ID A0A157K9U4_9BORD Unreviewed; 342 AA.
AC A0A157K9U4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SAI72557.1};
DE EC=1.1.1.95 {ECO:0000313|EMBL:SAI72557.1};
GN Name=serA4 {ECO:0000313|EMBL:SAI72557.1};
GN ORFNames=SAMEA3906487_03262 {ECO:0000313|EMBL:SAI72557.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI72557.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI72557.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI72557.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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}.
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DR EMBL; LT546645; SAI72557.1; -; Genomic_DNA.
DR RefSeq; WP_063492262.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157K9U4; -.
DR STRING; 123899.SAMEA3906487_03262; -.
DR GeneID; 56589498; -.
DR KEGG; btrm:SAMEA390648703262; -.
DR PATRIC; fig|123899.6.peg.3259; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000076825; Chromosome 1.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR CDD; cd12173; PGDH_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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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:UP000076825}.
FT DOMAIN 66..326
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 119..294
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 342 AA; 36048 MW; A9DE56B5E90B0250 CRC64;
MSATQIARLD LWIDPVFDRL VQAEPALSLK VLPALAGDAR TAAGLAEAQA YHVSAAKDEV
PRDWWVDAEL LAACPQLLCV SSGGAGYDTV DVAACTEAGV AVVNQAGANA ASVAEMTYAL
LLSLVKRLDA SGAALRGGQS VSREALMGRE IEGRVLGLVG IGEIGQRVAR IAPAFGLQVL
ACDPLLSDAE IRERGAEPVD FDSLLARADI VSLHCPLNAE TRGSFDTQAF ARMKPGALFL
STARGGIHDE AALLAALESG HLHGAGLDVW TVEPPPADHG LLARADVVAT YHTGGVTHEG
RRKVAEGSAR QLIAMLRGER PARLLNPQVW PRYLERLRAA RA
//
