ID I4NAV6_9PSED Unreviewed; 352 AA.
AC I4NAV6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=D-erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:EIK98596.1};
GN ORFNames=PMM47T1_01120 {ECO:0000313|EMBL:EIK98596.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK98596.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK98596.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK98596.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(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:EIK98596.1}.
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DR EMBL; AJWX01000001; EIK98596.1; -; Genomic_DNA.
DR RefSeq; WP_008364973.1; NZ_AJWX01000001.1.
DR AlphaFoldDB; I4NAV6; -.
DR STRING; 1179778.PMM47T1_01120; -.
DR PATRIC; fig|1179778.3.peg.227; -.
DR eggNOG; COG0057; Bacteria.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000004339; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004339}.
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 352 AA; 38534 MW; 5A1C2BA1B0E3DFF6 CRC64;
MPQPRPYKVA LNGYGRIGRC VMRALYERGA EAGFEVVAIN DLADMASLEY LTRFDSTHGR
FPGQVRSEGD CLMINGDCVK VLRSATPEGI DWAALDVDLV LECSGAWHTR ADGQRFLDAG
APRVLFSQPM ASETDVDATV VFGINQEVLT GTERLVSNAS CTTNCSVPLL RLLDEALGLE
YISITTIHSA MNDQPVIDAY HAEDLRRTRS AFQSIIPVST GLARGIERLL PELGGRIQAK
AVRVPTVNVS CLDITLQVTR DTDAAEVNRI LHDAALSGPL KGLVAYTELP HASCDFNHDP
HSAIVDASQT RVSGPRLVNI LAWFDNEWGF ANRMLDVADH FLYVVNQQLK QA
//
