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Database: UniProt
Entry: A0A367B9J7_9ACTN
LinkDB: A0A367B9J7_9ACTN
Original site: A0A367B9J7_9ACTN 
ID   A0A367B9J7_9ACTN        Unreviewed;       317 AA.
AC   A0A367B9J7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=D-2-hydroxyacid dehydrogenase family protein {ECO:0000313|EMBL:RBY97940.1};
GN   ORFNames=DQ237_03330 {ECO:0000313|EMBL:RBY97940.1};
OS   Blastococcus sp. TF02-8.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY97940.1, ECO:0000313|Proteomes:UP000252403};
RN   [1] {ECO:0000313|EMBL:RBY97940.1, ECO:0000313|Proteomes:UP000252403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TF02-8 {ECO:0000313|EMBL:RBY97940.1,
RC   ECO:0000313|Proteomes:UP000252403};
RA   Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA   Thomas W.K., Tisa L.S.;
RT   "Genome Sequence of Blastococcus sp. TF02-8.";
RL   Submitted (JUL-2018) 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:RBY97940.1}.
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DR   EMBL; QOHK01000001; RBY97940.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367B9J7; -.
DR   OrthoDB; 117809at2; -.
DR   Proteomes; UP000252403; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; 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.
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:UP000252403}.
FT   DOMAIN          26..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   317 AA;  33683 MW;  2F74C96B07E3FE10 CRC64;
     MTRIAVLDDY QSIAAEFCDW SRVPGEVEVV AFTEHLGDED AVAAALQGFQ VVVAMRERTE
     FRRSLLERLP DLRLLVTTGM RNKSIDVAAA AEHGITVCGT GSNATATVEL AWALILAAVR
     HIPAEDAAVR AGGWQQTIGT DLAGARLGVV GLGRLGSRVA AIGQAFGMDV VAWSQNLTDG
     RAAEVGVRRV ERDELFATAD VITIHLLLSK RTRGLIGADD LALMKHTAVL VNTSRGPIVQ
     QQPLLDALTD GRIGGAALDV YDSEPLPADS PLRTAPRTVL TPHLGYVTRG TYGVFYGEAV
     DDVAAWVAGS PVRVIAD
//
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