ID A0A0F4J7G4_9ACTN Unreviewed; 315 AA.
AC A0A0F4J7G4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:KJY28896.1};
GN ORFNames=VR44_24245 {ECO:0000313|EMBL:KJY28896.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY28896.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY28896.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY28896.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJY28896.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JZWV01000695; KJY28896.1; -; Genomic_DNA.
DR RefSeq; WP_045949702.1; NZ_JZWV01000695.1.
DR AlphaFoldDB; A0A0F4J7G4; -.
DR STRING; 68223.GCA_002028425_05003; -.
DR PATRIC; fig|68223.7.peg.829; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000033551; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12166; 2-Hacid_dh_7; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 53..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..280
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 33642 MW; 8A0ACEF2CD15A877 CRC64;
MTATTADVWL PFPPGEIDGL PDSFSYRQWD GEEEFPADPA ACVFYVTPYM KSQEVTLRPL
PAMPGLRVVQ TLTAGIDHVL PGLGHLRPGV RLCNARGVHE ASTAELALTL TLASLRGIPG
MVRGQDREDW RGGFYEALAD KSVLIVGYGA IGAAIEDRLL PFECGRITRV ARSARTAPHG
PVHALGDLPV LLPEADVVIL STPLTEDTRG LAGAAFLGRM KDGALLVNVS RGPVADTKSL
LAELESGRLR AALDVTDPEP LPPGHPLWHA PNVLITPHVG GSSSAFEPRA KRLVARQLTR
FAAGEPVENT VLITD
//
