ID   A0A074WLF9_9PEZI        Unreviewed;      1099 AA.
AC   A0A074WLF9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Heme peroxidase {ECO:0000313|EMBL:KEQ70602.1};
GN   ORFNames=M436DRAFT_53115 {ECO:0000313|EMBL:KEQ70602.1};
OS   Aureobasidium namibiae CBS 147.97.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX   NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ70602.1, ECO:0000313|Proteomes:UP000027730};
RN   [1] {ECO:0000313|EMBL:KEQ70602.1, ECO:0000313|Proteomes:UP000027730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ70602.1,
RC   ECO:0000313|Proteomes:UP000027730};
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).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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DR   EMBL; KL584716; KEQ70602.1; -; Genomic_DNA.
DR   RefSeq; XP_013424870.1; XM_013569416.1.
DR   AlphaFoldDB; A0A074WLF9; -.
DR   STRING; 1043004.A0A074WLF9; -.
DR   GeneID; 25411717; -.
DR   HOGENOM; CLU_002329_1_0_1; -.
DR   OrthoDB; 3322316at2759; -.
DR   Proteomes; UP000027730; 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:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd20612; CYP_LDS-like_C; 1.
DR   CDD; cd09817; linoleate_diol_synthase_like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   InterPro; IPR034812; Ppo-like_N.
DR   PANTHER; PTHR11903:SF37; LINOLEATE 8R-LIPOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   Pfam; PF03098; An_peroxidase; 2.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW   Oxidoreductase {ECO:0000313|EMBL:KEQ70602.1};
KW   Peroxidase {ECO:0000313|EMBL:KEQ70602.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027730}.
FT   BINDING         371
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   1099 AA;  124386 MW;  5C606159DEC365A1 CRC64;
     MADKVRESLG AMSTLLSAMK APLPTGTGDG SALPVERDET IASTLSTVIK DVSHLEFDSV
     EKVAKMTIMT KSGAYVDDKE YLMEHLISAA QKLPNDVVGQ KLTNGLITTL WNDLDHPPKA
     FMSDKYQYRS ADGSDNSYLH PRLGAAHEAY ARTVKPSTIQ PGNLPDPAVL FDVLMARDKP
     TEHPNKISSM LFYMASIIIH DLFKTNHRDF RISDTSSYLD LSPLYGSDQS EQDTVRTFKD
     GKLKLDSFAE TRLLSFPPGV GVIMIMFNRF HNYIVEQLAL INENSRFTRP TEDASKDKWV
     KYDNDLFQTG RLITCGLYIN IILVDYVRTI LNLNKTDSDW SLNPRAEFPG QPDLGCGNQV
     SAEFNLVYRW HSAVSDKDDK WTQDLFAKLF PGRKPDEVPQ LEFLKTLGHM EVDLKAQDPV
     ARNFHDIKRN ADGTLPDDEL AKILVESVED CANAFGPRQV PLVMKQIEVL GIRQARAWNL
     ATLNEFRKHF SLKPYSTFEE ITADKEISES LKHLYDHPDN VELYPGLVVE DAKFSMRPGS
     GLCPSYTTSR AILSDATVLV RGDRFYTTSH HPAALTNWGF AEQGSDLKIN HGCVMYKLFM
     KAFPNHFRPD SVWVHFPFTV PSEMKKVLTG LGKAHKYNFD RPTRLPPTKM LFSYDAAKKV
     LFDQDAFKVY WGPKIEFLMG PTAKNFMLAG DTKANTASRD MIEQALYLGK FARAAPTGNE
     KWLLEVRKFY QEHTSMLLQK HSYKLAGTNY VDLIRDVSNI VHVHFCSEIF NLPLKTEDNP
     DGAFTEKQMY LVMAAVFACV FFDVDPEHSF ALRQGAYDAI QAVGKLMEMQ VQALSKLPHM
     SEAVDRIGEW WSGKDRSVLT QYGKHMVERL LQTSGMDVQE LVWAQIIPTA GSMCANQGQF
     FGQVIDWLFS EGREYLPILH EIAVQDTPEA EEKMMRYFLE FSRLHSETGV YRTVAKETIV
     EDMDRRVKLN VGDTVAVNFR SASRDPNIFP DPEKIRLDRP IESYIHLGQG PHQCLGQPMT
     LVAMGAILKT LCKLPNLRPA PVWPGPVDSV KKVVKDFSTL APDVDFKPEW TYHCYLLEGW
     DQYFPFPASL KICYDGPAA
//