ID D4GV02_HALVD Unreviewed; 319 AA.
AC D4GV02; L9V5T8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=D-2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ADE04909.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:ADE04909.1};
GN Name=serA2 {ECO:0000313|EMBL:ADE04909.1};
GN OrderedLocusNames=HVO_2648 {ECO:0000313|EMBL:ADE04909.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE04909.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE04909.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001956; ADE04909.1; -; Genomic_DNA.
DR RefSeq; WP_004042769.1; NZ_AOHU01000046.1.
DR AlphaFoldDB; D4GV02; -.
DR STRING; 309800.HVO_2648; -.
DR PaxDb; 309800-C498_08520; -.
DR EnsemblBacteria; ADE04909; ADE04909; HVO_2648.
DR GeneID; 8925896; -.
DR KEGG; hvo:HVO_2648; -.
DR PATRIC; fig|309800.29.peg.1667; -.
DR eggNOG; arCOG01757; Archaea.
DR HOGENOM; CLU_019796_1_0_2; -.
DR OrthoDB; 168224at2157; -.
DR Proteomes; UP000008243; 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; cd05300; 2-Hacid_dh_1; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; 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:UP000008243}.
FT DOMAIN 54..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 319 AA; 34262 MW; 1C58F43BF6EB5BCB CRC64;
MSDPDIAVLR QKIHGLSAEA YAETLRERLP DREVALATTP AEERDLLSRA RVATGFDVSE
ADLDAAENLD LFACVFAGTG HLPIEAFEAR DVAVTNASGV HGPNIAEQVL GSLLYFARRF
HVAERQKDAG VWQSYPTVEL QGSTVVVVGL GALGEAVVDR LDPFGVETVG VRHSPEKGGP
TDEVVGFDDE QGLHDAFARA DYVVIACPLT DATRGLVDAD AFASMAPDTV LVNVGRGPVV
DTDALVSQLR SNGIRGAALD VTDPEPLPAD HPLWEFENVL ITPHNAGHTP KYWERMADII
AENLDKLDAG DDDLRNRVA
//
