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Database: UniProt
Entry: A0A2M9J441_9ACTN
LinkDB: A0A2M9J441_9ACTN
Original site: A0A2M9J441_9ACTN 
ID   A0A2M9J441_9ACTN        Unreviewed;       339 AA.
AC   A0A2M9J441;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:PJN01675.1};
GN   ORFNames=CG740_17995 {ECO:0000313|EMBL:PJN01675.1};
OS   Streptomyces sp. CB01201.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020324 {ECO:0000313|EMBL:PJN01675.1, ECO:0000313|Proteomes:UP000231916};
RN   [1] {ECO:0000313|Proteomes:UP000231916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01201 {ECO:0000313|Proteomes:UP000231916};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       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:PJN01675.1}.
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DR   EMBL; NNBJ01000008; PJN01675.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9J441; -.
DR   OrthoDB; 117809at2; -.
DR   Proteomes; UP000231916; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd12172; PGDH_like_2; 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; IPR029752; D-isomer_DH_CS1.
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.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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          46..321
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          116..289
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   339 AA;  35583 MW;  925A76D767CE2B3D CRC64;
     MTPTRGRVLV TTGWLGPGDE VDRYLTGAGL QVVHGSIRER ERRGRTLSDV VGSVDAIVAG
     TEHIGREVFE AAPRLRVIGR TGVGHDNVDV VAATAHGVAV CPTPGVNRQS VAEHTMGLLL
     GLARGIPQNV ASVRAGRWEQ PSGRELAGAT LGVVGLGAIG RLVAGLAQAF GMRVVAHDPA
     IDRAYAAEHD IGVRELPRLL NESDFVSLHL FLSPGTRHLL DANAFALMKP GAFVINTARG
     GIVDEDALAD ALASGRLGGA AMDTVGTEPL PPDSPLRSFD NVLVTAHIGA ATEESRARSG
     LMAARSVLTV LRGGRAEHTV NPEYAMLRDR ARPHGAARR
//
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