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Database: UniProt
Entry: A0A1B9IH11_9TREE
LinkDB: A0A1B9IH11_9TREE
Original site: A0A1B9IH11_9TREE 
ID   A0A1B9IH11_9TREE        Unreviewed;       374 AA.
AC   A0A1B9IH11;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Peroxidase {ECO:0000256|RuleBase:RU363051};
DE            EC=1.11.1.- {ECO:0000256|RuleBase:RU363051};
GN   ORFNames=L486_07510 {ECO:0000313|EMBL:OCF54855.1};
OS   Kwoniella mangroviensis CBS 10435.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1331196 {ECO:0000313|EMBL:OCF54855.1, ECO:0000313|Proteomes:UP000092583};
RN   [1] {ECO:0000313|EMBL:OCF54855.1, ECO:0000313|Proteomes:UP000092583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10435 {ECO:0000313|EMBL:OCF54855.1,
RC   ECO:0000313|Proteomes:UP000092583};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Kwoniella mangroviensis CBS10435.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000092583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10435 {ECO:0000313|Proteomes:UP000092583};
RA   Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA   Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT   "Evolution of pathogenesis and genome organization in the Tremellales.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC       {ECO:0000256|ARBA:ARBA00003917}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-
CC         [cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5;
CC         Evidence={ECO:0000256|ARBA:ARBA00035967};
CC   -!- SUBUNIT: Forms a one-to-one complex with cytochrome c.
CC       {ECO:0000256|ARBA:ARBA00038574}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000256|ARBA:ARBA00004305}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Cytochrome c peroxidase
CC       subfamily. {ECO:0000256|ARBA:ARBA00005997}.
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DR   EMBL; KI669468; OCF54855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9IH11; -.
DR   STRING; 1331196.A0A1B9IH11; -.
DR   Proteomes; UP000092583; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR   CDD; cd00691; ascorbate_peroxidase; 1.
DR   Gene3D; 1.10.520.10; -; 1.
DR   Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
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:SF58; CYTOCHROME C PEROXIDASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR31356; THYLAKOID LUMENAL 29 KDA PROTEIN, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00141; peroxidase; 1.
DR   PRINTS; PR00459; ASPEROXIDASE.
DR   PRINTS; PR00458; PEROXIDASE.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS00435; PEROXIDASE_1; 1.
DR   PROSITE; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU363051};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU363051};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092583};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          95..374
FT                   /note="Plant heme peroxidase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50873"
SQ   SEQUENCE   374 AA;  41402 MW;  A0E34A05E12017BE CRC64;
     MSFRTPLLRT ACARRAGQSV QLRSPVVRRR FASGGPEVSP PPPPRSSSVP YLLAGVGLAA
     AGAAYLFYGT DGTPRETAKE LESSARGAAA AAEGKLGLRH SQKDYQKVYD RIAETLDKEG
     YDDGSLAPVL IRLAWHSSGT YNKEDNSGGS NYATMRFKPE AEHGANNGLG VARDHMQKIK
     DEFPWISYGD LWTLGGVAAV QESGGPTIPW RPGRIDGFEH NVTPDGRLPD AAQAQDHLRF
     IFYRMGFNDQ EIVALSGAHA MGRCHTDRSG FEGPWTFSPV TFSNQYFTLL EDEPWQWRKW
     KGPAQYEDKK TKSLMMLPTD MALVKDKSFK KFVDIYAKDE DAFFKDFSKA FAKLLELGVP
     TAQFAGEPWK MGSE
//
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