ID A0A0Q9N998_9BACL Unreviewed; 327 AA.
AC A0A0Q9N998;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=D-glycerate dehydrogenase {ECO:0000313|EMBL:KRE69860.1};
DE EC=1.1.1.79 {ECO:0000313|EMBL:KRE69860.1};
DE EC=1.1.1.81 {ECO:0000313|EMBL:KRE69860.1};
GN ORFNames=ASL11_15995 {ECO:0000313|EMBL:KRE69860.1};
OS Paenibacillus sp. Soil750.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736398 {ECO:0000313|EMBL:KRE69860.1, ECO:0000313|Proteomes:UP000051252};
RN [1] {ECO:0000313|EMBL:KRE69860.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE69860.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE69860.1, ECO:0000313|Proteomes:UP000051252}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil750 {ECO:0000313|EMBL:KRE69860.1,
RC ECO:0000313|Proteomes:UP000051252};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE69860.1}.
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DR EMBL; LMSD01000012; KRE69860.1; -; Genomic_DNA.
DR RefSeq; WP_056616134.1; NZ_LMSD01000012.1.
DR AlphaFoldDB; A0A0Q9N998; -.
DR STRING; 1736398.ASL11_15995; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000051252; Unassembled WGS sequence.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:KRE69860.1}.
FT DOMAIN 7..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 327 AA; 35918 MW; 469AE3E9428214A0 CRC64;
MSTKPKILVT HKLPETVQDY LNLHGDCTFW NQEGSMPRSV ILDKVSDAEG ILGGTIDEEL
LSRAPRLRVA STSSVGYNHF DLDAMRSHGV IGTHTPYVLD STVADLVLAL MLSAGRRIAE
LDAYVKQGKW QKGTSGTELF GVDVHHSTLG IIGMGRIGEA IAQRAVFGFD MNLLYHSRRP
KKEVDERFHA RFCELDELLR ESDYIVVMTP LTPETKHMIG EEQFNLMKSS AIFINASRGA
TVDEQALIKA LQQGKIRGAG LDVFDIEPTP ADNPLLSMPN VVTLPHIGSA TARTRNDMAE
LAAKNLVEAL NGGQAYVVQE LKDLVPN
//
