APX3_ORYSI
ID APX3_ORYSI Reviewed; 291 AA.
AC Q01MI9; A2XQN2; Q6TY83; Q7XWZ7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Probable L-ascorbate peroxidase 3;
DE EC=1.11.1.11;
DE AltName: Full=OsAPx03;
GN Name=APX3; ORFNames=H0515C11.2, OsI_014375;
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND NOMENCLATURE.
RX PubMed=15599508; DOI=10.1007/s00239-004-2666-z;
RA Teixeira F.K., Menezes-Benavente L., Margis R., Margis-Pinheiro M.;
RT "Analysis of the molecular evolutionary history of the ascorbate peroxidase
RT gene family: inferences from the rice genome.";
RL J. Mol. Evol. 59:761-770(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
CC -!- FUNCTION: Plays a key role in hydrogen peroxide removal. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O2 + L-ascorbate = 2 H2O + L-dehydroascorbate;
CC Xref=Rhea:RHEA:22996, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58539; EC=1.11.1.11;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Binds one cation per subunit; probably K(+), but might
CC also be Ca(2+). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: According to PubMed:15599508, it may be peroxisomal. There is
CC however no experimental evidence to prove this. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY382617; AAQ88105.1; -; mRNA.
DR EMBL; CR855043; CAH66026.1; -; Genomic_DNA.
DR EMBL; CM000129; EAY93142.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01MI9; -.
DR SMR; Q01MI9; -.
DR STRING; 39946.Q01MI9; -.
DR EnsemblPlants; BGIOSGA015546-TA; BGIOSGA015546-PA; BGIOSGA015546.
DR Gramene; BGIOSGA015546-TA; BGIOSGA015546-PA; BGIOSGA015546.
DR HOGENOM; CLU_036959_3_0_1; -.
DR OMA; DANQGAR; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR002207; Peroxidase_I.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 2: Evidence at transcript level;
KW Calcium; Heme; Hydrogen peroxide; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Peroxidase; Potassium; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..291
FT /note="Probable L-ascorbate peroxidase 3"
FT /id="PRO_0000300258"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 113..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 41
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297,
FT ECO:0000255|PROSITE-ProRule:PRU10012"
FT BINDING 161
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
FT BINDING 162
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00297"
SQ SEQUENCE 291 AA; 32076 MW; 9D2E57C3DBC277F6 CRC64;
MSAAPVVDAE YMAEVERARR DLRALIASKS CAPIMLRLAW HDAGTYDKAT KTGGPNGSIR
FPQEYSHAAN AGIKIAIDLL EPMKQRHPKI TYADLYQLAG VVAVEVTGGP TIDYVPGRRD
SSDSPEEGRL PDAKKGAAHL REVFYRMGLS DKDIVALSGG HTLGKARPER SGFDGAWTKD
PLKFDNSYFI ELLKENSEGL LKLPTDKALV EDPTFRRYVE LYAKDEDAFF RDYAESHKKL
SELGFTPPRS AFIYKSCQKP KSLLMQTAAG VAVAAAVVAW AYLCESNKRL G
