ID A0A3L7DVZ0_9GAMM Unreviewed; 340 AA.
AC A0A3L7DVZ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:RLQ20945.1};
DE EC=1.2.1.12 {ECO:0000313|EMBL:RLQ20945.1};
GN Name=gapA {ECO:0000313|EMBL:RLQ20945.1};
GN ORFNames=DWB85_15370 {ECO:0000313|EMBL:RLQ20945.1};
OS Seongchinamella sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Seongchinamella.
OX NCBI_TaxID=2283635 {ECO:0000313|EMBL:RLQ20945.1, ECO:0000313|Proteomes:UP000265509};
RN [1] {ECO:0000313|EMBL:RLQ20945.1, ECO:0000313|Proteomes:UP000265509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0301 {ECO:0000313|EMBL:RLQ20945.1,
RC ECO:0000313|Proteomes:UP000265509};
RA Ye M.-Q., Du Z.-J.;
RT "Halioglobus sp. genome submission.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RLQ20945.1}.
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DR EMBL; QRAN01000018; RLQ20945.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7DVZ0; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000265509; Unassembled WGS sequence.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 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 NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:RLQ20945.1}.
FT DOMAIN 2..154
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 181
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 340 AA; 37144 MW; 9B5D9C5AA59B038E CRC64;
MIRLAINGYG RIGRSVLRAL QESPLQAHMQ VVAINELADA GTVLHLTRYD STHGRFPREL
HGDDRQLVVA GQAIKLLRSA DIGALPWADL GIDLVLECTG AFTDRSTAEQ HLDRGAGRVL
FSQPAQPDVD ATVVFGINED ELRAEHRVVS AGSCTTNGIV PVIRALADTV GIESGTITTI
HSAMNDQPVL DAYHHTDLRK TRAASQSIIP VDTGLARGVE RVLPEMKGRF SAQALRVPTL
NVSAMDLTVQ TCRDTSVRAV NQALHEAAQS RFAGVLGYTE EPLASCDFNH DLRSSIIDAS
QTRVSGTRLV KVLTWFDNEW AYANRMLDVA HHWTSLEEKT
//
