ID K1WNN5_MARBU Unreviewed; 1787 AA.
AC K1WNN5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN ORFNames=MBM_08168 {ECO:0000313|EMBL:EKD13967.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD13967.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD13967.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD13967.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; JH921448; EKD13967.1; -; Genomic_DNA.
DR RefSeq; XP_007296057.1; XM_007295995.1.
DR STRING; 1072389.K1WNN5; -.
DR GeneID; 18764103; -.
DR KEGG; mbe:MBM_08168; -.
DR eggNOG; KOG0157; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_238419_0_0_1; -.
DR InParanoid; K1WNN5; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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 CDD; cd06206; bifunctional_CYPOR; 1.
DR CDD; cd11068; CYP120A1; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF127; BIFUNCTIONAL CYTOCHROME P450/NADPH--P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 493..634
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 665..895
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1722..1778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1240..1261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1749
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1756..1778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1787 AA; 196848 MW; 444D32B4EE4E6236 CRC64;
MTTPIPGPPG LPFVGNINDL DPEGSIASLS RLAETYGKPP RSIFKLTLGG NERLFISTHE
LMDEVCDEKR FTKMVSGALE QVRNGVSDGL FTAHTHEHNW EVAHRVLMPA FGPINIRSMF
DEMHDVASQL VVKWARFGPR QRINVTDDFT RLTLDSIALC AMDTRFNSFY HEELNPFVDA
MLGLLQESEA RSRRPAVANF FYRSAQQKYD ADIALLKSVA AEVVKERRSA PNDKKDLLNT
MINGRDPKTG EGLTEERHET TSGLISFLFY FLVKNPAVYQ TAQRQVDEVI GRGPITVDHM
SKLPYIEACL RETLRLTPTA PAFTLQARTD TPDEHLILGG KYEIKKGQSI VALLGKIHTD
PAVFGEDAQS FKPERMLAEE FSKLPKNAWK PFGNGLRSCI GRPFAWQEVI LTTAMLLQTF
NFRFEDPSYQ LAIKQTLTLK PKDLFMHASL REHIDAMHIE KMLHVQSSMQ SLSTEKNVKM
HQASAAARPK KPMSILYGSN AGTCEALAQS LARAASGRGY AAQVEPLDSA VDRVPKAQPV
VLISSSYEGQ PPDNAAHFFE WLQSLEGNDK LKGVKYAVFG CGNHDWVSTF HRVPKLLNSG
FEENGASKIT EMGLGDVAAG DIFNDFDKWQ DEYLWSALGG DAEAEEETSL ELEIDTGNRS
SRLRQDVKEA VVLSNEILTK PGVPEKRHIT LNLPTGMTYK AGDYIAVLPM NNASTVRRVL
KWAHLPWDTM LTIKSGASTT LPTGHPISAM DVLTMYVELS QPATRKNIAR IAASSPDEAV
RAKILDLAAK DFEEEILNKR KSPLDILEEY PSAVLPLGDF LAMLPPMRIR QYSISSSPLA
DPTIATLTWA VLDTPSKAAG GKRFLGVASN YMSGLEEGDR IHVAVKPSHG LFHPPADLEG
TPVIMFCAGT GLAPFRGFVQ ERAIQFQGGR KLAPAYLFIG CAHPEKDCLF SEELRHWEEA
GVVKTFYAYS QCSESSKGCR YVQDRLWEER VEMVKAFEEG AKLFVCGSSR VGEGVAAMTK
KIYMEAAEAL GKPKTDEEVE QWWAGIKGER SRREAFHAEN SIYYYHRISN HIRTQIDNHA
GVYRYPRIHA SPTTTAVHDR SPRGRRGYIM SSGRGDNHGH GRDLKIKASL EAISLARATT
DGLSWSRRPP RRLSRARSGP LQRMRSCSRC VRISWRASNM IPWLWSHGRL SGRPSPPGWG
TSGTVDRRRP VLIAGAESRG LRRGLFLRRM LLACEMDKGQ HQLSSNTSPG SNFNESLDAP
TPTGSLKRKP SRLDCRESTL SICEDNIGVQ ARDDHPSKRI RLEPEYARHC SGEARTHVSS
SSARMLPIQS DRPEDGEFGQ SIGSPTDASR NSSRADSSES RETAATSTSS HGTVVSSFSA
ADKPGGSALP IPDQALSSEE ITSEKEPDLQ HSMVNELPSF QAPVSGALGH PVNTGPRLLS
NTSIPTVMSA GPSVNPPPLS QTSGPSLASE STPGSEREVI SRKANTYQAQ IDSLNRDVTA
RLQNICHIDQ RVEAITKKQR DLHHERDELI RQTIMEIEAS KDVELEAMER SSDELKKRKK
SFGHIQALIN GMTSRIESNA SAETAAQVKP FPRRGPLRVV VLDPHGTRDV DAGIGQLLLG
RVHRVSHSRR RQPQLAGPLA GRDPTHARRG EEAALALRAA GQVRHDVVPV VVGRALLAPG
PACGGAATGG EENLEGGYVG GHDGDLELDA GDDDDLAEGV REVGELLELE EDSEAQDGDD
DDDAAQGDDG EELQPLAQGE LDHPEGLDRE DEDHDVHEDV LAVFKNR
//