ID A0A0J6CUZ6_9BACI Unreviewed; 316 AA.
AC A0A0J6CUZ6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KMM35929.1};
GN ORFNames=AB986_21020 {ECO:0000313|EMBL:KMM35929.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM35929.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM35929.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM35929.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-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:KMM35929.1}.
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DR EMBL; LELK01000015; KMM35929.1; -; Genomic_DNA.
DR RefSeq; WP_048313651.1; NZ_LELK01000015.1.
DR AlphaFoldDB; A0A0J6CUZ6; -.
DR STRING; 157733.AB986_21020; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000035996; 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; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
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:UP000035996}.
FT DOMAIN 14..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 105..277
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 316 AA; 36079 MW; 7907C850676A9BC7 CRC64;
MQILSTAKLR SDIKDQLIEA YPEVTFRFER SMKEAELFLS EAEILLTYGE DLTVEHIEKA
RHLKWIMVLS AGLERMPLET IKERGILITN ARGIHSIPMA EYTISVMLQV AREVKQVIAN
ESQGIWKKKV PMEEITGSTI GVVGTGAIGC EIGRIAHAFR MKTLGVNRTG HDADHFDEIY
KNEDITSMLP RCDYVIGVLP STTNTKHYFR KKHFEEMKQS AVFINIGRGD TVNEQELLDS
LNAGELKHAV LDVFENEPLD PSHPFWIMDN VTVTPHHSAI SENYQPRAIE IFEYNLKKYL
NECDDMKNVI DPNRGY
//
