ID A0A368TTA0_9GAMM Unreviewed; 345 AA.
AC A0A368TTA0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Erythrose-4-phosphate dehydrogenase {ECO:0000313|EMBL:RCV87850.1};
DE EC=1.2.1.12 {ECO:0000313|EMBL:RCV87850.1};
GN Name=gapA {ECO:0000313|EMBL:RCV87850.1};
GN ORFNames=DU506_15995 {ECO:0000313|EMBL:RCV87850.1};
OS Halomonas rituensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=2282306 {ECO:0000313|EMBL:RCV87850.1, ECO:0000313|Proteomes:UP000253204};
RN [1] {ECO:0000313|EMBL:RCV87850.1, ECO:0000313|Proteomes:UP000253204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TQ8S {ECO:0000313|EMBL:RCV87850.1,
RC ECO:0000313|Proteomes:UP000253204};
RA Lu H., Xing P., Wu Q.;
RT "Halomonas rutogse sp. nov., isolated from Lake TangqianCo on Tibetan
RT Plateau.";
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:RCV87850.1}.
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DR EMBL; QPIJ01000046; RCV87850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368TTA0; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000253204; 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; IPR020830; GlycerAld_3-P_DH_AS.
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.
DR PROSITE; PS00071; GAPDH; 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:RCV87850.1}.
FT DOMAIN 8..159
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 159
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 17..18
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 323
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 186
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 345 AA; 37994 MW; 52057BDA442B3C04 CRC64;
MAYSPSVFRI AINGYGRIGQ CVLRALVELG DTDIEVVAIN ELSDLATITY LTRYDTTHGR
FPGHVESRDG DLIVNGRPIR VLCEPDPERL PWKALDIDLV LECSGSFKDR HTAEKHIEAG
AKQLLFSQPA ESDVDATIVR GINDHSLSRS QRILSAASCT TNCLIPVLTV LDEALGLAHG
VTTTIHSAMN DQPVIDAYHQ TDLRLTRSAM HSIVPVDTNL ALGINRLMPH LAGRFECLHM
RVPTINVSAM DMSLCVNRQT SASEVNALLR QASRERLVGV LGYTEEPMAS SDFNHDPRSG
IVDATQTRVA GGQLVKLLCW FDNEWGFANR MLDIGRQLAK LPPTY
//
