(data stored in ACNUC1104 zone)

SWISSPROT: 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   11-DEC-2019, entry version 142.
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}.
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; NC_003888.3.
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   SMR; P16544; -.
DR   STRING; 100226.SCO5086; -.
DR   DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DR   DrugBank; DB07715; Emodin.
DR   DrugBank; DB01942; Formic acid.
DR   PRIDE; P16544; -.
DR   EnsemblBacteria; CAC44199; CAC44199; CAC44199.
DR   GeneID; 1100527; -.
DR   KEGG; sco:SCO5086; -.
DR   PATRIC; fig|100226.15.peg.5166; -.
DR   eggNOG; ENOG4105DTD; Bacteria.
DR   eggNOG; ENOG410XPTP; LUCA.
DR   InParanoid; P16544; -.
DR   KO; K12420; -.
DR   OMA; ASHAYCG; -.
DR   PhylomeDB; P16544; -.
DR   UniPathway; UPA00173; -.
DR   EvolutionaryTrace; P16544; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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;
DR   PRODOM; P16544.
DR   SWISS-2DPAGE; P16544.
KW   3D-structure; Antibiotic biosynthesis; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..261
FT                   /note="Putative ketoacyl reductase"
FT                   /id="PRO_0000054447"
FT   NP_BIND         11..39
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15458634,
FT                   ECO:0000269|PubMed:15544323"
FT   ACT_SITE        157
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         63
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15458634,
FT                   ECO:0000269|PubMed:15544323"
FT   BINDING         144
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /note="NADP"
FT                   /evidence="ECO:0000269|PubMed:15458634,
FT                   ECO:0000269|PubMed:15544323"
FT   STRAND          8..12
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           17..28
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          32..38
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           40..52
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          57..61
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           67..80
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          85..89
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           99..101
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           104..114
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           116..126
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   TURN            127..129
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           131..134
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          136..142
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           145..147
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           155..175
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   TURN            176..178
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          179..187
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          189..192
FT                   /evidence="ECO:0000244|PDB:3CSD"
FT   HELIX           193..206
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           210..220
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           229..240
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   HELIX           242..244
FT                   /evidence="ECO:0000244|PDB:2RHC"
FT   STRAND          251..255
FT                   /evidence="ECO:0000244|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
//

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