ID A0A0A0D629_9PROT Unreviewed; 322 AA.
AC A0A0A0D629;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:KGM33559.1};
GN ORFNames=P409_15175 {ECO:0000313|EMBL:KGM33559.1};
OS Inquilinus limosus MP06.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Inquilinus.
OX NCBI_TaxID=1398085 {ECO:0000313|EMBL:KGM33559.1, ECO:0000313|Proteomes:UP000029995};
RN [1] {ECO:0000313|EMBL:KGM33559.1, ECO:0000313|Proteomes:UP000029995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP06 {ECO:0000313|EMBL:KGM33559.1,
RC ECO:0000313|Proteomes:UP000029995};
RA Pino M., Di Conza J., Gutkind G.;
RT "Genome sequence determination for a cystic fibrosis isolate, Inquilinus
RT limosus.";
RL Submitted (JAN-2014) 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:KGM33559.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JANX01000170; KGM33559.1; -; Genomic_DNA.
DR RefSeq; WP_034838404.1; NZ_JANX01000170.1.
DR AlphaFoldDB; A0A0A0D629; -.
DR OrthoDB; 9793626at2; -.
DR Proteomes; UP000029995; 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; cd12175; 2-Hacid_dh_11; 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF286; D-3-PHOSPHOGLYCERATE DEHYDROGENASE 1-RELATED; 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 5..108
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 34175 MW; BE1E6F3966631ED1 CRC64;
MTETVVVLDP ISEDSVTRLR ALLPPGLVLT HGTARGDDHL KEIIAGAEYA IAGQVGVSGE
VLRAAPRLKL LHKWGVGVDN LDLDTARELN IRVARTTGSN AVPVAEFTLG LTLAALRCIA
FGHAELKKGH WRTATAMPMQ TFMLSGKTVG IIGFGAIGQA FARILKGFGC TILYSKRTPL
SAAEEADLGA RFATVPEILA QADVITLNCP LTPETKNLID RKALAAMKKT AVLVNAARGG
VVVEADLIEA LRSRTIHAAA MDVYEIEPLP ADSPLLTLDN LVVTPHLAAI AADNFVKTVN
QMFGNIACVA RGEPVPERDL VV
//
