ID A0A1G5B4Q2_9ACTN Unreviewed; 356 AA.
AC A0A1G5B4Q2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SCX85103.1};
GN ORFNames=SAMN02745898_10135 {ECO:0000313|EMBL:SCX85103.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCX85103.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCX85103.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCX85103.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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; FMVI01000001; SCX85103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5B4Q2; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000199326; 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; cd12167; 2-Hacid_dh_8; 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:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199326}.
FT DOMAIN 60..347
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 162..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 356 AA; 37433 MW; E0EA217602E6A672 CRC64;
MRTTEEAPAH SGSDTAETPP RRPRTVLVMS PGLVDDVFPP AVRARLEESA DLLTPSALGE
FASPEAAEAL ASAEVLLTGW GCPPVDAALL DRAPGLRAVI HAAGTVKTFL SPVAFDRGIV
VSSAAAANAV PVAEYTLAAI IMGAKRVFPL AGLFRTRRTH RTGADLDRQH WLGTHGLTIG
VVGASRIGRR VIELLRILDA DVLLHDPYVG AAEAARLGVT PTDLDTLVAT SDVVTVHAPD
TPETRGLIDA RRIGLMRPGT LLVNTARGPL VDTEALTEHL VSGRLDAVLD VTSPEPLPDG
HPLWDLPNVF LTPHLAGAQG NEVGRLGALA VDELVRYAQG APLAHPVHRA DLGRIA
//
