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Database: UniProt
Entry: I3TCN7_THEC1
LinkDB: I3TCN7_THEC1
Original site: I3TCN7_THEC1 
ID   I3TCN7_THEC1            Unreviewed;       309 AA.
AC   I3TCN7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding protein {ECO:0000313|EMBL:AFK50525.1};
GN   OrderedLocusNames=TCELL_0100 {ECO:0000313|EMBL:AFK50525.1};
OS   Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Thermogladius.
OX   NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50525.1, ECO:0000313|Proteomes:UP000005270};
RN   [1] {ECO:0000313|EMBL:AFK50525.1, ECO:0000313|Proteomes:UP000005270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22663 / VKM B-2946 / 1633
RC   {ECO:0000313|Proteomes:UP000005270};
RX   PubMed=22843584; DOI=10.1128/JB.00894-12;
RA   Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A.,
RA   Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the hyperthermophilic cellulolytic
RT   Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL   J. Bacteriol. 194:4446-4447(2012).
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; CP003531; AFK50525.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TCN7; -.
DR   STRING; 1184251.TCELL_0100; -.
DR   KEGG; thg:TCELL_0100; -.
DR   eggNOG; arCOG01754; Archaea.
DR   HOGENOM; CLU_019796_1_3_2; -.
DR   InParanoid; I3TCN7; -.
DR   OrthoDB; 7437at2157; -.
DR   Proteomes; UP000005270; Chromosome.
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   CDD; cd05303; PGDH_2; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 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:UP000005270}.
FT   DOMAIN          8..308
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   309 AA;  33864 MW;  EBDEA6FFC7B10235 CRC64;
     MKHVVYRVLV ASKISRSAVD YLKSQGFEVV EVHEPSEDEL ARLIKGFHAI IVRSKPRVTR
     RVIEAADQLK VIARAGVGLD NIDVQAAESR GIKVVNAPES VTQAVAELTV GLMLALLRKI
     AFSDRKMREG VWVKHEAVGT ELKGKTLGLV GFGRIGRAVA RICYYGFGMK IIYTDRQCNI
     EAGREFNAEC VDLDTLLRTA DIVSLHVPLT PETTHLINEE KLRLMKKTAI LVNTARGAVV
     DTNALVKALK EGWIAGAALD VFEEEPLPKD HPLLQLDNVV LTPHIGASSV EAQDQAGIEV
     AKKIAELLK
//
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