ID A0A177E1G1_ALTAL Unreviewed; 632 AA.
AC A0A177E1G1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:OAG25072.1};
GN ORFNames=CC77DRAFT_299044 {ECO:0000313|EMBL:OAG25072.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG25072.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG25072.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25072.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KV441470; OAG25072.1; -; Genomic_DNA.
DR RefSeq; XP_018390493.1; XM_018531124.1.
DR AlphaFoldDB; A0A177E1G1; -.
DR STRING; 5599.A0A177E1G1; -.
DR GeneID; 29116718; -.
DR KEGG; aalt:CC77DRAFT_299044; -.
DR VEuPathDB; FungiDB:CC77DRAFT_299044; -.
DR OMA; AFAPWTK; -.
DR OrthoDB; 1086441at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09818; PIOX_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR034815; A_dioxygenase.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR PANTHER; PTHR11903:SF11; ALPHA-DIOXYGENASE 1; 1.
DR PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
PE 4: Predicted;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Peroxidase {ECO:0000313|EMBL:OAG25072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248}.
FT BINDING 395
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:0000256|PIRSR:PIRSR619791-2"
SQ SEQUENCE 632 AA; 71030 MW; 0811B0374F15486C CRC64;
MGVSSQSKPE PYTYTPGLPQ RALIAVFHGV NNIIPWHKLP TWIGVLNVAA FRYELRQKNL
HDVYPSPNDQ GTLGCPHLSD EQYLHTRHSD GLFNDLSAPK MGCTGMRFGR NVPREHTAKP
SEEELMTPNP RLISEQLLKR DNFKPATSLN LLAAAWIQFQ VHDWFQHENS ASETYTVPLP
EGDKWSSPDG RMKIEQTQPD AVLDKTDKTA PAYRNVNTHW WDGSQIYGST ELRTTELRGQ
SKNGKLTVDT QKIATFLPRD SNGIPQTGFM TNWWLGLEML HTLFVLEHNT ICDALVTAYP
SWSSERIFDT ARLVNCALMA KIHTVEWTPA ILAHPVLEIS MNANWWGVLG ERLYKLLGRV
SATSEAISGI PGSSVEHHAA PYALTEEFVS VYRMHALIPD TIAFFNSRTG EHKTTHSIGD
VAFEKARAPL ENDGLDFSDV FYSFGVNYPG AITLNNTPDF LRDLHTPDGR HIDLSTIDVL
RDRERGVPRY NAFRRLFHLA PMTSFLELTG GNKAVAEKLA VIYEDDIEKV DLLVGCLAEP
LPAGFGFSDT AFRVFILMAS RRLKSDRFIA GDWNEKTYSK VGMQWVQNGG MKDVLGRHFP
ELESVLAKSG NPFAPWAMKD ASKKYEGKET NA
//
