 193305 49791979 |
||||||||
| 1gbnA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gbnB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gbnC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1oatA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1oatB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1oatC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2canA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2canB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2canC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2oatA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2oatB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2oatC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gbnA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GBC-PLP |
| 1gbnB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GBC-PLP |
| 1gbnC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:GBC-PLP |
| 1oatA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1oatB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1oatC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound |
| 2canA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CAN-PLP |
| 2canB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CAN-PLP |
| 2canC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CAN-PLP |
| 2oatA02 |
|
|
|
|
|
Analogue:PFM | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PFM |
| 2oatB02 |
|
|
|
|
|
Analogue:PFM | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PFM |
| 2oatC02 |
|
|
|
|
|
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 |
|
|
|
|
|
|||||
| 1gbnB01 |
|
|
|
|
|
|||||
| 1gbnC01 |
|
|
|
|
|
|||||
| 1oatA01 |
|
|
|
|
|
|||||
| 1oatB01 |
|
|
|
|
|
|||||
| 1oatC01 |
|
|
|
|
|
|||||
| 2canA01 |
|
|
|
|
|
|||||
| 2canB01 |
|
|
|
|
|
|||||
| 2canC01 |
|
|
|
|
|
|||||
| 2oatA01 |
|
|
|
|
|
|||||
| 2oatB01 |
|
|
|
|
|
|||||
| 2oatC01 |
|
|
|
|
|
|||||
| 1gbnA02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 1gbnB02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 1gbnC02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 1oatA02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 1oatB02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 1oatC02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 2canA02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 2canB02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 2canC02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 2oatA02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 2oatB02 |
|
|
|
|
|
LYS 292 | LYS 292(PLP binding) | |||
| 2oatC02 |
|
|
|
|
|
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), (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, |
| Created | Updated |
|---|---|
| 2004-03-17 | 2009-02-26 |