ID A0A1H1WBF4_9PSED Unreviewed; 350 AA.
AC A0A1H1WBF4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=D-erythrose 4-phosphate dehydrogenase {ECO:0000313|EMBL:SDS94414.1};
GN ORFNames=SAMN05216221_3039 {ECO:0000313|EMBL:SDS94414.1};
OS Pseudomonas oryzae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1392877 {ECO:0000313|EMBL:SDS94414.1, ECO:0000313|Proteomes:UP000243359};
RN [1] {ECO:0000313|Proteomes:UP000243359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 32247 {ECO:0000313|Proteomes:UP000243359};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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DR EMBL; LT629751; SDS94414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1WBF4; -.
DR STRING; 1392877.SAMN05216221_3039; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000243359; Chromosome i.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0048001; F:erythrose-4-phosphate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006422; E4P_DH_bac.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01532; E4PD_g-proteo; 1.
DR PANTHER; PTHR43148:SF3; D-ERYTHROSE-4-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyridoxine biosynthesis {ECO:0000256|ARBA:ARBA00023096};
KW Reference proteome {ECO:0000313|Proteomes:UP000243359}.
FT DOMAIN 6..160
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 160
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 15..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 40
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 126
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 325
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 187
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 350 AA; 37991 MW; 52F09291B80F9DFD CRC64;
MPNRPYKVAL NGYGRIGRCV LRALYERGAD AALEIVALND LADQASIEYL TRFDSTHGRF
PGEVKVAGDC LHINGDCVKV LRQATPEAID WAALGVDLVL ECSGVYHSRA DGERFLAAGA
PRVLFSQPMA SEADVDATVV YGVNQASLSG AEKLLSNASC TTNCSVPLLK LLDEAIGLDY
VAITTIHSAM NDQPVIDAYH HEDLRRTRSA FQSVIPVSTG LARGIERLLP ELSGRVKAKA
IRVPTVNVSC LDITLQTRRD TSAAEINRVL REAAASGPLQ GLVAYTELPH ASCDFNHDPH
SAIVDGSQTL VSGPRLVNLL AWFDNEWGFA NRMLDVAEHF LRVAHRPQPM
//