HYDL_STRHA
ID HYDL_STRHA Reviewed; 555 AA.
AC Q05355;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Putative polyketide hydroxylase;
DE EC=1.14.13.-;
GN Name=schC;
OS Streptomyces halstedii.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1944;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRRL 2381;
RX PubMed=8253693; DOI=10.1128/jb.175.24.8043-8048.1993;
RA Blanco G., Pereda A., Brian P., Mendez C., Chater K.F., Salas J.A.;
RT "A hydroxylase-like gene product contributes to synthesis of a polyketide
RT spore pigment in Streptomyces halstedii.";
RL J. Bacteriol. 175:8043-8048(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75.
RC STRAIN=NRRL 2381;
RX PubMed=8344517; DOI=10.1016/0378-1119(93)90352-4;
RA Blanco G., Brian P., Pereda A., Mendez C., Salas J.A., Chater K.F.;
RT "Hybridization and DNA sequence analyses suggest an early evolutionary
RT divergence of related biosynthetic gene sets encoding polyketide
RT antibiotics and spore pigments in Streptomyces spp.";
RL Gene 130:107-116(1993).
CC -!- FUNCTION: Involved in developmentally regulated synthesis of a compound
CC biosynthetically related to polyketide antibiotics which is essential
CC for spore color in Streptomyces halstedii.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; L05390; AAA02830.2; -; Genomic_DNA.
DR PIR; B49918; B49918.
DR AlphaFoldDB; Q05355; -.
DR SMR; Q05355; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase.
FT CHAIN 1..555
FT /note="Putative polyketide hydroxylase"
FT /id="PRO_0000214042"
FT REGION 366..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 16..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 303..313
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 59379 MW; 23CCF55BF6738D58 CRC64;
MNARADRAGD TVHRVPVLVV GGSLVGLSTS VFLGRLGVRH MLVERHAGTS VHPRGRGNNV
RTMEVYRAAG VEQGIRRAAA TLAGNHGILQ TPSLVGDEGE WLLRDIDPGG GLARFSPSSW
CLCSQNDLEP VLLDHAVELG GEIRFSTELQ SFEQDPAGVT AVIKSRRSGE HTTVRADYLV
AADGPRSPVR EQLGIGQSGP GDLFHNVSVT FRSRRLAEFV GDRHFIVCYL TNPEADGALL
PVDNRENWVF HAPWYPRAAR PLEDFTDERC ADHIRRAVGV PDLDVEITGK APWHAAQRVA
RQYRAGRVFL AGDSAHEMSP TGAFGSNTGI QDAHNLAWKL AAVLGGWAGD GLLDTYDAER
RPVAEATTAR AAARSAEHSH PGFAPPPGTS GGPQGGILNV ALGYRYPGGA VLGADPATPV
VPEALTLAGE PGSRAPHLWM SRRGERLSTL DLYERSPVLL SDADAGAPDA WHESAVRLAE
ELSVPLTSYR VGRSAGADLT PEDDVNWTAR HGTPPGGAVL VRPDGFVAWR SQEPVPAEET
EPTLRHVLTT VLSLG