EzCatDB: M00031

DB codeM00031
CATH domainDomain 13.40.50.220
Domain 23.40.640.10Catalytic domain
Domain 33.90.1150.10
Domain 43.90.100.10
E.C.4.1.1.17
CSA1ord

CATH domainRelated DB codes (homologues)
3.40.640.10D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,D00279
3.90.1150.10D00085,D00092,D00101,D00102,D00103,D00104,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,D00279

Enzyme Name
Swiss-protKEGG

P43099
Protein nameOrnithine decarboxylase, inducibleornithine decarboxylase
SpeC
L-ornithine carboxy-lyase
SynonymsODC
EC 4.1.1.17

KEGG pathways
MAP codePathways
MAP00220Urea cycle and metabolism of amino groups
MAP00480Glutathione metabolism

Swiss-prot:Accession NumberP43099
Entry nameDCOR_LACS3
ActivityL-ornithine = putrescine + CO(2).
SubunitDodecamer.
Subcellular location
CofactorPyridoxal phosphate.


CofactorsSubstratesProducts
KEGG-idC00018C00077C00134C00011
CompoundPyridoxal phosphateL-OrnithinePutrescineCO2
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,amine group,lipidamine group,lipidothers
1c4kA01UnboundUnboundUnboundUnbound
1ordA01UnboundUnboundUnboundUnbound
1ordB01UnboundUnboundUnboundUnbound
1c4kA02Bound:PLPUnboundUnboundUnbound
1ordA02Bound:PLPUnboundUnboundUnbound
1ordB02Bound:PLPUnboundUnboundUnbound
1c4kA03UnboundUnboundUnboundUnbound
1ordA03UnboundUnboundUnboundUnbound
1ordB03UnboundUnboundUnboundUnbound
1c4kA04UnboundUnboundUnboundUnbound
1ordA04UnboundUnboundUnboundUnbound
1ordB04UnboundUnboundUnboundUnbound

Active-site residues
resource
literature [3], [4]
pdbCatalytic residuesCofactor-binding residuescomment
1c4kA01


1ordA01


1ordB01


1c4kA02HIS 223;ASP 316;HIS 354;LYS 355
LYS 355(PLP binding)
utant G121Y
1ordA02HIS 223;ASP 316;HIS 354;LYS 355
LYS 355(PLP binding)

1ordB02HIS 223;ASP 316;HIS 354;LYS 355
LYS 355(PLP binding)

1c4kA03


1ordA03


1ordB03


1c4kA04


1ordA04


1ordB04



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]p.648-649, Table 1
[4]p.851
[6]Scheme 1
[7]p.1983-1984

references
[1]
PubMed ID2925664
JournalJ Biol Chem
Year1989
Volume264
Pages4722-4
AuthorsMomany C, Hackert ML
TitleCrystallization and molecular symmetry of ornithine decarboxylase from Lactobacillus 30a.
[2]
PubMed ID1715911
JournalJ Electron Microsc Tech
Year1991
Volume18
Pages157-66
AuthorsStoops JK, Momany C, Ernst SR, Oliver RM, Schroeter JP, Bretaudiere JP, Hackert ML
TitleComparisons 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.
[3]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
Medline ID96017733
PubMed ID7563080
JournalJ Mol Biol
Year1995
Volume252
Pages643-55
AuthorsMomany C, Ernst S, Ghosh R, Chang NL, Hackert ML
TitleCrystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution.
Related PDB1c4k
Related Swiss-protP43099
[4]
PubMed ID7663340
JournalProtein Sci
Year1995
Volume4
Pages849-54
AuthorsMomany C, Ghosh R, Hackert ML
TitleStructural motifs for pyridoxal-5'-phosphate binding in decarboxylases: an analysis based on the crystal structure of the Lactobacillus 30a ornithine decarboxylase.
[5]
PubMed ID9405048
JournalBiochemistry
Year1997
Volume36
Pages16147-54
AuthorsOliveira MA, Carroll D, Davidson L, Momany C, Hackert ML
TitleThe GTP effector site of ornithine decarboxylase from Lactobacillus 30a: kinetic and structural characterization.
[6]
PubMed ID9442028
JournalJ Biol Chem
Year1998
Volume273
Pages1939-45
AuthorsTramonti A, De Biase D, Giartosio A, Bossa F, John RA
TitleThe roles of His-167 and His-275 in the reaction catalyzed by glutamate decarboxylase from Escherichia coli.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
Medline ID20133100
PubMed ID10666573
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages1978-85
AuthorsVitali J, Carroll D, Chaudhry RG, Hackert ML
TitleThree-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.
Related PDB1ord
Related Swiss-protP43099
[8]
PubMed ID10477260
JournalBiochem J
Year1999
Volume342 Pt 3
Pages509-12
AuthorsBertoldi M, Carbone V, Borri Voltattorni C
TitleOrnithine and glutamate decarboxylases catalyse an oxidative deamination of their alpha-methyl substrates.


createdupdated
2004-05-202009-02-26


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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