EzCatDB: S00145
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00145
CATH domainDomain 12.60.120.10 : Jelly RollsCatalytic domain
E.C.1.2.3.4

CATH domainRelated DB codes (homologues)
2.60.120.10 : Jelly RollsS00155,D00842,D00843,T00255,M00216,T00101

Enzyme Name
UniProtKBKEGG

P45850
Protein nameOxalate oxidase 1oxalate oxidase
aero-oxalo dehydrogenase
oxalic acid oxidase
SynonymsEC 1.2.3.4
Germin
PfamPF00190 (Cupin_1)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00630Glyoxylate and dicarboxylate metabolism

UniProtKB:Accession NumberP45850
Entry nameOXO1_HORVU
ActivityOxalate + O(2) + 2 H(+) = 2 CO(2) + H(2)O(2).
SubunitHexamer.
Subcellular locationSecreted, extracellular space, apoplast (By similarity). Secreted, cell wall (By similarity).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00034C00007C00080C00209C00011C00027
CompoundManganeseO2H+OxalateCO2H2O2
Typeheavy metalothersotherscarboxyl groupothersothers
ChEBI18291
35154
27140
26689
15379
15378
16995
16526
16240
PubChem23930
977
1038
971
3819775
18676629
280
784
22326046
              
1fi2ABound:_MNUnbound UnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P45850
pdbCofactor-binding residues
         
1fi2AHIS 88;HIS 90;GLU 95;HIS 137(Manganese binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[9]p.1038-1039
[10]Fig.8, p.141-144
[11]Scheme 2, p.177-179

references
[1]
PubMed ID9143327
JournalArch Biochem Biophys
Year1997
Volume340
Pages239-49
AuthorsKotsira VP, Clonis YD
TitleOxalate oxidase from barley roots: purification to homogeneity and study of some molecular, catalytic, and binding properties.
[2]
PubMed ID9349269
JournalPlant Mol Biol
Year1997
Volume35
Pages459-69
AuthorsMembre N, Berna A, Neutelings G, David A, David H, Staiger D, Saez Vasquez J, Raynal M, Delseny M, Bernier F
TitlecDNA sequence, genomic organization and differential expression of three Arabidopsis genes for germin/oxalate oxidase-like proteins.
[3]
PubMed ID9765992
JournalBiochem Soc Trans
Year1998
Volume26
PagesS273
AuthorsRequena L, Bornemann S
TitleStructure and function studies of oxalate oxidase.
[4]
PubMed ID9573603
JournalBiotechnol Genet Eng Rev
Year1998
Volume15
Pages1-32
AuthorsDunwell JM
TitleCupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins.
[5]
PubMed ID9804177
JournalFEBS Lett
Year1998
Volume437
Pages87-90
AuthorsWoo EJ, Dunwell JM, Goodenough PW, Pickersgill RW
TitleBarley oxalate oxidase is a hexameric protein related to seed storage proteins: evidence from X-ray crystallography.
[6]
PubMed ID9541544
JournalJ Mol Evol
Year1998
Volume46
Pages488-93
AuthorsGane PJ, Dunwell JM, Warwicker J
TitleModeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase.
[7]
PubMed ID10493928
JournalBiochem J
Year1999
Volume343 Pt 1
Pages185-90
AuthorsRequena L, Bornemann S
TitleBarley (Hordeum vulgare) oxalate oxidase is a manganese-containing enzyme.
[8]
PubMed ID10952990
JournalJ Biol Chem
Year2000
Volume275
Pages36726-33
AuthorsCarter C, Thornburg RW
TitleTobacco nectarin I. Purification and characterization as a germin-like, manganese superoxide dismutase implicated in the defensE of floral reproductive tissues.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
Medline ID20517598
PubMed ID11062559
JournalNat Struct Biol
Year2000
Volume7
Pages1036-40
AuthorsWoo EJ, Dunwell JM, Goodenough PW, Marvier AC, Pickersgill RW
TitleGermin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities.
Related PDB1fi2
Related UniProtKBP45850
[10]
PubMed ID11862550
JournalJ Biol Inorg Chem
Year2002
Volume7
Pages136-45
AuthorsWhittaker MM, Whittaker JW
TitleCharacterization of recombinant barley oxalate oxidase expressed by Pichia pastoris.
[11]
PubMed ID15581576
JournalArch Biochem Biophys
Year2005
Volume433
Pages176-92
AuthorsSvedruzic D, Jonsson S, Toyota CG, Reinhardt LA, Ricagno S, Lindqvist Y, Richards NG
TitleThe enzymes of oxalate metabolism: unexpected structures and mechanisms.

comments
This enzyme belongs to the germin family.
The manganese ion seems to play an important role in catalysis.

createdupdated
2004-01-302009-03-19


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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.