ID C6A377_THESM Unreviewed; 333 AA.
AC C6A377;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ACS90072.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:ACS90072.1};
GN OrderedLocusNames=TSIB_1016 {ECO:0000313|EMBL:ACS90072.1};
OS Thermococcus sibiricus (strain DSM 12597 / MM 739).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=604354 {ECO:0000313|EMBL:ACS90072.1, ECO:0000313|Proteomes:UP000009079};
RN [1] {ECO:0000313|EMBL:ACS90072.1, ECO:0000313|Proteomes:UP000009079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12597 / MM 739 {ECO:0000313|Proteomes:UP000009079};
RX PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT "Metabolic versatility and indigenous origin of the archaeon Thermococcus
RT sibiricus, isolated from a siberian oil reservoir, as revealed by genome
RT analysis.";
RL Appl. Environ. Microbiol. 75:4580-4588(2009).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001463; ACS90072.1; -; Genomic_DNA.
DR RefSeq; WP_015849291.1; NC_012883.1.
DR AlphaFoldDB; C6A377; -.
DR STRING; 604354.TSIB_1016; -.
DR GeneID; 8096012; -.
DR KEGG; tsi:TSIB_1016; -.
DR eggNOG; arCOG01755; Archaea.
DR HOGENOM; CLU_019796_1_3_2; -.
DR OrthoDB; 34275at2157; -.
DR Proteomes; UP000009079; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:ACS90072.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009079}.
FT DOMAIN 6..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 333 AA; 37664 MW; 30362238EF58ED6A CRC64;
MKPKVLVLFN MKSNAMKLLK EYCDVDVMVY PTKEEVLQVI GAYDGLIVSP LNLVDKEIIE
HGKKLKVIST QSAGYDHIDI NAATEKGIYV TKVSGILSEA VAEFAVGLTI ALLRKIAYSD
RFIRKGLWDS HKTIWGWYKE METLHGKKIG ILGMGSIGKG IARRMKAMNT EIYYWSRTRK
EDIEKEVNAK WLPINDVLKE SDIVILALPS TPETYHIINE ETLELLKGKY LVNVGRGSLV
DEKVLIKALK EGNLKGFATD VFEKEPIQES ELFEMEWETV LTPHHAGLAQ EAMEDMALQA
VNNLLEILMG NVSENLVNRD VLKVRPIEDI KMF
//
