ACT3_STRCO
ID ACT3_STRCO Reviewed; 261 AA.
AC P16544;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative ketoacyl reductase;
DE EC=1.3.1.-;
GN Name=actIII; OrderedLocusNames=SCO5086; ORFNames=SCBAC28G1.12c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2469622; DOI=10.1016/0378-1119(88)90165-5;
RA Hallam S., Malpartida F., Hopwood D.;
RT "Nucleotide sequence, transcription and deduced function of a gene involved
RT in polyketide antibiotic synthesis in Streptomyces coelicolor.";
RL Gene 74:305-320(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADPH.
RX PubMed=15544323; DOI=10.1021/bi048133a;
RA Korman T.P., Hill J.A., Vu T.N., Tsai S.C.;
RT "Structural analysis of actinorhodin polyketide ketoreductase: cofactor
RT binding and substrate specificity.";
RL Biochemistry 43:14529-14538(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADPH, AND SUBUNIT.
RX PubMed=15458634; DOI=10.1016/j.str.2004.08.002;
RA Hadfield A.T., Limpkin C., Teartasin W., Simpson T.J., Crosby J.,
RA Crump M.P.;
RT "The crystal structure of the actIII actinorhodin polyketide reductase:
RT proposed mechanism for ACP and polyketide binding.";
RL Structure 12:1865-1875(2004).
CC -!- PATHWAY: Antibiotic biosynthesis; actinorhodin biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15458634,
CC ECO:0000269|PubMed:15544323}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; M19536; AAA26688.1; -; Genomic_DNA.
DR EMBL; AL939122; CAC44199.1; -; Genomic_DNA.
DR PIR; JS0108; A28788.
DR RefSeq; NP_629236.1; NC_003888.3.
DR RefSeq; WP_003973892.1; NZ_VNID01000008.1.
DR PDB; 1W4Z; X-ray; 2.50 A; A/B=1-261.
DR PDB; 1X7G; X-ray; 2.30 A; A/B=1-261.
DR PDB; 1X7H; X-ray; 2.30 A; A/B=1-261.
DR PDB; 1XR3; X-ray; 2.71 A; A/B=1-261.
DR PDB; 2RH4; X-ray; 2.30 A; A/B=1-261.
DR PDB; 2RHC; X-ray; 2.10 A; A/B=1-261.
DR PDB; 2RHR; X-ray; 2.50 A; A/B=1-261.
DR PDB; 3CSD; X-ray; 2.29 A; A/B=1-261.
DR PDB; 3QRW; X-ray; 2.79 A; A/B=1-261.
DR PDB; 3RI3; X-ray; 2.29 A; A/B=1-261.
DR PDB; 4DBZ; X-ray; 2.64 A; A/B=1-261.
DR PDB; 4DC0; X-ray; 2.81 A; A/B=1-261.
DR PDB; 4DC1; X-ray; 2.82 A; A/B=1-261.
DR PDBsum; 1W4Z; -.
DR PDBsum; 1X7G; -.
DR PDBsum; 1X7H; -.
DR PDBsum; 1XR3; -.
DR PDBsum; 2RH4; -.
DR PDBsum; 2RHC; -.
DR PDBsum; 2RHR; -.
DR PDBsum; 3CSD; -.
DR PDBsum; 3QRW; -.
DR PDBsum; 3RI3; -.
DR PDBsum; 4DBZ; -.
DR PDBsum; 4DC0; -.
DR PDBsum; 4DC1; -.
DR AlphaFoldDB; P16544; -.
DR SMR; P16544; -.
DR STRING; 100226.SCO5086; -.
DR DrugBank; DB07715; Emodin.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR GeneID; 1100527; -.
DR KEGG; sco:SCO5086; -.
DR PATRIC; fig|100226.15.peg.5166; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_11; -.
DR InParanoid; P16544; -.
DR OMA; CLCPSVV; -.
DR PhylomeDB; P16544; -.
DR UniPathway; UPA00173; -.
DR EvolutionaryTrace; P16544; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..261
FT /note="Putative ketoacyl reductase"
FT /id="PRO_0000054447"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 11..39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15458634,
FT ECO:0000269|PubMed:15544323"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15458634,
FT ECO:0000269|PubMed:15544323"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15458634,
FT ECO:0000269|PubMed:15544323"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:2RHC"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 136..142
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 155..175
FT /evidence="ECO:0007829|PDB:2RHC"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3CSD"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 229..240
FT /evidence="ECO:0007829|PDB:2RHC"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2RHC"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:2RHC"
SQ SEQUENCE 261 AA; 27265 MW; B87C83F45A88B7A9 CRC64;
MATQDSEVAL VTGATSGIGL EIARRLGKEG LRVFVCARGE EGLRTTLKEL REAGVEADGR
TCDVRSVPEI EALVAAVVER YGPVDVLVNN AGRPGGGATA ELADELWLDV VETNLTGVFR
VTKQVLKAGG MLERGTGRIV NIASTGGKQG VVHAAPYSAS KHGVVGFTKA LGLELARTGI
TVNAVCPGFV ETPMAASVRE HYSDIWEVST EEAFDRITAR VPIGRYVQPS EVAEMVAYLI
GPGAAAVTAQ ALNVCGGLGN Y
