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Database: UniProt
Entry: K1WNN5_MARBU
LinkDB: K1WNN5_MARBU
Original site: K1WNN5_MARBU 
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
//
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