ID A0A074XI75_AURPU Unreviewed; 627 AA.
AC A0A074XI75;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:KEQ81732.1};
GN ORFNames=M438DRAFT_323887 {ECO:0000313|EMBL:KEQ81732.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ81732.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ81732.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ81732.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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DR EMBL; KL584990; KEQ81732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XI75; -.
DR STRING; 1043002.A0A074XI75; -.
DR HOGENOM; CLU_033051_0_0_1; -.
DR OrthoDB; 1086441at2759; -.
DR Proteomes; UP000030706; 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:KEQ81732.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030706}.
FT BINDING 387
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 627 AA; 70679 MW; 4CA5468CEA1FE70C CRC64;
MDAPNFRPGF LDRLLVGLFH FVNFFIPWHK LPSIIGALNL DALRVELRQF NLHDGYTSAT
AQGNTEDTPL DDKRFLSARN SEGKDNSLTM PKMGCSGMRF GRNFPRKYCE KPTEEELWTP
NPILVSEAFM SRKPGEFKPA TTLNLLAAAW IQFQVHDWVF HESSEETFDV PLLPNDTWHD
HQMKLYRTKP DEVLDASDIK CPGYKNTSTA WWDGSQIYGS SEAVTRELRD QHQDGKLLLE
TRGYEETFLP RDAEGNPKTG FSDNWWTGME LLHTLFALEH NAICVKIREA HPDWTGDKIF
DKARLVNCAL MAKIHTVEWT PAILGHPTLE ISMNANWWGI AGETLNKIVG RISKTSEAIS
GIPGSTVDHQ GVSYSLTEEF VSVYRMHSLI PDNVAFFDVA SGKHKATVPV AEITFKDAVK
PLKSGKVSFA DAFYSFCINY PGAITNNNYA NLMRNLPTPD GQVRDLATVD ILRDRERGVP
RYCQFRRLLR LSVPKTFDEL TGGDKELAAR LSEVYSGDIE TVDALVGSHS EPVIKGFGFS
ETAFRIFILM ASRRLKSDRF IAGQWNADMY TEVGFHWVQN TGMKDVLARH FPELAAAIPK
KTNVFAPWVK LPGSRAYTGV ETNAPET
//
