ID A0A232ENJ9_9HYME Unreviewed; 1323 AA.
AC A0A232ENJ9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000256|RuleBase:RU363003};
DE EC=1.1.1.95 {ECO:0000256|RuleBase:RU363003};
GN ORFNames=TSAR_001015 {ECO:0000313|EMBL:OXU19907.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU19907.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU19907.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU19907.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU19907.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU363003}.
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:OXU19907.1}.
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DR EMBL; NNAY01003149; OXU19907.1; -; Genomic_DNA.
DR STRING; 543379.A0A232ENJ9; -.
DR UniPathway; UPA00135; UER00196.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006564; P:L-serine 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; IPR028005; AcTrfase_ESCO_Znf_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; IPR028009; ESCO_Acetyltransf_dom.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006236; PGDH.
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; PF13880; Acetyltransf_13; 1.
DR Pfam; PF13878; zf-C2H2_3; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU363003};
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|RuleBase:RU363003};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU363003};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Serine biosynthesis {ECO:0000256|ARBA:ARBA00023299,
KW ECO:0000256|RuleBase:RU363003};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 703..857
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1323 AA; 144161 MW; ED9B9E6E212E902F CRC64;
MNEIVPESPD KETDAEDEST YVPETPQKDG SPQIKSPIII RKSLGVLDNN VSVLEDNANI
QSPKSRRGTE NRISTSASKK SAKLRSYRKD RHSNLHKVKV SLFHSRFKEN EPEKPSFYVS
AKSFYGSSCR KAPESYALAP VTLKPVSRHS SKKKRSPDAQ PLVKKKSPAQ PAAMKKHKRK
GEINCGVGHG IKKPKRKRSS LKNDSMDSDK SLSDKQNSSA VEERIPIEAH IDQIENFDSN
NVTESTTVET YDPKRKFFKH NRRTVEKPVK SSTTVSPLTE SQDTDIPIHE SIGKITCADK
TIAVAEKPAT KTTGCAGTIS HLGLCEKNGQ LMIKPLISQK DIDDWNKLSA VDITDFDISM
TNISNLDSID PVQDILKELE DVWADTSVTQ TVSMNAVNNF SKGSNNDAQD VNSVNENSSI
NLGLNNVINL PVEDLVPADS DLIEDADTSY ESIVISLGLN DTVNLPMGNS LSESTSSIIE
SRKTNSSSYK NTNKEIDQTA TNSASVLLNS VENIASKSVS QKDVSDLLSI LQNEWSEDEE
PIGNSTSVVS DTSFPLETNE NVYNSTMFEE NIVETTTNDT TESQNCGELS EQTSKKYYPL
FSKGSSFGIV TDTTVKSKKM NENRVLLNHS SDPKQYQIDA GQKLFGIIQC KKCELLYHLG
DKDDENTHIK YHNRWKKGLG LNFQGWKNEH IVFQDSNTKS KIILIEPSDP MNHRKKVLDI
LQIINQDLGI IELDSSDYVN DKAYLYVRNK SIIGLLISKR IHSAFKIIPE MSELNCCSSE
SSPAKCGINV IWTAEHHRRQ GIATKLVDTL RNMSVNLRSV LVSDPVDERC AALLTSHGVP
VTTKYKLSKE ELINELQKHD GLIVRSETKV TADVIAASPN LKLVGRAGTG VDNIDIPAAT
RNGILVLNTP GGNSVSACEL TCAVISALAR NVVQAGQSMK EGRWDRKLYA GRELSGKALG
VVGFGRIGRE VAHRMKAFGM EIIAYDPFFT KEQAAEIGVT KGELEDIWKN ADYITVHTPL
IPQTRNLINA STLAKCKKGV YIVNVARGGI VDEEALLHSI NAGHVAGAAL DVFIEEPPKN
PVTLELIKHP KVVATPHLGA STAEAQTRVA IEIAEQFLAI SGKSDKYSVT GIVNAPVMAA
AANPDNAAWI ELAKRLGKVA GKFVANQGQV VVESRTTGPD TASKKFVHTA LNVGLLANRV
NSGLNLVNAP NLAKELGITV NEGHENVGQN AIVVKAGGHV VQGTVVGNAT LLVSIDDSVF
VDGVHLQDNI SLYKAKSAQD LAQVVAAHVA KGVAINNVSI AGNWIIVQTN KPVSLAVDGV
ESY
//
