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UniProtKB/Swiss-Prot entry P45850


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name OXO1_HORVU
Primary accession number P45850
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 58)
Name and origin of the protein
Protein name Oxalate oxidase 1
Synonyms EC 1.2.3.4
Germin
Gene name None
From
Hordeum vulgare (Barley) [TaxID: 4513] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Pooideae; Triticeae; Hordeum.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-18.
TISSUE=Seedling root;
PubMed=8509360 [NCBI, ExPASy, EBI, Israel, Japan]
Lane B.G., Dunwell J.M., Ray J.A., Schmitt M.R., Cuming A.C.;
"Germin, a protein marker of early plant development, is an oxalate oxidase.";
J. Biol. Chem. 268:12239-12242(1993).
[2]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
DOI=10.1038/80954; PubMed=11062559 [NCBI, ExPASy, EBI, Israel, Japan]
Woo E.-J., Dunwell J.M., Goodenough P.W., Marvier A.C., Pickersgill R.W.;
"Germin is a manganese containing homohexamer with oxalate oxidase and superoxide dismutase activities.";
Nat. Struct. Biol. 7:1036-1040(2000).
Comments
  • FUNCTION: Releases hydrogen peroxide in the apoplast which may be important for cross-linking reactions in the cell wall biochemistry. May play an important role in several aspects of plant growth and defense mechanisms.
  • CATALYTIC ACTIVITY: Oxalate + O2 + 2 H+ = 2 CO2 + H2O2.
  • SUBUNIT: Hexamer.
  • SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast (By similarity). Secreted, cell wall (By similarity).
  • INDUCTION: By salt stress.
  • PTM: Glycosylated. A form called G contains antennary GlcNAc residues, whereas a form called G' lacks antennary GlcNAc residues in its otherwise identical glycans.
  • SIMILARITY: Belongs to the germin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
L15737; AAA32959.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A45980; A45980.
3D structure databases
PDB
1FI2; X-ray; 1.60 A; A=2-201.[ExPASy / RCSB / EBI]
2ET1; X-ray; 1.60 A; A=2-201.[ExPASy / RCSB / EBI]
2ET7; X-ray; 1.70 A; A=1-201.[ExPASy / RCSB / EBI]
2ETE; X-ray; 1.75 A; A/B=1-201.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FI2; -.
2ET1; -.
2ET7; -.
2ETE; -.
ModBase P45850.
Organism-specific databases
Gramene P45850; -.
Family and domain databases
InterPro IPR006045; Cupin_1.
IPR001929; Germin.
IPR014710; RmlC-like_jellyroll.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
Pfam PF00190; Cupin_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00325; GERMIN.
PROSITE PS00725; GERMIN; 1.
BLOCKS P45850.
Other
ProtoNet P45850.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoplast; Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing; Glycoprotein; Manganese; Metal-binding; Oxidoreductase; Secreted; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   201  201     Oxalate oxidase 1. PRO_0000192013
METAL   88    88        Manganese. 
METAL   90    90        Manganese. 
METAL   95    95        Manganese. 
METAL   137   137        Manganese. 
CARBOHYD   47    47        N-linked (GlcNAc...). 
CARBOHYD   52    52        N-linked (GlcNAc...) (Potential). 
DISULFID   10    26         
STRAND   6     8  3      
HELIX   29    31  3      
STRAND   53    60  8      
TURN   61    63  3      
HELIX   65    67  3      
STRAND   73    79  7      
STRAND   84    89  6      
STRAND   95   109  15      
HELIX   112   114  3      
STRAND   117   124  8      
STRAND   128   131  4      
STRAND   137   141  5      
STRAND   143   145  3      
STRAND   147   156  10      
HELIX   163   169  7      
HELIX   176   183  8      
HELIX   187   196  10      
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 21203 Da [This is the MW of the unprocessed precursor] CRC64: 76764D474CCB0F26 [This is a checksum on the sequence]
        10         20         30         40         50         60 
SDPDPLQDFC VADLDGKAVS VNGHTCKPMS EAGDDFLFSS KLTKAGNTST PNGSAVTELD 

        70         80         90        100        110        120 
VAEWPGTNTL GVSMNRVDFA PGGTNPPHIH PRATEIGMVM KGELLVGILG SLDSGNKLYS 

       130        140        150        160        170        180 
RVVRAGETFV IPRGLMHFQF NVGKTEAYMV VSFNSQNPGI VFVPLTLFGS DPPIPTPVLT 

       190        200 
KALRVEAGVV ELLKSKFAGG S 

P45850 in FASTA format

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