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Database: UniProt/TrEMBL
Entry: E3E5G2_PAEPS
LinkDB: E3E5G2_PAEPS
Original site: E3E5G2_PAEPS 
ID   E3E5G2_PAEPS            Unreviewed;      1058 AA.
AC   E3E5G2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   26-NOV-2014, entry version 27.
DE   SubName: Full=Bifunctional reductase 1 {ECO:0000313|EMBL:ADO57681.1};
GN   OrderedLocusNames=PPSC2_c3726 {ECO:0000313|EMBL:ADO57681.1};
OS   Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57681.1, ECO:0000313|Proteomes:UP000006868};
RN   [1] {ECO:0000313|EMBL:ADO57681.1, ECO:0000313|Proteomes:UP000006868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC2 {ECO:0000313|EMBL:ADO57681.1,
RC   ECO:0000313|Proteomes:UP000006868};
RX   PubMed=21037012; DOI=10.1128/JB.01234-10;
RA   Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA   Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J.,
RA   Du B.;
RT   "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of
RT   plant growth-promoting Rhizobacterium with broad-spectrum
RT   antimicrobial activity.";
RL   J. Bacteriol. 193:311-312(2011).
CC   -!- COFACTOR:
CC       Note=Heme group. {ECO:0000256|PIRSR:PIRSR000209-1};
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DR   EMBL; CP002213; ADO57681.1; -; Genomic_DNA.
DR   RefSeq; YP_003947922.1; NC_014622.1.
DR   ProteinModelPortal; E3E5G2; -.
DR   EnsemblBacteria; ADO57681; ADO57681; PPSC2_c3726.
DR   GeneID; 9852020; -.
DR   KEGG; ppm:PPSC2_c3726; -.
DR   PATRIC; 42510576; VBIPaePol172748_3561.
DR   HOGENOM; HOG000093545; -.
DR   KO; K14338; -.
DR   OMA; IDYEDYQ; -.
DR   BioCyc; PPOL886882:GBY1-3823-MONOMER; -.
DR   GO; GO:0070330; F:aromatase activity; IEA:InterPro.
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:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   Gene3D; 1.20.990.10; -; 1.
DR   Gene3D; 3.40.50.360; -; 1.
DR   InterPro; IPR023206; Bifunctional_P450_P450_red.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR029039; Flavoprotein-like.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
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   PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
DR   SUPFAM; SSF63380; SSF63380; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000006868};
KW   Heme {ECO:0000256|PIRSR:PIRSR000209-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR000209-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000209-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006868}.
FT   METAL       403    403       Iron (heme axial ligand).
FT                                {ECO:0000256|PIRSR:PIRSR000209-1}.
SQ   SEQUENCE   1058 AA;  119257 MW;  F84D113E0B9BF9BF CRC64;
     MTSTNSIPQP KTYGPLGNLP LIDTHAPVQS LVKLANEHGP IFRMDLPEGT NIYISGHKLV
     ADACDESRFD KQVWAPLQKV RAFAGDGLFT SWTEEPNWRK AHQILLPSFS QRAMKGYHNM
     MLDLAVQLVQ KWSRLNPDES VEVPEDMTRL TLDTIGLCGF NYRFNSFYRD QPHPFVTSMT
     RALDEAMGQL QRLNLQNKLM LSKKKQFKHD IETMFSLVDS IIQERKTVGN QGEEDLLARM
     LEGKDPETGE TLDDENIRYQ IITFLIAGHE TTSGLLSFAI YYLLKNPRTL TKAYEEVDRV
     LTDSLPSYTQ VRELKYIRMI LNEALRLWPT APAFSLFAKE DTLLDGTYPL KKGDSVNVLI
     PKLHRDTEAW GEDVEEFRPE RFEDPSAIPQ DAYKPFGNGQ RACIGQQFAL QEATLVLGMV
     LKHFELIDHT HYELKVKETL TLKPGGFTIQ VRPRSTQTTI MLPGAAQELH EKEEQKVAAP
     HAEKHDTSLL SLYGSNLGTA EGLAGELADL GRNWGFKSSI ATLNDHVDHL PKEGVVLITT
     ATYNGHPPDN ADAFVEWLKE VDEGQLAGIR YAVFGCGDRN WASTYQRIPR MIDELMTAKG
     AKRLYDRGEG DASGDFEKDW EVWNHGLWPE LLNAFGIEHS DTEPQDTSSL SIEFVSDVLS
     APLAANYEAA TAVVTVNREL HAAESERSTR HLEIQLPTGL SYREGDHLGV LPRNPALLVN
     RVMQRFKLQD QNYIVLRGSD RDAAHLPLDR PVSVGDLLTL SVELQEPATR AQLRQLASFT
     VCPPHKKEIE ALLEDTTFDQ EIRKKRVTML DILEKYPACE LPFENFISLL PPLKPRYYSI
     SSSPLESENS ASITVSVVRG PARSGQGEYL GIASNYLAQL QPDDPVVIFV RKPQSGFRLP
     EDPTVPVIMV GPGTGVAPFR GFLQTRHVLK ERGEQLGEAH LYYGCRDPKL DYLYKQELQT
     WEQEGIVTVH TAFSRLPGQP KRYVQHVMNE GADTLIHLLD EGAHLYVCGD GSRMAPDVEN
     TLCAAYADIH HTSKEEAQQW LDHLQQEKRY AKDVWTGI
//
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