ID A0A1N6EUH6_9RHOB Unreviewed; 332 AA.
AC A0A1N6EUH6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Glyceraldehyde 3-phosphate dehydrogenase {ECO:0000313|EMBL:SIN86739.1};
GN ORFNames=SAMN05444002_1118 {ECO:0000313|EMBL:SIN86739.1};
OS Vannielia litorea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Vannielia.
OX NCBI_TaxID=1217970 {ECO:0000313|EMBL:SIN86739.1, ECO:0000313|Proteomes:UP000184932};
RN [1] {ECO:0000313|Proteomes:UP000184932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29440 {ECO:0000313|Proteomes:UP000184932};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR EMBL; FSRL01000001; SIN86739.1; -; Genomic_DNA.
DR RefSeq; WP_074255223.1; NZ_FSRL01000001.1.
DR AlphaFoldDB; A0A1N6EUH6; -.
DR STRING; 1217970.SAMN05444002_1118; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000184932; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; 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 Reference proteome {ECO:0000313|Proteomes:UP000184932}.
FT DOMAIN 3..151
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 332 AA; 35709 MW; 1B0EC91E559AA6D5 CRC64;
MTITIGINGF GRIGRCTLAH IAESARNDVQ VVRINAPGDI ETHAHLLRYD SVHGRFPGEV
RVKDKAIDLG RGPIDVMSSY DPAELDWGGC DVVLECTGTF NDGHKSAIHL QRGAGKVLIS
APASNVDRTV VYGVNHRALR PTERMVSNGS CTTNCLAPLA KVLNDAIGIE QGLMTTIHSY
TGDQPTLDRR HKDLYRARAA AMAMIPTSTG AAKALGEVLP ELAGKLDGTA MRVPTPNVSA
VDLTFTAARD VSVDNVNEVV REACAGHMGM VMAYDPAPKV SIDFNHTPQS SIFAPDQTKV
VGRLVRVLAW YDNEWGFSAR MADVAGHMGR LN
//
