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Database: UniProt
Entry: A0A1H1WBF4_9PSED
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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
//
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