ID C5KDC3_PERM5 Unreviewed; 318 AA.
AC C5KDC3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=D-3-phosphoglycerate dehydrogenase, putative {ECO:0000313|EMBL:EER17556.1};
GN ORFNames=Pmar_PMAR008118 {ECO:0000313|EMBL:EER17556.1};
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:EER17556.1, 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; GG672055; EER17556.1; -; Genomic_DNA.
DR RefSeq; XP_002785760.1; XM_002785714.1.
DR AlphaFoldDB; C5KDC3; -.
DR EnsemblProtists; EER17556; EER17556; Pmar_PMAR008118.
DR GeneID; 9062894; -.
DR InParanoid; C5KDC3; -.
DR OMA; EDICFAR; -.
DR OrthoDB; 4204864at2759; -.
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 31..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 126..243
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 318 AA; 34559 MW; 49469DCF0710248F CRC64;
MTAHTVLLAT TKPFAKDAVA AIKTICEEHG LVFDKLEGYK DRAELYAAVA SAEACIVRSD
VCDEEFFSHA KKLKVLVRAG AGVDAIDLAA ATRHGVCVQN TPGQNSNAVA ELAFGMLLAH
KRNYFDGNSG TEIRGSSLGL YGCGNVSRFM ILAAQGFGMD IYAYDPFLTP DQITDLGAEP
LYDVPSIFKC DVVSLHVPST RETKHSIDEK LLRSMPKGGV LINTARKNIV QEADLLKALV
DRPDLSYLAD DKPDNTEEIK ESLGEVRVKK QFLVTPKKMG AQTAEANSNS GIAAAKQVVE
FFRDNLVKHQ VNVNGKHF
//
