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Database: UniProt
Entry: U5RRN0_9CLOT
LinkDB: U5RRN0_9CLOT
Original site: U5RRN0_9CLOT 
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
//
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