ID A0A2H3IIA5_9EURO Unreviewed; 672 AA.
AC A0A2H3IIA5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Heme peroxidase {ECO:0000313|EMBL:PCH02442.1};
GN ORFNames=PENO1_037610 {ECO:0000313|EMBL:PCH02442.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCH02442.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCH02442.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCH02442.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
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:PCH02442.1}.
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DR EMBL; NPFK01000083; PCH02442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3IIA5; -.
DR STRING; 290292.A0A2H3IIA5; -.
DR OrthoDB; 1086441at2759; -.
DR Proteomes; UP000218381; 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: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 InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022767};
KW Oxidoreductase {ECO:0000313|EMBL:PCH02442.1};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Peroxidase {ECO:0000313|EMBL:PCH02442.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381}.
SQ SEQUENCE 672 AA; 76361 MW; A67082830DDE3D3A CRC64;
MEPPNFQPTF LERVCIKIFL FINRYVPWHR LPGFLGALNL NFLRIELRAY NLHDGYSSGD
AQGNTVNHPL EDERFISARN SDGRFNSAEL PLMGCAGMRF GRNFPRKYTQ KPSKEELWTP
NPRLVSERFM ARKSRGYIPA KSLNLLAAAW IQFQIHDWFQ HESVRIEALS SDAVVSEEIL
DIPLPSGDTW PYGRMILHRT KPDETLDESD IQCPGYKNQN TAWWDGSQIY GSSEATTQSL
RTKDQDGKLS LSRNGTVTFL PRDKTGNPRT GFNDNWWTGM EMLHTLFAME HNAICDMLRT
AYPDWTGDQI FDKARLVNCA LMAKIHTVEW TPAILAHPAL EIGMNANWWG IAGETLTKMV
GRISKTSETI SGIPGSGVNH FGIPYSLTEE FVSVYRMHPL IPDEIAFFSA TDGRHKSTIP
IVDTIFGGAQ RPFDHGISFA DSFYSFGINY PGAITNNNYP DFMRNLSTPD GQHRDLGTVD
ILRDRERGVP RYNQFRRLLR MSVPKTFEEL TGNNKELAQE LREVYGDIEL VDTLVGSHSE
PVPEGFGFSD TAFRIFILMA SRRLNSDRFI AGQWNTNTYT EEGFHWVQNT GMKDVLLRHF
PELKGGTVYV TARSASRYEG AIEKIKDQTR GKKTEGVLKS MILDLADLTT IKPAVEKFLQ
QETRLDVLVN NT
//
