ID A0A2W2DMY9_9ACTN Unreviewed; 332 AA.
AC A0A2W2DMY9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:PZG13316.1};
GN ORFNames=C1J01_30320 {ECO:0000313|EMBL:PZG13316.1};
OS Nonomuraea aridisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2070368 {ECO:0000313|EMBL:PZG13316.1, ECO:0000313|Proteomes:UP000249304};
RN [1] {ECO:0000313|EMBL:PZG13316.1, ECO:0000313|Proteomes:UP000249304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC333 {ECO:0000313|EMBL:PZG13316.1,
RC ECO:0000313|Proteomes:UP000249304};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Nonomuraea sp. KC333.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:PZG13316.1}.
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DR EMBL; POUD01000160; PZG13316.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2DMY9; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000249304; 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; 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000249304}.
FT DOMAIN 47..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 332 AA; 36065 MW; F10EAE95EE6C3781 CRC64;
MLESALPVPP CERTLMIALS LTPELREMFL PSPIWDDLVR LGPIVPMEEA EVLVTGWETP
RLDAEALERA PRLRLVAHTG AAVGFLVSDA LWDRGIRVTQ TGAAMAPAVG EMALTFTLSL
LHQVHRFDHR LRSGGGWEET RAAARPAREL RGSVVGVVGA SRTGRAYLEL VRPLGAELLL
TDPLVDAAEA AALGATLVPL DELLSRSDVV ALHAPAIPAT RHLLGRRELA LLRDGAALVN
TARSWLVDSD ALLDELRAGR IDAALDVFDE EPLPLDSPLR ALPNVLLTPH QAAATVEGHE
RQGRSTVAEI ARFLSGEPLR HEITRERLRW TA
//
