ID A0A194SB45_RHOGW Unreviewed; 1112 AA.
AC A0A194SB45;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Heme peroxidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=RHOBADRAFT_51621 {ECO:0000313|EMBL:KPV77814.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV77814.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV77814.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV77814.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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DR EMBL; KQ474074; KPV77814.1; -; Genomic_DNA.
DR RefSeq; XP_018273863.1; XM_018415934.1.
DR AlphaFoldDB; A0A194SB45; -.
DR STRING; 578459.A0A194SB45; -.
DR GeneID; 28976382; -.
DR OMA; INEWGRW; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000053890; 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:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProt.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
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; 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; 1.
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:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890}.
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406
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 1112 AA; 123032 MW; 3521BE0A48790024 CRC64;
MPTTTVAPVT LGQPQEEYQQ PGSSSSSSTP PSPSSRRGVL GAARSVVSTT LSMAQAALAD
TAPVEAAHHA AHESKHAFYS LLDSLKENTL AKDAIGMIQV GQSQVAGLDD RKFLLEEIVT
VLAKLPPGAP IGTTVTNALL RVLWDDIPKP PATLVGDYRY READGSKNNI FLHDLGKARM
PYARSVPNLH AFPAQLPDHG VVWDSLLKRD KFVPHPSGIS SLLFGFAQLI VHSIFQTDPR
NGEVNEASSY LDLSPIYGNN AAEQATVRSG VQGLLHPDAV ANKRIFLVSP SCVALAILFS
RNHNDIAQRL FAVNEQGRYA EWDSLDDEAK KRQDNDLFNT ARNVNCGHFV NVIFQDYIRV
ILNLNKTDST WSLVPTGEIK SLLGGRLARG EGNHVSVEFN ILYRWHASSS EKDTEWLEGL
MRQYNGGKPF SEMTTEDFQV AARKALDDMK GGPETWTFLG LKRTESGAFR DEDIVKVLLE
ATDNVASAFK ARAIPEVMRA IDLLGMEAAR KTWRCCSMNE FREFLGLKKY SSFEEWNPDK
DVARAAEKLY QHVDHLELYP GLMAEEPKPS MNGSGLAPGY SISRAILSDA AALVRGDRFF
TTDYNAGNLT SAMWEDLKPE LDNGSFGGVI GKLLMRHFSA HFTYNSIYAL FPFSTPHTTK
ANLEHLGIAS EYDYRRPSTP PAWKRLTSYA DLKQVLDDKG QRLSSVYGPA LDELTQAKQP
SILSYLRLGD SSKGRDSAAD ILELALFPPH WAQTALVDLG DVTKRTLEEH KFAYGKDKFR
IDVVGDVAVP VVVEYLADLF GIPLKSKSNP LGLFTVDGLY DALTDLYAFV YLDFDPTVAF
KLRDRARKHS ELLRGIILMR LGQTEFIPDL AGDLLRDFKR VLTGKGSGGY VLSDRSRKLY
KRTTQSDRPI DELAGVLLTA LIRLVQVVPQ VANVVDFFLE PSRHKDLQHV CHAAQQQVGM
ANDSLIIKYV LEAMRLQPSV TGIARRVKGD ADKKPNELLW VDLVSCGRDD KVFSEPDKVD
VTRDAKLYQP LDKATSVVNQ EGESYNVPLV SGIVRELLTV NSPSRPSGSE GQLGVVEGPL
GLRVYARDET RQRPRAFPGR MIVAFEGVKG KR
//
