ID Q9FDT6_MICAE Unreviewed; 337 AA.
AC Q9FDT6;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:BAB12215.1};
GN Name=mcyI {ECO:0000313|EMBL:BAB12215.1};
OS Microcystis aeruginosa.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1126 {ECO:0000313|EMBL:BAB12215.1};
RN [1] {ECO:0000313|EMBL:BAB12215.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K-139 {ECO:0000313|EMBL:BAB12215.1};
RX PubMed=10467167;
RA Nishizawa T., Asayama M., Fujii K., Harada K., Shirai M.;
RT "Genetic analysis of the peptide synthetase genes for a cyclic heptapeptide
RT microcystin in Microcystis spp.";
RL J. Biochem. 126:520-529(1999).
RN [2] {ECO:0000313|EMBL:BAB12215.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=K-139 {ECO:0000313|EMBL:BAB12215.1};
RX PubMed=10788786;
RA Nishizawa T., Ueda A., Asayama M., Fujii K., Harada K., Ochi K., Shirai M.;
RT "Polyketide synthase gene coupled to the peptide synthetase module involved
RT in the biosynthesis of the cyclic heptapeptide microcystin.";
RL J. Biochem. 127:779-789(2000).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; AB032549; BAB12215.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9FDT6; -.
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; cd12173; PGDH_4; 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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 18..330
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 120..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 337 AA; 36793 MW; DA50BE8522C4BB38 CRC64;
MTTTSPKTLT MDIQKPRVLL IGKMYDEAGQ KLLEESTNIE ILSNPTLEEI NEAIQEVSGV
FVRYPNKLEA SSIRLAKQLK VISTSGFGTD SIDIMAATEQ GVIVVNNPGM STTSVAEHTL
SMILALAKKL PFLDHCVKKG NYLIRNQMQP IQLENKTLGI VGLGRIGTLV AHKCNLALGM
RVLAYDPYVP ASKAETVGAT WVKDLDVLLA ESDFVSLHTE LTSETREMFN ISVFKKMKPT
AFLINTSRGK VVCEKDLGIA LNQKLIAGCA LDVFEPEPPA LDNPLYNFEN VILSPHLAGV
TPEASLAAAV SAANQILQVL QGEKPPYMIN PEVWNLF
//
