ID Q9KYM4_STRCO Unreviewed; 263 AA.
AC Q9KYM4;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:CAB92206.1};
GN Name=SC9H11.17c {ECO:0000313|EMBL:CAB92206.1};
GN OrderedLocusNames=SCO7363 {ECO:0000313|EMBL:CAB92206.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB92206.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB92206.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
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., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., 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 [2] {ECO:0007829|PDB:5H5X}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH NADH.
RA Li M., Kong X.-D., Zhou J., Yu H.-L., Zhang Z.-J., Xu J.-H.;
RT "Crystal structure of NADH bound carbonyl reductase from Streptomyces
RT coelicolor.";
RL Submitted (NOV-2016) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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DR EMBL; AL939131; CAB92206.1; -; Genomic_DNA.
DR RefSeq; NP_631416.1; NC_003888.3.
DR RefSeq; WP_003971780.1; NZ_VNID01000005.1.
DR PDB; 5H5X; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-263.
DR PDBsum; 5H5X; -.
DR AlphaFoldDB; Q9KYM4; -.
DR SMR; Q9KYM4; -.
DR STRING; 100226.gene:17765023; -.
DR PaxDb; 100226-SCO7363; -.
DR PATRIC; fig|100226.15.peg.7466; -.
DR eggNOG; COG1028; Bacteria.
DR HOGENOM; CLU_010194_1_0_11; -.
DR InParanoid; Q9KYM4; -.
DR OrthoDB; 7064009at2; -.
DR PhylomeDB; Q9KYM4; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR CDD; cd05233; SDR_c; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR24321:SF11; BLR0893 PROTEIN; 1.
DR PANTHER; PTHR24321; DEHYDROGENASES, SHORT CHAIN; 1.
DR Pfam; PF13561; adh_short_C2; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5H5X}; Metal-binding {ECO:0007829|PDB:5H5X};
KW Nucleotide-binding {ECO:0007829|PDB:5H5X};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT BINDING 29
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 31
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 50
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 76
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 77
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 103
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 127
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 170
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 174
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 203
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 205
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0007829|PDB:5H5X"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:5H5X"
SQ SEQUENCE 263 AA; 26370 MW; 5C61DEA606ACBBA2 CRC64;
MSTTGTTPAT TGYAAEFAGR TALVTGAASG IGLATARRLG AGGARVVVAD FNAEGAEKAA
AELRAGGVEA AAVELDVTRP ESVEAAVGFA VDTFGSLDLA VNNAGIGGPS APTGEYDVAA
YQRVVRTNLD GVFYSMRYEL PAIEAAGKGG SIVNVASILG SVGFAGSPAY VAAKHGVVGL
TKAAAAEYAA RGIRINAVGP GFIDTPLLKT MDEAAYKGLV ALHPAGRLGR SEEVAELIAF
LLSDRASFVA GSYHLVDGAY TAV
//
