ID   OXO2_HORVU              Reviewed;         224 AA.
AC   P45851;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Oxalate oxidase 2;
DE            EC=1.2.3.4;
DE   AltName: Full=Germin;
DE   Flags: Precursor;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. CM 72; TISSUE=Root;
RX   PubMed=8159797; DOI=10.1104/pp.104.2.803;
RA   Hurkman W.J., Lane B.G., Tanaka C.K.;
RT   "Nucleotide sequence of a transcript encoding a germin-like protein that is
RT   present in salt-stressed barley (Hordeum vulgare L.) roots.";
RL   Plant Physiol. 104:803-804(1994).
CC   -!- FUNCTION: Releases hydrogen peroxide in the apoplast. May play an
CC       important role in several aspects of plant growth and defense
CC       mechanisms.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + O2 + oxalate = 2 CO2 + H2O2; Xref=Rhea:RHEA:21880,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:30623; EC=1.2.3.4;
CC   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Root.
CC   -!- INDUCTION: By salt stress.
CC   -!- PTM: Glycosylated. A form called G contains antennary GlcNAc residues,
CC       whereas a form called G' lacks antennary GlcNAc residues in its
CC       otherwise identical glycans.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; U01963; AAA20245.1; -; mRNA.
DR   AlphaFoldDB; P45851; -.
DR   SMR; P45851; -.
DR   OMA; LDVSEWP; -.
DR   ExpressionAtlas; P45851; baseline and differential.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0050162; F:oxalate oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   2: Evidence at transcript level;
KW   Apoplast; Cell wall; Disulfide bond; Glycoprotein; Manganese;
KW   Metal-binding; Oxidoreductase; Secreted; Signal; Stress response.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..224
FT                   /note="Oxalate oxidase 2"
FT                   /id="PRO_0000010833"
FT   DOMAIN          63..214
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..49
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   224 AA;  23479 MW;  425B69B31C1CAECF CRC64;
     MGYSKTLAVS LFAVLLLAPA VLASDPDPLQ DFCVADLDGK AVSVNGHPCK PMSEAGDDFL
     FSSKLAKAGN TSTPNGSAVT ELDVAEWPGT NTLGVSMNRV DFAPGGTNPP HVHPRATEIG
     IVMKGELLVG ILGSLDSGNK LYSRVVRAGE TFLIPRGLMH FQFNVGKTEA SMVVSFNSQN
     PGIVFVPLTL FGSNPPIPTP VLTKALRVEA GVVELLKSKF AAGF