ID A0A0F5K0R7_9BURK Unreviewed; 325 AA.
AC A0A0F5K0R7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Dihydrofolate reductase {ECO:0000313|EMBL:KKB63683.1};
GN ORFNames=WM40_10200 {ECO:0000313|EMBL:KKB63683.1};
OS Robbsia andropogonis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Robbsia.
OX NCBI_TaxID=28092 {ECO:0000313|EMBL:KKB63683.1, ECO:0000313|Proteomes:UP000033618};
RN [1] {ECO:0000313|EMBL:KKB63683.1, ECO:0000313|Proteomes:UP000033618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP2807 {ECO:0000313|EMBL:KKB63683.1,
RC ECO:0000313|Proteomes:UP000033618};
RA Lopes-Santos L., Castro D.B., Ottoboni L.M., Park D., Weirc B.S.,
RA Destefano S.A.;
RT "Draft Genome Sequence of Burkholderia andropogonis type strain ICMP2807,
RT isolated from Sorghum bicolor.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:KKB63683.1}.
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DR EMBL; LAQU01000008; KKB63683.1; -; Genomic_DNA.
DR RefSeq; WP_024903890.1; NZ_LAQU01000008.1.
DR AlphaFoldDB; A0A0F5K0R7; -.
DR STRING; 28092.WM40_10200; -.
DR PATRIC; fig|28092.6.peg.2412; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000033618; 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; cd05301; GDH; 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; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000033618}.
FT DOMAIN 24..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 118..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 34897 MW; 8B78476C12C50539 CRC64;
MQTDSSDLPR AYLCRRFPVS IEASLREKYQ LSVNNEDSIL SPAGIARQAQ GVSILFVSAT
ERVDASVIAS LSPTLRTIAT LSVGLDHIDI VAARVHGVSV LHTPDVLNDA CAEIAMLHVL
NTCRRGYEGD KMIRDGAWQG CAPTQMLGKG LVGARLGIFG MGRIGRAIAR RAQAFDMVIH
YHNRSRLPER LEAGAVYHST LDELATVSDV LVIAAPGTPE SRGAINADRI ALLPKGSVVV
NISRGDLVDD TALIAALTSG HLMAAGLDVF ANEPYVDMRY RTLPNVFMTP HIGSATHQTR
EAMGQMLIDG LDQLAAGKRP TNLVV
//
