EzCatDB: D00103

DB codeD00103
CATH domainDomain 13.90.1150.10
Domain 23.40.640.10Catalytic domain
E.C.2.6.1.13
CSA2oat

CATH domainRelated DB codes (homologues)
3.40.640.10D00085,D00092,D00101,D00102,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279
3.90.1150.10D00085,D00092,D00101,D00102,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279

Enzyme Name
Swiss-protKEGG

P04181
Protein nameOrnithine aminotransferase, mitochondrialornithine 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
SynonymsEC 2.6.1.13
Ornithine--oxo-acid aminotransferase
ContainsOrnithine aminotransferase, hepatic form
Ornithine aminotransferase, renal form

KEGG pathways
MAP codePathways
MAP00330Arginine and proline metabolism

Swiss-prot:Accession NumberP04181
Entry nameOAT_HUMAN
ActivityL-ornithine + a 2-oxo acid = L-glutamate 5- semialdehyde + an L-amino acid.
SubunitHomotetramer.
Subcellular locationMitochondrion matrix.
CofactorPyridoxal phosphate.


CofactorsSubstratesProductsintermediates
KEGG-idC00018C00077C00161C01165C00151
CompoundPyridoxal phosphateL-Ornithine2-Oxo acidL-Glutamate 5-semialdehydeL-Amino acid
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,amine group,lipidcarbohydrate,carboxyl groupamino acids,carbohydrateamino acids
1gbnA01UnboundUnboundUnboundUnboundUnboundUnbound
1gbnB01UnboundUnboundUnboundUnboundUnboundUnbound
1gbnC01UnboundUnboundUnboundUnboundUnboundUnbound
1oatA01UnboundUnboundUnboundUnboundUnboundUnbound
1oatB01UnboundUnboundUnboundUnboundUnboundUnbound
1oatC01UnboundUnboundUnboundUnboundUnboundUnbound
2canA01UnboundUnboundUnboundUnboundUnboundUnbound
2canB01UnboundUnboundUnboundUnboundUnboundUnbound
2canC01UnboundUnboundUnboundUnboundUnboundUnbound
2oatA01UnboundUnboundUnboundUnboundUnboundUnbound
2oatB01UnboundUnboundUnboundUnboundUnboundUnbound
2oatC01UnboundUnboundUnboundUnboundUnboundUnbound
1gbnA02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:GBC-PLP
1gbnB02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:GBC-PLP
1gbnC02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:GBC-PLP
1oatA02Bound:PLPUnboundUnboundUnboundUnboundUnbound
1oatB02Bound:PLPUnboundUnboundUnboundUnboundUnbound
1oatC02Bound:PLPUnboundUnboundUnboundUnboundUnbound
2canA02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:CAN-PLP
2canB02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:CAN-PLP
2canC02Bound:PLPUnboundUnboundUnboundUnboundIntermediate-analogue:CAN-PLP
2oatA02Analogue:PFMUnboundUnboundUnboundUnboundIntermediate-analogue:PFM
2oatB02Analogue:PFMUnboundUnboundUnboundUnboundIntermediate-analogue:PFM
2oatC02Analogue:PFMUnboundUnboundUnboundUnboundIntermediate-analogue:PFM

Active-site residues
resource
Swiss-prot
pdbCatalytic residuesModified residues
1gbnA01

1gbnB01

1gbnC01

1oatA01

1oatB01

1oatC01

2canA01

2canB01

2canC01

2oatA01

2oatB01

2oatC01

1gbnA02LYS 292
LYS 292(PLP binding)
1gbnB02LYS 292
LYS 292(PLP binding)
1gbnC02LYS 292
LYS 292(PLP binding)
1oatA02LYS 292
LYS 292(PLP binding)
1oatB02LYS 292
LYS 292(PLP binding)
1oatC02LYS 292
LYS 292(PLP binding)
2canA02LYS 292
LYS 292(PLP binding)
2canB02LYS 292
LYS 292(PLP binding)
2canC02LYS 292
LYS 292(PLP binding)
2oatA02LYS 292
LYS 292(PLP binding)
2oatB02LYS 292
LYS 292(PLP binding)
2oatC02LYS 292
LYS 292(PLP binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.91-92
[5]p.304-306

references
[1]
PubMed ID3803391
JournalEur J Biochem
Year1987
Volume162
Pages345-50
AuthorsMarkovic-Housley Z, Kania M, Lustig A, Vincent MG, Jansonius JN, John RA
TitleQuaternary structure of ornithine aminotransferase in solution and preliminary crystallographic data.
[2]
PubMed ID7932736
JournalJ Mol Biol
Year1994
Volume243
Pages128-30
AuthorsShen BW, Ramesh V, Mueller R, Hohenester E, Hennig M, Jansonius JN
TitleCrystallization and preliminary X-ray diffraction studies of recombinant human ornithine aminotransferase.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS)
Medline ID97454792
PubMed ID9309222
JournalStructure
Year1997
Volume5
Pages1067-75
AuthorsShah SA, Shen BW, Brunger AT
TitleHuman ornithine aminotransferase complexed with L-canaline and gabaculine: structural basis for substrate recognition.
Related PDB2can,1gbn
Related Swiss-protP04181
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID9818101
PubMed ID9514741
JournalJ Mol Biol
Year1998
Volume277
Pages81-102
AuthorsShen BW, Hennig M, Hohenester E, Jansonius JN, Schirmer T
TitleCrystal structure of human recombinant ornithine aminotransferase.
Related PDB1oat
Related Swiss-protP04181
[5]
CommentsX-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS)
Medline ID99096924
PubMed ID9878407
JournalJ Mol Biol
Year1999
Volume285
Pages297-309
AuthorsStorici P, Capitani G, Muller R, Schirmer T, Jansonius JN
TitleCrystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine.
Related PDB2oat
Related Swiss-protP04181

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.

createdupdated
2004-03-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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