ID A0A0U3F154_9BURK Unreviewed; 335 AA.
AC A0A0U3F154;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:ALT77361.1};
GN ORFNames=AT984_09320 {ECO:0000313|EMBL:ALT77361.1};
OS Paucibacter sp. KCTC 42545.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Paucibacter.
OX NCBI_TaxID=1768242 {ECO:0000313|EMBL:ALT77361.1, ECO:0000313|Proteomes:UP000056576};
RN [1] {ECO:0000313|EMBL:ALT77361.1, ECO:0000313|Proteomes:UP000056576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42545 {ECO:0000313|EMBL:ALT77361.1,
RC ECO:0000313|Proteomes:UP000056576};
RA Kim S.-G., Lee Y.-J.;
RT "Complete genome of Paucibacter sp. KCTC 42545.";
RL Submitted (DEC-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}.
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DR EMBL; CP013692; ALT77361.1; -; Genomic_DNA.
DR RefSeq; WP_058719862.1; NZ_CP013692.1.
DR AlphaFoldDB; A0A0U3F154; -.
DR STRING; 1768242.AT984_09320; -.
DR KEGG; pkt:AT984_09320; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000056576; Chromosome.
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; cd12169; PGDH_like_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; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000056576}.
FT DOMAIN 34..324
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 36665 MW; 18DD8E723CDBB853 CRC64;
MNIIILDDYQ DAVRKLRCAA KLEHLHAKVF TNTVKGIGQL SVRLRDAEVL VLIRERTAFP
RQLLEKLPKL KLISQTGRVG AHVDVAACTK LGIAVAEGVG SPTAPAELTW ALIMAAMRRL
PQYISNLKHG IWQQSGLKAA SMPPNFGLGM VLKGKTMGIW GYGRIGQLVA GYAHAFGMQV
MVWGSEASRL RASADGYLAA ESREQFFESC DVLSLHLRLS PTTTGLVGPE DFARMKPTAL
FVNTSRAELI AEGALVSALN RGRPGMAAID VFETEPVLQG HPLLRMENAV CTPHIGYVEQ
DSYELYLDAA FENVLNFIKS EPSNLINPEA LKVMR
//