ID A0A1C4T777_9ACTN Unreviewed; 320 AA.
AC A0A1C4T777;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SCE55193.1};
GN ORFNames=GA0115234_111250 {ECO:0000313|EMBL:SCE55193.1};
OS Streptomyces sp. DvalAA-43.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCE55193.1, ECO:0000313|Proteomes:UP000199186};
RN [1] {ECO:0000313|EMBL:SCE55193.1, ECO:0000313|Proteomes:UP000199186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCE55193.1,
RC ECO:0000313|Proteomes:UP000199186};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMBW01000079; SCE55193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4T777; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000199186; 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; cd12166; 2-Hacid_dh_7; 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; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 64..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 33713 MW; E438F95C430BFA82 CRC64;
MTKTPDEAKT PEVWLPFPAD EIEGLPEGLT YRLWDGEPDY PADPADCAFY VVPYMKGPAV
AVRPLGAMAG VRVVQTLSAG IDHVEPALGL LPAGVRLCNA KGVHEASTAE LALTLILSSL
RGVPGFVHGQ DKEEWRSGFY PALADKSVLI VGYGSIGAAI EDRLAPFECA RVARVARSAR
TTARGPVHTL DDLPALLPDA DVVVLSTPLN PSTQGLVDAE FLAAMPDGAL LVNVARGGVV
DTEALLLELQ SGRLRAALDV TDPEPLPAGH PLWHAPHVLI TPHVGGSTSA FEPRAKRLLA
GQLSLFAAGE PVRNVVHTLG
//