ID J3IP79_9PSED Unreviewed; 350 AA.
AC J3IP79;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:EJN31943.1};
GN ORFNames=PMI37_02431 {ECO:0000313|EMBL:EJN31943.1};
OS Pseudomonas sp. GM80.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144339 {ECO:0000313|EMBL:EJN31943.1, ECO:0000313|Proteomes:UP000007301};
RN [1] {ECO:0000313|EMBL:EJN31943.1, ECO:0000313|Proteomes:UP000007301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM80 {ECO:0000313|EMBL:EJN31943.1,
RC ECO:0000313|Proteomes:UP000007301};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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:EJN31943.1}.
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DR EMBL; AKJD01000067; EJN31943.1; -; Genomic_DNA.
DR RefSeq; WP_008081035.1; NZ_AKJD01000067.1.
DR AlphaFoldDB; J3IP79; -.
DR PATRIC; fig|1144339.3.peg.2278; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000007301; Unassembled WGS sequence.
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}.
FT DOMAIN 7..161
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 41
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 127
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 188
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 350 AA; 38179 MW; 47938CA0D250D37D CRC64;
MPQPRPYKVA LNGYGRIGRC VLRALFERGE KAGFEIVAIN DLADMASIEY LTRFDSTHGR
FPGKVRVEGD CLHINGDCVK VLRSATPEGI DWASLGVDLV LECSGAYNTR EDGQRFLDAG
APRVLFSQPM ASEADVDATI VYGVNQDCLT GDELLVSNAS CTTNCGVPLL RLLDKAIGLD
YVSITTIHSA MNDQPVIDAY HHEDLRRTRS AFQSVIPVST GLARGIERLL PELAGRIQAK
AVRVPTVNVS CLDITMQTAT ATDANEVNRI LREAATTGPL KGLLAYTELP HASCDFNHDP
HSAIVDASQT RVSGPKLVNI LAWFDNEWGF ANRMLDVAEH YLQTAISKKP
//
