ID A0A0N0UXB5_9BACI Unreviewed; 317 AA.
AC A0A0N0UXB5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KOY83734.1};
GN ORFNames=ADM90_02195 {ECO:0000313|EMBL:KOY83734.1};
OS Lysinibacillus macroides.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=33935 {ECO:0000313|EMBL:KOY83734.1, ECO:0000313|Proteomes:UP000037977};
RN [1] {ECO:0000313|EMBL:KOY83734.1, ECO:0000313|Proteomes:UP000037977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 54 {ECO:0000313|EMBL:KOY83734.1,
RC ECO:0000313|Proteomes:UP000037977};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:KOY83734.1}.
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DR EMBL; LGCI01000003; KOY83734.1; -; Genomic_DNA.
DR RefSeq; WP_053993432.1; NZ_LGCI01000003.1.
DR AlphaFoldDB; A0A0N0UXB5; -.
DR STRING; 33935.ADM90_02195; -.
DR PATRIC; fig|33935.3.peg.4626; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000037977; 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; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 21..315
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34884 MW; 4E332E9F95737165 CRC64;
MNIVILDGYT LNPGDLSWRK LSEVGEVTVY NRTPNNLIVE RAVEAEIILT NKTPLPKEIL
AQLPKLKYIG VLATGYDVVD VEAAKEQNVV VTNIPAYGTH SVAQMVFALL LEHCQRVQRH
SDAVRAGEWT NHQDWCFWNY PLIELAGKKF GIVGFGRIGY QTAQVASALG MSIIAYNRQQ
REVDLPNFQW ADHLTDLLKE ADVISLHCPL TPETEEIINR DNLAIMKASA IIINTSRGRL
INNQDLADAL NNGVIAGAGL DVLDVEPPSA SNPLLSAKNC MITPHISWAT KEARGRLLDM
AVDNVKAFVA GAARNIV
//
