ID E3E5G2_PAEPS Unreviewed; 1058 AA.
AC E3E5G2;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 29-MAY-2013, entry version 18.
DE SubName: Full=Bifunctional reductase 1;
GN OrderedLocusNames=PPSC2_c3726;
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=886882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2;
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: Heme group (By similarity).
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DR EMBL; CP002213; ADO57681.1; -; Genomic_DNA.
DR RefSeq; YP_003947922.1; NC_014622.1.
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; CEIRFER; -.
DR BioCyc; PPOL886882:GBY1-3823-MONOMER; -.
DR GO; GO:0070330; F:aromatase activity; IEA:InterPro.
DR GO; GO:0009055; F:electron carrier 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 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; 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; Cytochrome_P450; 1.
DR SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 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 Complete proteome; Heme; Iron; Metal-binding.
FT METAL 403 403 Iron (heme axial ligand) (By similarity).
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
//