ID A0A0N8PS87_9CHLR Unreviewed; 224 AA.
AC A0A0N8PS87;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:KPV52037.1};
DE Flags: Fragment;
GN ORFNames=SE17_17845 {ECO:0000313|EMBL:KPV52037.1};
OS Kouleothrix aurantiaca.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Kouleothrix.
OX NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV52037.1, ECO:0000313|Proteomes:UP000050509};
RN [1] {ECO:0000313|EMBL:KPV52037.1, ECO:0000313|Proteomes:UP000050509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COM-B {ECO:0000313|EMBL:KPV52037.1,
RC ECO:0000313|Proteomes:UP000050509};
RA Hemp J.;
RT "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL Submitted (SEP-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}.
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:KPV52037.1}.
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DR EMBL; LJCR01000683; KPV52037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N8PS87; -.
DR Proteomes; UP000050509; 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; 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.
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:UP000050509}.
FT DOMAIN 7..110
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..223
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT NON_TER 224
FT /evidence="ECO:0000313|EMBL:KPV52037.1"
SQ SEQUENCE 224 AA; 24036 MW; C4107668592C723E CRC64;
MTERPRVYVT RRLPQSALDL LARHARLSVW PGEQPPPRVV LMKEVAGLDG LLTLPSERVD
AALLAAAPNL RAVSNYAADS ENIDLAAATQ RGVLVAITPD IPTETCADFT FALMLAAARR
VGEGVQYLKA GQWRSWGPEV LLGRDIYGAT LGIVGMGRIG QAVARRARGF GMQILYADPA
PCPAIEQATG AAHVALDELL ASSEIISLHC PLTDDTYQLI DRDA
//
