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Database: UniProt
Entry: A0A212TT57_9ACTN
LinkDB: A0A212TT57_9ACTN
Original site: A0A212TT57_9ACTN 
ID   A0A212TT57_9ACTN        Unreviewed;       358 AA.
AC   A0A212TT57;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SNC69179.1};
GN   ORFNames=SAMN06272741_3023 {ECO:0000313|EMBL:SNC69179.1};
OS   Streptomyces sp. 2114.4.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938836 {ECO:0000313|EMBL:SNC69179.1, ECO:0000313|Proteomes:UP000198141};
RN   [1] {ECO:0000313|Proteomes:UP000198141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2114.4 {ECO:0000313|Proteomes:UP000198141};
RA   Varghese N., Submissions S.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FYEY01000001; SNC69179.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212TT57; -.
DR   OrthoDB; 4324715at2; -.
DR   Proteomes; UP000198141; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          61..349
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          157..318
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   358 AA;  38065 MW;  C4A5FA49DCF639D1 CRC64;
     MTPPAHHHGG QAEKTRRTPG AAHRPAVLLS MGPGIAERLL DARHHTRLAA LARTDPRLVA
     HELADPTPAV AAALADAEVL LTCWGAPRLT GRVLDAAPRL RAVVHAAGSV KHHLTDACWE
     RGIAVASAAA ANALPVAEYT LAAILFAGKG VLHAAHRYRG LRTAHDWHRE LGAAGNYRRT
     VGVIGASRIG RRVIELLRPF DLQVLLYDPY VTDADATRLG ARPVPLDALC TGSDLVTVHA
     PQLPATRHLL GARELALLPD GATLINTARG SLVDGAALLP ELVSGRLHAV LDVTEPELPP
     VGSPLYELPN VLLTPHVAGS LGTELHRLAD HALDELEHYA QGRPFTDPVR PEQLPHSA
//
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