ID A0A2A9DTB1_9MICO Unreviewed; 323 AA.
AC A0A2A9DTB1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Lactate dehydrogenase-like 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:PFG29824.1};
GN ORFNames=ATJ78_0739 {ECO:0000313|EMBL:PFG29824.1};
OS Microbacterium agarici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=630514 {ECO:0000313|EMBL:PFG29824.1, ECO:0000313|Proteomes:UP000221369};
RN [1] {ECO:0000313|EMBL:PFG29824.1, ECO:0000313|Proteomes:UP000221369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21798 {ECO:0000313|EMBL:PFG29824.1,
RC ECO:0000313|Proteomes:UP000221369};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG29824.1}.
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DR EMBL; PDJE01000001; PFG29824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9DTB1; -.
DR Proteomes; UP000221369; 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 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; 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; 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; 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 ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000221369}.
FT DOMAIN 18..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 323 AA; 34707 MW; F39C443039105338 CRC64;
MTELNVLVLN DAEGLLASSE GIRRMREHAN VRVVSISLDD IPDAELADVQ VLMAVRERSK
LGAAELDRLP KLELVLQTGG HAYHLDGAHA TARGIPVTLG RRGQGPRAAV PELTFALAIG
ALRHIGTAGE SMRAGKWEPF LGRTLSGRTL GILGYGRHGK TVARLAKAFG MDVLVWSRTD
HDPDEDVEFA PLDELLTRSD VISIHLRLSD ESRGLIGERE LSSMKPGSVL VNTARGAIVD
QDALIAALTN GPLAAAGLDV FTHEPLASGS ELRSLPNVIA LPHIGWTVEE VFLEFAEIAA
DQLDDYLRGE LSPDELLNPD VLG
//
