GenomeNet

Database: UniProt
Entry: M9LZV1_PSEA3
LinkDB: M9LZV1_PSEA3
Original site: M9LZV1_PSEA3 
ID   M9LZV1_PSEA3            Unreviewed;      1262 AA.
AC   M9LZV1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   SubName: Full=NADP/FAD dependent oxidoreductase {ECO:0000313|EMBL:GAC72985.1};
GN   ORFNames=PANT_8d00010 {ECO:0000313|EMBL:GAC72985.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC72985.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; DF196774; GAC72985.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LZV1; -.
DR   STRING; 1151754.M9LZV1; -.
DR   OrthoDB; 5488444at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06207; CyPoR_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 3.40.920.10; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR003097; CysJ-like_FAD-binding.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR002869; Pyrv_flavodox_OxRed_cen.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR19384:SF109; SULFITE REDUCTASE [NADPH] FLAVOPROTEIN COMPONENT; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF53323; Pyruvate-ferredoxin oxidoreductase, PFOR, domain III; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT   DOMAIN          849..1080
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          36..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1262 AA;  133752 MW;  B3B9103F40FA2F44 CRC64;
     MAATSSQSLY QSAAIFAGGL AIGAGTLALS RAAFAPAHKP NKSIKRKVSD AKLRSAPSAP
     AAAAAAAAAP TQAKADTTPS TGNGRVDPPA SQQLDQVDAK GAGPAAPAKE QLPGHVAPNG
     VDATAGGQKL TGLVNAQPVN AAVPEPAPAN RAQHLDARMD LGLVQGPTEA EIAAKLAAQS
     WLLGIPSATL TSTGAIDSIA YANSTAVFSY ESETNGGFGS FSENEAKLAA EKGWFKGRAS
     VFKMQTRSGA GNAIVGYLNA KGGSSSTEPA KVVTALTNAA GFAAMAPTLA SYNGSDNAKL
     VLQVSAASHS TDGADELSIT NDYASVLAAA ATLGDAYEVV LSATRQEAVD FAQYAYQSNK
     NVVHVFDGAF AGREVGTLAI PTKGQKVDVP EPFLFTGSPK AKTVLVVPNG SHSQAARAVL
     VTLPPAVRHN VALLSVRTLA SWDETDLRKA LPKSVESLHV LEQVLGGAAS GQLYDDIVSS
     VFGTEFSGSD VPSHVFPVAL AAGQDLTAAE LHKLLETLGD ARKAALKVQD VLDEADESHA
     DLLALSGASV VTFFDTETSP TAPLAQLTAR AIRDRGADTQ LNARLLSRFD NFEASGIVRS
     DIILSSRPES AADAPIVLAA EENAAKVLVV SDPATTLKSY APFQSLVRGG TVIFNTPGWE
     VAELDSKLRA EDKRVLAQKS ARLLLVDAAA VVEKLNVKTA NASGGKAKVG DNVVPAEIAA
     AVLLVAVLRV QLNTSGAALA AFLKRVLGTA PVGIDGVEGL VSAAESAIQL HAFSDDEWSK
     AQPISEAEEN APLRPTQIRY NGFGPNPEAA TVGTELAPVR TTWAQSAWQH LFSEAYDTAA
     DALRPDLPEQ TWVVEVTENR RLTPVDYDRN VFHMELSTKG TDLKYEVGEA LGVHGWNDAE
     EVADIIRWAG FDADEIVNAP SLTQAGKHEA RTVFQTLQQN LDIFGKPPKR FYEELAKLAT
     NRDEARWLRF ISSAEGSFTF KKLSEIETLT YADVLRMFPS ARLPIDQLLT LVEPIKPRHY
     SIASAQSAVG ESIHLLIVTV DWKTPSGSPR FGQCTRYLSE LKPGAKVTVS LKPSVMKLPP
     IDTQPIIMAG LGTGAAPFRA FIQARAHKKA QGIEVGPLVY YFGSRYRSAE YLYGEELEAY
     TQDGVIQHMG LAFSRDTSKK VYIQHKILED GDLLTQYLGP EIEKLEAAGG KAEVVLQDGL
     INDEDIEDGK KGYFFVCGPT WPVPDIHEAL VGAFVKKGLT KDQAEKKMEA LKEDERYVLE
     VY
//
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