ID A0A090N3D0_OSTTA Unreviewed; 509 AA.
AC A0A090N3D0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase,NAD-binding {ECO:0000313|EMBL:CEF97903.1};
GN ORFNames=OT_ostta05g01360 {ECO:0000313|EMBL:CEF97903.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEF97903.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CEF97903.1}.
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DR EMBL; CAID01000005; CEF97903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090N3D0; -.
DR STRING; 70448.A0A090N3D0; -.
DR InParanoid; A0A090N3D0; -.
DR OrthoDB; 6392at2759; -.
DR Proteomes; UP000009170; Chromosome 5.
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 GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR CDD; cd12174; PGDH_like_3; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF55021; ACT-like; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT DOMAIN 133..398
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 190..366
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 53824 MW; 94B63C11E4BB6306 CRC64;
MLSTHVAVRA PRARAHATRG RVHARVPAAR RPRAVVTRAS DATDDEIEFL EKALKLAKSR
KGASGGGASA SAGAGSYNGA SFNVKTFNAI SPVGLGKFPP GKYAVSGDDG ALPGDPMAIM
LRSHKLQVSE VGPTVRGIVR CGAGTNNIPT KEMSERGIPV FNTPGANANA VKELVVCSLL
LASRGILEGN RHVNEVINVE ENGDYAKISS RIEKDKAMFG GMEIEGKTLG VIGLGAIGSR
VVNAALGLGM KVVGYDPVLS LEAAWRLPGD KMSRADDLDE LFEKSDYITI HVPYIKGVTH
HLIDARALSK CKPGVHLLNF ARGEIIDGSA VRAAYDSGKL TGKYVSDFSD PDLMGHPRHI
VLPHLGASTE EAEENSAAMA AETMMDFLET GTIRNSVNFP TTILPPHKNS SGARLCIVNK
NEAGALGEIT TFLGTQGCNI LQQINTSRDG IAYTVIDLEK IPADPAALQD ALAKTCPMVV
SSRFIGSVFN DELGSPGTYF WVRDATGSA
//
