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Database: UniProt
Entry: C5L617_PERM5
LinkDB: C5L617_PERM5
Original site: C5L617_PERM5 
ID   C5L617_PERM5            Unreviewed;       282 AA.
AC   C5L617;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase, putative {ECO:0000313|EMBL:EER07826.1};
DE   Flags: Fragment;
GN   ORFNames=Pmar_PMAR026206 {ECO:0000313|EMBL:EER07826.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EER07826.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) 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; GG679674; EER07826.1; -; Genomic_DNA.
DR   RefSeq; XP_002776010.1; XM_002775964.1.
DR   AlphaFoldDB; C5L617; -.
DR   EnsemblProtists; EER07826; EER07826; Pmar_PMAR026206.
DR   GeneID; 9043033; -.
DR   InParanoid; C5L617; -.
DR   OrthoDB; 179007at2759; -.
DR   Proteomes; UP000007800; 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:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
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; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT   DOMAIN          18..111
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..244
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EER07826.1"
FT   NON_TER         282
FT                   /evidence="ECO:0000313|EMBL:EER07826.1"
SQ   SEQUENCE   282 AA;  30833 MW;  D9FB91C4CFF78D43 CRC64;
     LLSSPFNKIA VDGIEKICKD NGLTFGKIEG YKTQEELYSA AESAEACIVR SDKLDEEFFN
     RAKNLKIVVR AGAGVDTIDL DAASKHHVVV ENTPGQNANA VAEMVFALLI AMKRNHFDAT
     SGREIRGSTL GLYGCGNVSR AMIEVSKGFA MKCYSYDPFL SDEQIKECGA EPLHDLKELF
     KCDIVSLHVP ATPQTINSIN EDLMSLMPEN GVLVDAARSE VIDEDSVISI FQKRPDLGYI
     SDVGFTKIDE LREKIGAAQL KKQLIVTPKK MGAQTLESNV NA
//
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