ID I1ZP68_STRPA Unreviewed; 345 AA.
AC I1ZP68;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00021022, ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN Name=gapA {ECO:0000313|EMBL:AFJ26842.1};
GN ORFNames=Spaf_1898 {ECO:0000313|EMBL:AFJ26842.1};
OS Streptococcus parasanguinis FW213.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1114965 {ECO:0000313|EMBL:AFJ26842.1, ECO:0000313|Proteomes:UP000002865};
RN [1] {ECO:0000313|EMBL:AFJ26842.1, ECO:0000313|Proteomes:UP000002865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW213 {ECO:0000313|EMBL:AFJ26842.1,
RC ECO:0000313|Proteomes:UP000002865};
RX PubMed=22529932; DOI=10.1371/journal.pone.0034769;
RA Geng J., Chiu C.H., Tang P., Chen Y., Shieh H.R., Hu S., Chen Y.Y.;
RT "Complete Genome and Transcriptomes of Streptococcus parasanguinis FW213:
RT Phylogenic Relations and Potential Virulence Mechanisms.";
RL PLoS ONE 7:E34769-E34769(2012).
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; CP003122; AFJ26842.1; -; Genomic_DNA.
DR AlphaFoldDB; I1ZP68; -.
DR STRING; 1114965.Spaf_1898; -.
DR PaxDb; 1114965-Spaf_1898; -.
DR KEGG; scf:Spaf_1898; -.
DR PATRIC; fig|1114965.3.peg.1816; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_3_9; -.
DR Proteomes; UP000002865; Chromosome.
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; 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; 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.
DR PROSITE; PS00071; GAPDH; 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 ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 12..161
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 21..22
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 43
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 87
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 160..162
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 191
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 221..222
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 244
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 325
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 188
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 345 AA; 37106 MW; 7B70B3C1A738EF6D CRC64;
MIFIRRKSRM VVKVGINGFG RIGRLAFRRI QNVEGVEVTR INDLTDPVML AHLLKYDTTQ
GRFDGTVEVK EGGFEVNGKF VKVSAERDPE QIDWANDGVE IVLEATGFFA TKAAAEKHLH
AGGAKKVVIT APGGSDVKTV VFNTNHDILD GTETVISGAS CTTNCLAPMA KALQDNFGVV
EGLMTTIHAY TGDQMILDGP HRKGDLRRAR AGAANIVPNS TGAAKAIGLV IPELNGKLDG
AAQRVPTPTG SVTELVVVLE KNVTVDEVNA AMKAVANESY GYTEDPIVSS DVVGMSYGSL
FDATQTKVLD VDGKQLVKVV SWYDNEMSYT AQLVRTLEYF AKIAK
//
