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Database: UniProt
Entry: A0A1I3J5J9_9SPHI
LinkDB: A0A1I3J5J9_9SPHI
Original site: A0A1I3J5J9_9SPHI 
ID   A0A1I3J5J9_9SPHI        Unreviewed;       327 AA.
AC   A0A1I3J5J9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:SFI55248.1};
GN   ORFNames=SAMN05444682_104319 {ECO:0000313|EMBL:SFI55248.1};
OS   Parapedobacter indicus.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Parapedobacter.
OX   NCBI_TaxID=1477437 {ECO:0000313|EMBL:SFI55248.1, ECO:0000313|Proteomes:UP000198670};
RN   [1] {ECO:0000313|EMBL:SFI55248.1, ECO:0000313|Proteomes:UP000198670}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RK1 {ECO:0000313|EMBL:SFI55248.1,
RC   ECO:0000313|Proteomes:UP000198670};
RA   de Groot N.N.;
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; FOQO01000004; SFI55248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3J5J9; -.
DR   STRING; 1477437.SAMN05444682_104319; -.
DR   OrthoDB; 1522997at2; -.
DR   Proteomes; UP000198670; 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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF257; GLYCERATE DEHYDROGENASE HPR, PEROXISOMAL; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198670}.
FT   DOMAIN          4..319
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..287
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   327 AA;  36276 MW;  E38119F9D6DBE26C CRC64;
     MKIFVTRALP EIIKQSLANE GHIVSEWTEK RDLSPAELTD YSLANDALFS IGKNQIDKHF
     LTACSHLRVI ALCSVGYDHV DVDEATKFGI PIGNTPGVLS KATADTAFLL IQNVARKAIY
     NHKEILRGNW GFFDPMANLG IELHGKTLGI YGLGRIGFEL ARSCRYAFDM PVIYYNRSHN
     ERAEHELNAR RVSFDELLQQ SDVLSVHANL SEETEGIFDR HAFSKMKASS IFINTARGAI
     HNETDLQLAL EEGQIWGAGL DVTHPEPMAP GNPLLAMPTV AILPHIGSAT IETRMKMMQL
     TVENILAGLN GQRLPYCVNP KVYGVEH
//
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