ID A0A423PQC0_9GAMM Unreviewed; 318 AA.
AC A0A423PQC0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:ROO27790.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:ROO27790.1};
GN ORFNames=SAOR_08175 {ECO:0000313|EMBL:ROO27790.1};
OS Salinisphaera orenii MK-B5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Salinisphaerales;
OC Salinisphaeraceae; Salinisphaera.
OX NCBI_TaxID=856730 {ECO:0000313|EMBL:ROO27790.1, ECO:0000313|Proteomes:UP000283993};
RN [1] {ECO:0000313|EMBL:ROO27790.1, ECO:0000313|Proteomes:UP000283993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MK-B5 {ECO:0000313|EMBL:ROO27790.1,
RC ECO:0000313|Proteomes:UP000283993};
RA Lai Q., Li C., Shao Z.;
RT "Salinisphaera orenii MK-B5 Genome Sequencing.";
RL Submitted (OCT-2013) 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:ROO27790.1}.
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DR EMBL; AYKH01000012; ROO27790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423PQC0; -.
DR Proteomes; UP000283993; Unassembled WGS sequence.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000283993}.
FT DOMAIN 28..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..287
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 33698 MW; 92C3D4A8E60C8052 CRC64;
MMRGCFLDAG SMGDALDWTA LTDTLDDWTW HHNTEPAEVG ERLRGVDVAV TNKVVLDAGT
IAAADALKLI CVAATGVNNV DLQAAADHGI PVLNVSGYGT PAVSQHVLAL MLGHATRWAA
YDAAVKRGAW AQSEFFCFLD YPIEELDGQT LGIVGHGELG GAVARLAEAF GMTVLVSERP
GADDVRPGRV AFDDVLTRAD FISLHCPLTP ETEHLIDAAA LARMKSNAFL INTARGGIVD
ASALIAALRE GRIAGAALDV LDQEPPPADH PLLDPSIPNL VVTPHSAWAS RGARQRLLNQ
IAANVRAFRA GDTDHRVN
//
