ID U5RRN0_9CLOT Unreviewed; 313 AA.
AC U5RRN0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:AGY75401.1};
GN ORFNames=CAETHG_1176 {ECO:0000313|EMBL:AGY75401.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY75401.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY75401.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY75401.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY75401.1; -; Genomic_DNA.
DR RefSeq; WP_023162164.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RRN0; -.
DR KEGG; cah:CAETHG_1176; -.
DR PATRIC; fig|1341692.11.peg.1171; -.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12173; PGDH_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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 5..313
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..281
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 313 AA; 34348 MW; 9D004DB499D4C31D CRC64;
MSYKVLITEN IYEEGKEYLR SHGYELKMAS DISENVLVEE VKDCDAILVR MANITEKIMK
SGTKLKVISK FGVGVDNIDV EAASSLGIRV TNSPESNKNS VAEYTMGLIL LLAKRLLIYD
RELRDGNFQI RKSFGMDLEG KTLGIIGVGS IGELVALKAS KGFGMKVIGF KRNIAANQID
NIKLTGDLDY VLKNSDFVSL HVPLTEKTKG MIGKRELSIM KPKAFLINTA RGEVVDEDAL
LEALLQNKIA GAAIDVFKGE EPSKDNPLFK LENVIVTPHT AAHTEEAGIR MSLHPAIGID
EVLSGREPSW PVN
//