ID A0A1H9FYW4_9LACT Unreviewed; 335 AA.
AC A0A1H9FYW4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00021022};
GN ORFNames=SAMN04488558_11072 {ECO:0000313|EMBL:SEQ43021.1};
OS Ignavigranum ruoffiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Ignavigranum.
OX NCBI_TaxID=89093 {ECO:0000313|EMBL:SEQ43021.1, ECO:0000313|Proteomes:UP000198833};
RN [1] {ECO:0000313|EMBL:SEQ43021.1, ECO:0000313|Proteomes:UP000198833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15695 {ECO:0000313|EMBL:SEQ43021.1,
RC ECO:0000313|Proteomes:UP000198833};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; FOEN01000010; SEQ43021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9FYW4; -.
DR STRING; 89093.SAMN04488558_11072; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000198833; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:SF6; GLYCERALDEHYDE-3-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|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198833}.
FT DOMAIN 3..153
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 153
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 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 335 AA; 36666 MW; 7019C493CAB5623A CRC64;
MTTRVAINGF GRIGRLALRR ILEIDTDLEI VGINSTTDSE QLAYLFMFDT VYGRVPYSVE
ARPGELIIDG KTIKVYTERD AAKIPWGELD VDIVLECTGI FLKAEQCQAH IDAGAKHVVI
SAPAKDETTK LIVFGINEDI IDPEDRIISS ASCSTNCLAP MAKVLHEQFG LISGVMSTIH
AYTASQFVLD KRTKTYRGGR AAAMNIIPYK TGAAKAVGKV IPELEGIVDG TAMRVPVATG
SVIEFYSNLE KEVTVEEINA AMKAASNPAF EYNEYQIVSS DIIGSTAGSV FDATLTKIVD
NDGDQLVKTV AWYDNEYGYT CNMIRLVEYY ADLIK
//
