ID G4FKM3_9SYNE Unreviewed; 326 AA.
AC G4FKM3;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:EHA63533.1};
DE EC=1.1.1.29 {ECO:0000313|EMBL:EHA63533.1};
GN ORFNames=Syn8016DRAFT_0574 {ECO:0000313|EMBL:EHA63533.1};
OS Synechococcus sp. WH 8016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA63533.1, ECO:0000313|Proteomes:UP000002752};
RN [1] {ECO:0000313|EMBL:EHA63533.1, ECO:0000313|Proteomes:UP000002752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT "The draft genome of Synechococcus sp. WH 8016.";
RL Submitted (SEP-2011) 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:EHA63533.1}.
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DR EMBL; AGIK01000001; EHA63533.1; -; Genomic_DNA.
DR RefSeq; WP_006852715.1; NZ_AGIK01000001.1.
DR AlphaFoldDB; G4FKM3; -.
DR STRING; 166318.Syn8016DRAFT_0574; -.
DR PATRIC; fig|166318.3.peg.628; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000002752; Unassembled WGS sequence.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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 26..314
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 120..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 35236 MW; FD144C467151F1B6 CRC64;
MAGDRSQTAE GTPLPPAVFL DALSLGPVDL APMQQWCDLQ AWPSTSLDER MERLQNAEIA
ITNKIPLDGL LLRQLPKLRL ICVAATGTDQ IDHAVCAEQG IRVHNAGRYS RASVVQITWA
LILELCCAMD QRRRDLIAGS WQRSPVFSLI EPEFDELEGQ TLVVLGAGDI GRGVLAIGAA
FGMECIALTS RSSSAELEAA LRKADVLSLH APLTPHTQNL INALRLSWMK PSALLVNMAR
GGLVNLEDLC AALRHGQLAG AALDVLPVEP PGPELERLLE TPNLLISPHM GWSSRQARCR
LVHTLAGHLQ AYVAAMARSG SRRPSL
//
