ID A0A0F0CAF2_9CLOT Unreviewed; 320 AA.
AC A0A0F0CAF2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KJJ68365.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:KJJ68365.1};
GN Name=hprA_4 {ECO:0000313|EMBL:KJJ68365.1};
GN ORFNames=CLFS41_44300 {ECO:0000313|EMBL:KJJ68365.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ68365.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ68365.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ68365.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-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:KJJ68365.1}.
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DR EMBL; JYHN01000069; KJJ68365.1; -; Genomic_DNA.
DR RefSeq; WP_045093507.1; NZ_JYHN01000069.1.
DR AlphaFoldDB; A0A0F0CAF2; -.
DR PATRIC; fig|1609975.3.peg.4742; -.
DR Proteomes; UP000033604; Unassembled WGS sequence.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT DOMAIN 21..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..289
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 35114 MW; 05FA075A038B533A CRC64;
MKIVVLDGYT ENPGDLSWGE LEKLGELTVY DRTSVTDENE IISRIGDAEV VITNKTPITK
NIMDACPGIK YIAMLATGYN VVDYVYAREK GIPLSNVPSY GTASVGQFAI AMLLELCHHV
AHHSQTVHEG KWEHCQDWCY WDYPLIELDG KTMGIIGFGR IGQQTGKIAK AMGMNILAYD
NYPNESGKEI AEYVDLDTLY AKSDVIALHC PLFPETQGII NKDAIAKMKD GVMILNNSRG
PLVVEQDLAD ALNSGKVSGA GLDVVSTEPI KGDNPLLKAK NCIITPHISW APKESRQRIM
DHTVENVKAY LAGAPIHVVN
//
