ID Q9RK40_STRCO Unreviewed; 189 AA.
AC Q9RK40;
DT 01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:CAB56144.1};
GN OrderedLocusNames=SCO0339 {ECO:0000313|EMBL:CAB56144.1};
GN ORFNames=SCF12.18 {ECO:0000313|EMBL:CAB56144.1};
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:CAB56144.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAB56144.1, 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).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854}.
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DR EMBL; AL939105; CAB56144.1; -; Genomic_DNA.
DR RefSeq; NP_624663.1; NC_003888.3.
DR AlphaFoldDB; Q9RK40; -.
DR STRING; 100226.gene:17757922; -.
DR PaxDb; 100226-SCO0339; -.
DR PATRIC; fig|100226.15.peg.313; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_4_11; -.
DR InParanoid; Q9RK40; -.
DR OrthoDB; 117809at2; -.
DR PhylomeDB; Q9RK40; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT DOMAIN 2..145
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 189 AA; 20551 MW; 7EF59408E5AFE26A CRC64;
MLGLLSFGAI ARLVAERARA FGVEVWAHDP FVDESEIRAA RVRPVSFDDL VEGADHLVVQ
APLTPQTHHT FDRATLRRMK PTAVLVNTAR GPIVEDAALY EALTGGWIAG AALDDIEEEP
AKQRDWRPNN PLFELPNVVV TPHAAYYSEE AIGTVRTIAA EEAVRVLTGE PARYPVNEPA
AGSHRAEGA
//
