ID A0A0N0RD25_9CHLR Unreviewed; 328 AA.
AC A0A0N0RD25;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:KPL80965.1};
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:GAP19246.1};
GN ORFNames=ADN01_10810 {ECO:0000313|EMBL:KPL80965.1}, LSAC_03146
GN {ECO:0000313|EMBL:GAP19246.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:GAP19246.1};
RN [1] {ECO:0000313|EMBL:GAP19246.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:GAP19246.1};
RA Matsuura N., Tourlousse M.D., Ohashi A., Hugenholtz P., Sekiguchi Y.;
RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT saccharolytica KIBI-1, Longilinea arvoryzae KOME-1, Previously Described as
RT Members of the Class Anaerolineae (Chloroflexi).";
RL Genome Announc. 3:e00975-15(2015).
RN [2] {ECO:0000313|EMBL:KPL80965.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL80965.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-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}.
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DR EMBL; DF967975; GAP19246.1; -; Genomic_DNA.
DR EMBL; LGCM01000038; KPL80965.1; -; Genomic_DNA.
DR RefSeq; WP_062419537.1; NZ_LGCM01000038.1.
DR AlphaFoldDB; A0A0N0RD25; -.
DR STRING; 229921.ADN01_10810; -.
DR PATRIC; fig|229921.5.peg.565; -.
DR OrthoDB; 9792971at2; -.
DR Proteomes; UP000050501; 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; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000050501}.
FT DOMAIN 7..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 34889 MW; 68D3742507C7A767 CRC64;
MDSPRIFVTR RIAAQALKQL EGRVQMEVWE GSGPPPRAEL EARLPHLDGL LSLLTDPLNA
EMIALAGPNF RVLSQMAVGT DNIDLAAASA RRIPVGHTPG VLTEACADFA MALLLAAARR
VVEGDREVRA GIWRPWGPDI LVGKDLYGGT LGIVGFGRIG QAVARRAQGF GMRLLVHDLN
PDTHLEKCFG IQFVSLPELL RQSDFVSIHV YLSPQTRGMF NAETLGQMKP GAVLVNTARG
PIVEPQALQA ALESGRLAAA ALDVFDPEPI PADSPLLAMP NVIITPHIAS AAGQVRLNMA
QIAVENLLLG LAGQPLRFCA NAAALGPA
//
