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Database: UniProt
Entry: A0A1I2B2E6_9ACTN
LinkDB: A0A1I2B2E6_9ACTN
Original site: A0A1I2B2E6_9ACTN 
ID   A0A1I2B2E6_9ACTN        Unreviewed;       318 AA.
AC   A0A1I2B2E6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:SFE50246.1};
GN   ORFNames=SAMN05216574_10431 {ECO:0000313|EMBL:SFE50246.1};
OS   Blastococcus sp. DSM 46838.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798228 {ECO:0000313|EMBL:SFE50246.1, ECO:0000313|Proteomes:UP000198589};
RN   [1] {ECO:0000313|Proteomes:UP000198589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46838 {ECO:0000313|Proteomes:UP000198589};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOND01000004; SFE50246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2B2E6; -.
DR   STRING; 1798228.SAMN05216574_10431; -.
DR   OrthoDB; 117809at2; -.
DR   Proteomes; UP000198589; 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; cd12169; PGDH_like_1; 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; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198589}.
FT   DOMAIN          29..312
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          113..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   318 AA;  34655 MW;  AB82E09CEEE3DE7D CRC64;
     MHRIAVLDDY QSVAASFCDW SQLPEPAEVV EFHDAVADPD ALVARLRPFD VVLAMRERTR
     FPREVLERLP DLRLLVTTGM RNKSIDVTAA TELGITVCGT GSQTTATAEL TWALILATLR
     HVPQEDASIR AGGWQQTLGG DLAGGTLGVV GLGRLGSQVA RIGAAFGMDV VAWSQNLTDE
     RAAECGARRV GKEELFATAD VVTVHLVWSK RTRGLITAAD LARMKPTAVF VNTSRGPIVE
     EAALIDVLRE GRIAGAGIDV YDTEPLPRDH PLRELRRAVL TPHLGYVTRG SYEIYYREAV
     EDVAAWLSGR PLRVIRPG
//
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