ID S7QAZ7_GLOTA Unreviewed; 1046 AA.
AC S7QAZ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Linoleate diol synthase {ECO:0000313|EMBL:EPQ56503.1};
GN ORFNames=GLOTRDRAFT_138220 {ECO:0000313|EMBL:EPQ56503.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ56503.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ56503.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ56503.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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DR EMBL; KB469300; EPQ56503.1; -; Genomic_DNA.
DR RefSeq; XP_007865222.1; XM_007867031.1.
DR AlphaFoldDB; S7QAZ7; -.
DR GeneID; 19303928; -.
DR KEGG; gtr:GLOTRDRAFT_138220; -.
DR eggNOG; KOG2408; Eukaryota.
DR HOGENOM; CLU_002329_0_0_1; -.
DR OMA; RHYTIDY; -.
DR OrthoDB; 3322316at2759; -.
DR Proteomes; UP000030669; 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; 2.
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:0000256|ARBA:ARBA00022964};
KW Reference proteome {ECO:0000313|Proteomes:UP000030669}.
FT BINDING 362
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 1046 AA; 117700 MW; 18080FF8CC291D1E CRC64;
MSSILQTVSA TAVRAKDDAE RVVEEFRAKI KQDISFIPDA STLGAVVDAI RHNDAIDDRK
MLLEHVLVLL SRLPQGDLLK KLQDATVELL YLDLPHPPVT YIGSEHAFRT ADGSYNNIDN
PKLGQAGTPY SRSVQDIHLL PTRVLPDPGL VFDVLLKRDG FVKHPAGLSS LFFSFAALVI
HSIFRTSHQN YDINETSSYV DLAPLYGNNQ DEQNKVRVRD GRGLLHPDVF AENRLLLLPP
ATSVLLVLFN RNHNYIARKL LQINERGWYI DPDTIDPVDT EKNAKLLQQE EDIFQTARLV
NASWFASVVM SDYFSNILGL VRDGNTWVLN PFEDIRKSDH SLFERGRGNA CSVEFNCLYR
WHATMSVADE QYTQRVFSQV FPDKPMDQVT AADFKEVAKK QNDMDPDCSH WTFGGLQRQK
DGTFRDEDLA NFLRNSTEQP AAAFRARGTP EVMRLNEIMG ITQSRAWGCC SLNDFRKFLG
LKPYSSFLEW NPDPTIAAVA EKLYHSIDNL ELYVGLQAEE AKPVVEGAGL CPGYTISRAI
LADAIALTRG DRFFTADYTP YALTTWGFND CQRDPNGPGF GSMLGRLFLR TLGDQCRPNS
TYTWFPLMTP ESMKDVLTNL GKLNVYEFVR PSTQRPLVVI DDYRIVKEIL NNDNFVVVGV
DRAAPFIKGE GFFIASSDPE QGRREQREFL RFLAGTPELV QAVTKYFNRK TVELIRTNTY
GNVGSNTKNI NIVRDVVRYA PVHWVATELA GIPIRSKDHP DAPYTEQQLY DIVTGIYEYL
FLDIDPAKEL TLQDTVGKQM KELLGHIHSG LSRQGSLLSG IWDTISSIFT GQSNTDKGTF
AERFSTSGWS QDKMANTILA VLIGSTVELS QTLTHVINTY LDEKHASTIQ PYSSTWDATA
ESVVQAFARE AIRLDPPFAG VYRDCRRGKS IGTLSVQAKD RVFLDMEKAH KNDAVFKHSG
EVNQNRPKES YLIADGSTNC LGEELTLKII AEMLQVVFTL GNVRRAPGNS GVLQRHRNEA
NQAARWEYLK VGGVTFWPDS MVLQYE
//
