ID A0A2H5P0U8_CITUN Unreviewed; 859 AA.
AC A0A2H5P0U8;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=L-ascorbate peroxidase {ECO:0000256|ARBA:ARBA00012940};
DE EC=1.11.1.11 {ECO:0000256|ARBA:ARBA00012940};
GN ORFNames=CUMW_093530 {ECO:0000313|EMBL:GAY45982.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY45982.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY45982.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
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 Evidence={ECO:0000256|ARBA:ARBA00000939};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ascorbate peroxidase
CC subfamily. {ECO:0000256|ARBA:ARBA00006873}.
CC -!- SIMILARITY: Belongs to the synaptotagmin family.
CC {ECO:0000256|ARBA:ARBA00006996}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY45982.1}.
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DR EMBL; BDQV01000031; GAY45982.1; -; Genomic_DNA.
DR EMBL; BDQV01000031; GAY45983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5P0U8; -.
DR STRING; 55188.A0A2H5P0U8; -.
DR Proteomes; UP000236630; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProt.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016688; F:L-ascorbate peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00691; ascorbate_peroxidase; 1.
DR CDD; cd00030; C2; 1.
DR CDD; cd21677; SMP_SYT; 1.
DR Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
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 InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR045050; Synaptotagmin_plant.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR PANTHER; PTHR10774:SF188; CALCIUM-DEPENDENT LIPID-BINDING (CALB DOMAIN) FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR10774; EXTENDED SYNAPTOTAGMIN-RELATED; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF17047; SMP_LBD; 1.
DR PRINTS; PR00459; ASPEROXIDASE.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00458; PEROXIDASE.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
DR PROSITE; PS51847; SMP; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000236630};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055}.
FT TRANSMEM 7..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..249
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 240..362
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 401..519
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 603..833
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
SQ SEQUENCE 859 AA; 96828 MW; BEDB858170D9CC8F CRC64;
MGVISTIFGF CGFGVGISSG LVIGYFLFIY FQPTDVKNPE IRPLVERDSE TLQQMLPEIP
LWVKCPDYDR VDWLNKFLEL MWPYLDKAIC KTAKNIAKPI IAEQIPKYKI ESVEFETLTL
GTLPPTFQGM KVYVTDEKEL IMEPCLKWAA NPNVTIGVKA FGLKATVQVV DLQVFAQPRI
TLKPLVPAFP CFANIYVSLM EKPHVDFGLK LVGADLMSIP GLYRFVQELI KTQVANMYLW
PKTLEVPILD PSKAYRRPVG ILHVKVVKAM NLKKKDLLGA SDPYVKLKIT EDKLPSKKTT
VKHKNLNPEW NEEYNFTVRD PESQAVELAV YDWEQVGKHD KMGMNVVPLK ELTPEEPSVK
TLDLLKNMDL NDGQNEKSRG QLVVEFIYKP FKEEDLPKSF EESQTVQKAP ENTPAGGGLL
VVIVHEAQDV EGKHHTNPYA RILFRGEERK TKHVKKNRDP RWEEEFQFML EEPPTNDRLH
VEVCSVSSRI GLLHPKETLG YIDINLSDVV SNKRINEKYH LIDSKNGRIQ IDYKPSRGTV
ILHGPSPLTI SSRKTNDSCR KLSKGRYTEG APMALPVVDT EYLKEIDKAR RDLRALIAYK
NCAPIMLRLA WHDAGTYDVN TKTGGPNGSI RNEEEYSHGS NNGLKIALDF CEEVKAKHPK
ITYADLYQLA GVVAVEVTGG PTVDFFPGRK DSKISPKEGR LPDAKRGAPH LRDIFYRMGL
SDKDIVALSG GHTLGRAHPE RSGFDGPWTR EPLKFDNSYF VELLNGESEG LLQLPTDKAL
LEDPEFHRYV VLYAKDEDAF FRDYAASHKK LSELGFSPGS GSKSTANDCT ILAQGAVGVA
VTAAVVILSY FYEVRKRMK
//
