DB code: M00031

CATH domain 3.40.50.220 : Rossmann fold
3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
3.90.1150.10 : Aspartate Aminotransferase, domain 1
3.90.100.10 : Ornithine Decarboxylase; Chain A, domain 4
E.C. 4.1.1.17
CSA 1ord
M-CSA 1ord
MACiE

CATH domain Related DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P43099 Ornithine decarboxylase, inducible
ODC
EC 4.1.1.17
PF01276 (OKR_DC_1)
PF03711 (OKR_DC_1_C)
PF03709 (OKR_DC_1_N)
[Graphical View]

KEGG enzyme name
ornithine decarboxylase
SpeC
L-ornithine carboxy-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P43099 DCOR_LACS3 L-ornithine = putrescine + CO(2). Dodecamer. Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00220 Urea cycle and metabolism of amino groups
MAP00480 Glutathione metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C00077 C00134 C00011
E.C.
Compound Pyridoxal phosphate L-Ornithine Putrescine CO2
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,amine group,lipid amine group,lipid others
ChEBI 18405
15729
17148
16526
PubChem 1051
6262
88747248
1045
280
1c4kA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ordA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ordB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1c4kA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound
1ordA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound
1ordB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:PLP Unbound Unbound Unbound
1c4kA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ordA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ordB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1c4kA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ordA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1ordB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [3], [4]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1c4kA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ordA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ordB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1c4kA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 223;ASP 316;HIS 354;LYS 355 LYS 355(PLP binding) utant G121Y
1ordA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 223;ASP 316;HIS 354;LYS 355 LYS 355(PLP binding)
1ordB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 223;ASP 316;HIS 354;LYS 355 LYS 355(PLP binding)
1c4kA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ordA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ordB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1c4kA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ordA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ordB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
p.648-649, Table 1
[4]
p.851
[6]
Scheme 1
[7]
p.1983-1984

References
[1]
Resource
Comments
Medline ID
PubMed ID 2925664
Journal J Biol Chem
Year 1989
Volume 264
Pages 4722-4
Authors Momany C, Hackert ML
Title Crystallization and molecular symmetry of ornithine decarboxylase from Lactobacillus 30a.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1715911
Journal J Electron Microsc Tech
Year 1991
Volume 18
Pages 157-66
Authors Stoops JK, Momany C, Ernst SR, Oliver RM, Schroeter JP, Bretaudiere JP, Hackert ML
Title Comparisons of the low-resolution structures of ornithine decarboxylase by electron microscopy and X-ray crystallography: the utility of methylamine tungstate stain and Butvar support film in the study of macromolecules by transmission electron microscopy.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID 96017733
PubMed ID 7563080
Journal J Mol Biol
Year 1995
Volume 252
Pages 643-55
Authors Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML
Title Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution.
Related PDB 1c4k
Related UniProtKB P43099
[4]
Resource
Comments
Medline ID
PubMed ID 7663340
Journal Protein Sci
Year 1995
Volume 4
Pages 849-54
Authors Momany C, Ghosh R, Hackert ML
Title Structural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 9405048
Journal Biochemistry
Year 1997
Volume 36
Pages 16147-54
Authors Oliveira MA, Carroll D, Davidson L, Momany C, Hackert ML
Title The GTP effector site of ornithine decarboxylase from Lactobacillus 30a: kinetic and structural characterization.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9442028
Journal J Biol Chem
Year 1998
Volume 273
Pages 1939-45
Authors Tramonti A, De Biase D, Giartosio A, Bossa F, John RA
Title The roles of His-167 and His-275 in the reaction catalyzed by glutamate decarboxylase from Escherichia coli.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID 20133100
PubMed ID 10666573
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 1978-85
Authors Vitali J, Carroll D, Chaudhry RG, Hackert ML
Title Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.
Related PDB 1ord
Related UniProtKB P43099
[8]
Resource
Comments
Medline ID
PubMed ID 10477260
Journal Biochem J
Year 1999
Volume 342 Pt 3
Pages 509-12
Authors Bertoldi M, Carbone V, Borri Voltattorni C
Title Ornithine and glutamate decarboxylases catalyse an oxidative deamination of their alpha-methyl substrates.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-05-20 2009-02-26