ID A0A0L0FZD4_9EUKA Unreviewed; 553 AA.
AC A0A0L0FZD4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=SARC_06346 {ECO:0000313|EMBL:KNC81328.1};
OS Sphaeroforma arctica JP610.
OC Eukaryota; Ichthyosporea; Ichthyophonida; Sphaeroforma.
OX NCBI_TaxID=667725 {ECO:0000313|EMBL:KNC81328.1, ECO:0000313|Proteomes:UP000054560};
RN [1] {ECO:0000313|EMBL:KNC81328.1, ECO:0000313|Proteomes:UP000054560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP610 {ECO:0000313|EMBL:KNC81328.1,
RC ECO:0000313|Proteomes:UP000054560};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Young S.K., Zeng Q., Gargeya S., Alvarado L., Berlin A.,
RA Chapman S.B., Chen Z., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Howarth C., Mehta T., Neiman D.,
RA Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., White J., Yandava C., Burger G., Gray M.W., Holland P.W.H.,
RA King N., Lang F.B.F., Roger A.J., Ruiz-Trillo I., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Sphaeroforma arctica JP610.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+)
CC + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95;
CC Evidence={ECO:0000256|ARBA:ARBA00001878,
CC ECO:0000256|RuleBase:RU363003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 1/3. {ECO:0000256|ARBA:ARBA00005216,
CC ECO:0000256|RuleBase:RU363003}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU363003}.
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DR EMBL; KQ242045; KNC81328.1; -; Genomic_DNA.
DR RefSeq; XP_014155230.1; XM_014299755.1.
DR AlphaFoldDB; A0A0L0FZD4; -.
DR STRING; 667725.A0A0L0FZD4; -.
DR EnsemblProtists; KNC81328; KNC81328; SARC_06346.
DR GeneID; 25906850; -.
DR eggNOG; KOG0068; Eukaryota.
DR OrthoDB; 6392at2759; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000054560; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12173; PGDH_4; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR029009; ASB_dom_sf.
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 InterPro; IPR006236; PGDH.
DR InterPro; IPR045626; PGDH_ASB_dom.
DR NCBIfam; TIGR01327; PGDH; 1.
DR PANTHER; PTHR42938:SF22; D-3-PHOSPHOGLYCERATE DEHYDROGENASE; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF19304; PGDH_inter; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF143548; Serine metabolism enzymes domain; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW NAD {ECO:0000256|RuleBase:RU363003};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000054560};
KW Serine biosynthesis {ECO:0000256|RuleBase:RU363003}.
FT DOMAIN 480..552
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 553 AA; 58636 MW; 64AED5FF8E05DC91 CRC64;
MAVATNGEPQ QGMEVRKVLI SDPINPLCVK ILNDAGIEVD ARDKVPMDEL VKIISDYDAL
IVRSGTTVTA EVLAAGNLKI VGRAGTGVDN IDLDAATKAG TIVLNTPGGN TVSAAEHTCA
MLQSLCRFIP QSNEKLRAGK FDRKGGMGVE LHGKTIGIIG LGRIGREVAK RMQAFDVKTI
GYDPIMPKNV AAKFNIEAMD LDAVFAQSDF LTIHTPLTPQ TKGLLGEDAF KKCKKGFRVV
NCARGGIIDE EALLIALNDG VCAGAALDVF QEEPPMDSPI SSKLIAHPLV IATPHLGAST
KDAQVKVAVE IAESIVRATR GGALVGAVNA PKLVNAFSPE IKPYVALATK MGLIVSQVLG
GDAFLATNST IQSISLFAKG DLIKDMADVL KNALLTGLMS KLSDDPVNLI NAHHYAKDLD
FQINATGTDK IDDLPYKNVL SVSIDSADST HTYEGVVVAG APHLITINNF EIGAKPNGHV
LFYSNYNTPG VLGKVAGVCG AHNLNIFDFN MGEENNKKVH MSVLNVESPV TQEALKDIQA
IDGVLGVRYL DLE
//
