ID D5LT80_STAHA Unreviewed; 273 AA.
AC D5LT80;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00030823};
DE Flags: Fragment;
GN Name=gap {ECO:0000313|EMBL:ADF49529.1};
OS Staphylococcus haemolyticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1283 {ECO:0000313|EMBL:ADF49529.1};
RN [1] {ECO:0000313|EMBL:ADF49529.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ShlNN894 {ECO:0000313|EMBL:ADF49529.1};
RA Voronina O.L., Kunda M.S., Subbotina M.E., Lunin V.G.;
RT "Species differences of coagulase-negative Staphylococci from hospitals
RT demonstrated by genotyping.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC NAD. The first reaction step involves the formation of a hemiacetal
CC intermediate between G3P and a cysteine residue, and this hemiacetal
CC intermediate is then oxidized to a thioester, with concomitant
CC reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC second NAD, and the thioester is attacked by a nucleophilic inorganic
CC phosphate to produce BPG. {ECO:0000256|ARBA:ARBA00003501}.
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 -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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DR EMBL; GU968744; ADF49529.1; -; Genomic_DNA.
DR AlphaFoldDB; D5LT80; -.
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: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 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..126
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADF49529.1"
FT NON_TER 273
FT /evidence="ECO:0000313|EMBL:ADF49529.1"
SQ SEQUENCE 273 AA; 29041 MW; C2955CC057D4CA9C CRC64;
GIEVVAVNDL TDDEMLAHLL KYDTMQGRFT GEVEVVDGGF RVNGKEVKSY EEPDASKLPW
GDLDIDVVLE CTGFYTDKEK AEAHINAGAK KVLISAPAKG DVKTIVFNTN HNDLDGSETV
VSGASCTTNS LAPVAKVLSD EFGLVEGLMT TIHAYTGDQM TQDGPHKKGD KRRARAAAQN
IVPNSTGAAK AIGKVIPEID GKLDGGAQRV PVATGSLTEV TVVLEKDVTV EDVNKAMKNA
SNESFGYTED EIVSSDVVGM TYGSLFDATQ TRV
//
