ID A0A2U2MX38_9GAMM Unreviewed; 320 AA.
AC A0A2U2MX38;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:PWG61392.1};
GN ORFNames=DEM34_16615 {ECO:0000313|EMBL:PWG61392.1};
OS Spiribacter halobius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=2182432 {ECO:0000313|EMBL:PWG61392.1, ECO:0000313|Proteomes:UP000245474};
RN [1] {ECO:0000313|EMBL:PWG61392.1, ECO:0000313|Proteomes:UP000245474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E85 {ECO:0000313|EMBL:PWG61392.1,
RC ECO:0000313|Proteomes:UP000245474};
RA Zheng W.-S., Lu D.-C., Du Z.-J.;
RT "Spiribacter halobius sp. nov., a moderately halophilic bacterium isolated
RT from marine solar saltern.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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:PWG61392.1}.
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DR EMBL; QFFI01000036; PWG61392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2MX38; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000245474; Unassembled WGS sequence.
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; cd05301; GDH; 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; 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.
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:UP000245474}.
FT DOMAIN 6..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 34321 MW; 1E677BEC79B99EF2 CRC64;
MSKPKVLVTR KLPDSVQQRL QRDYDALFNH DDHVFDRGEL LAKAEGVAAI LPCHSERFSA
DVIDALPDSV RIIANYSVGV DHVDLEAAKR RGIVVTNTPD VLSDATAEIA LLLALGAARR
ASEGDRLVRR GAWTQWSPSF MVGTQITGKA VGIVGMGRVG RAAAQRFRGL DMEIHYHNRS
RLPEAQAQGA HYHASLDEML GAVDVVSLHC PATPDTTGLI NAERIARLRD GAILVNTARG
ALVDDDALIA GLKAGKPAAA GLDVFNGEPG GDPRYRELDN TFLLPHIGSA TTETRAAMGE
RALANLDAFF AGREPGDRVA
//
