OXO1_HORVU
ID OXO1_HORVU Reviewed; 201 AA.
AC P45850;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Oxalate oxidase 1 {ECO:0000303|PubMed:11062559, ECO:0000303|PubMed:8509360};
DE EC=1.2.3.4 {ECO:0000269|PubMed:11062559, ECO:0000269|PubMed:16291738};
DE AltName: Full=Germin {ECO:0000303|PubMed:11062559, ECO:0000303|PubMed:8509360};
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], PROTEIN SEQUENCE OF 1-18, GLYCOSYLATION,
RP INDUCTION BY SALT, AND SUBCELLULAR LOCATION.
RC TISSUE=Seedling root;
RX PubMed=8509360; DOI=10.1016/s0021-9258(18)31377-2;
RA Lane B.G., Dunwell J.M., Ray J.A., Schmitt M.R., Cuming A.C.;
RT "Germin, a protein marker of early plant development, is an oxalate
RT oxidase.";
RL J. Biol. Chem. 268:12239-12242(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH MANGANESE, SUBUNIT,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11062559; DOI=10.1038/80954;
RA Woo E.-J., Dunwell J.M., Goodenough P.W., Marvier A.C., Pickersgill R.W.;
RT "Germin is a manganese containing homohexamer with oxalate oxidase and
RT superoxide dismutase activities.";
RL Nat. Struct. Biol. 7:1036-1040(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
RP GLYOXYLIC ACID, GLYCOSYLATION AT ASN-47, DISULFIDE BONDS, FUNCTION,
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASN-75 AND ASN-85.
RX PubMed=16291738; DOI=10.1074/jbc.m510256200;
RA Opaleye O., Rose R.-S., Whittaker M.M., Woo E.-J., Whittaker J.W.,
RA Pickersgill R.W.;
RT "Structural and spectroscopic studies shed light on the mechanism of
RT oxalate oxidase.";
RL J. Biol. Chem. 281:6428-6433(2006).
CC -!- FUNCTION: Releases hydrogen peroxide in the apoplast which may be
CC important for cross-linking reactions in the cell wall biochemistry.
CC May play an important role in several aspects of plant growth and
CC defense mechanisms. {ECO:0000269|PubMed:11062559,
CC ECO:0000269|PubMed:16291738}.
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 Evidence={ECO:0000269|PubMed:11062559, ECO:0000269|PubMed:16291738};
CC -!- SUBUNIT: Homo hexamer; a trimer of dimers.
CC {ECO:0000269|PubMed:11062559}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250, ECO:0000303|PubMed:8509360}. Secreted, cell wall
CC {ECO:0000250, ECO:0000303|PubMed:8509360}.
CC -!- INDUCTION: By salt stress. {ECO:0000303|PubMed:8509360}.
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. {ECO:0000269|PubMed:16291738,
CC ECO:0000269|PubMed:8509360}.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; L15737; AAA32959.1; -; mRNA.
DR PIR; A45980; A45980.
DR PDB; 1FI2; X-ray; 1.60 A; A=1-201.
DR PDB; 2ET1; X-ray; 1.60 A; A=1-201.
DR PDB; 2ET7; X-ray; 1.70 A; A=1-201.
DR PDB; 2ETE; X-ray; 1.75 A; A/B=1-201.
DR PDBsum; 1FI2; -.
DR PDBsum; 2ET1; -.
DR PDBsum; 2ET7; -.
DR PDBsum; 2ETE; -.
DR AlphaFoldDB; P45850; -.
DR SMR; P45850; -.
DR MoonProt; P45850; -.
DR PRIDE; P45850; -.
DR BioCyc; MetaCyc:MON-16186; -.
DR BRENDA; 1.2.3.4; 2687.
DR SABIO-RK; P45850; -.
DR EvolutionaryTrace; P45850; -.
DR ExpressionAtlas; P45850; baseline and differential.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:1902693; C:superoxide dismutase complex; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0030145; F:manganese ion binding; IDA:CAFA.
DR GO; GO:0050162; F:oxalate oxidase activity; IDA:CAFA.
DR GO; GO:0004784; F:superoxide dismutase activity; IDA:CAFA.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019430; P:removal of superoxide radicals; IDA:CAFA.
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 1: Evidence at protein level;
KW 3D-structure; Apoplast; Cell wall; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Manganese;
KW Metal-binding; Oxidoreductase; Secreted; Stress response.
FT CHAIN 1..201
FT /note="Oxalate oxidase 1"
FT /id="PRO_0000192013"
FT DOMAIN 40..191
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 75
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ETE"
FT BINDING 85
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:16291738,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ETE"
FT BINDING 88
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11062559,
FT ECO:0000269|PubMed:16291738, ECO:0007744|PDB:1FI2,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ET7,
FT ECO:0007744|PDB:2ETE"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11062559,
FT ECO:0000269|PubMed:16291738, ECO:0007744|PDB:1FI2,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ET7,
FT ECO:0007744|PDB:2ETE"
FT BINDING 90
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:16291738,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ETE"
FT BINDING 95
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11062559,
FT ECO:0000269|PubMed:16291738, ECO:0007744|PDB:1FI2,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ETE"
FT BINDING 95
FT /ligand="oxalate"
FT /ligand_id="ChEBI:CHEBI:30623"
FT /evidence="ECO:0000269|PubMed:16291738,
FT ECO:0007744|PDB:2ETE"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:11062559,
FT ECO:0000269|PubMed:16291738, ECO:0007744|PDB:1FI2,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ET7,
FT ECO:0007744|PDB:2ETE"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16291738,
FT ECO:0007744|PDB:2ETE"
FT DISULFID 10..26
FT /evidence="ECO:0000269|PubMed:11062559,
FT ECO:0000269|PubMed:16291738, ECO:0007744|PDB:1FI2,
FT ECO:0007744|PDB:2ET1, ECO:0007744|PDB:2ET7,
FT ECO:0007744|PDB:2ETE"
FT MUTAGEN 75
FT /note="N->A: Impaired oxalate oxidase activity."
FT /evidence="ECO:0000269|PubMed:16291738"
FT MUTAGEN 85
FT /note="N->A: Impaired oxalate oxidase activity."
FT /evidence="ECO:0000269|PubMed:16291738"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1FI2"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1FI2"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1FI2"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 95..109
FT /evidence="ECO:0007829|PDB:1FI2"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:1FI2"
FT STRAND 147..156
FT /evidence="ECO:0007829|PDB:1FI2"
FT HELIX 163..169
FT /evidence="ECO:0007829|PDB:1FI2"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:1FI2"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:1FI2"
SQ SEQUENCE 201 AA; 21203 MW; 76764D474CCB0F26 CRC64;
SDPDPLQDFC VADLDGKAVS VNGHTCKPMS EAGDDFLFSS KLTKAGNTST PNGSAVTELD
VAEWPGTNTL GVSMNRVDFA PGGTNPPHIH PRATEIGMVM KGELLVGILG SLDSGNKLYS
RVVRAGETFV IPRGLMHFQF NVGKTEAYMV VSFNSQNPGI VFVPLTLFGS DPPIPTPVLT
KALRVEAGVV ELLKSKFAGG S
