GAPN_STRMU
ID GAPN_STRMU Reviewed; 475 AA.
AC Q59931;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE EC=1.2.1.9;
DE AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)];
DE AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE AltName: Full=Triosephosphate dehydrogenase;
GN Name=gapN; OrderedLocusNames=SMU_676;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NG5 / Serotype c;
RX PubMed=7751269; DOI=10.1128/jb.177.10.2622-2627.1995;
RA Boyd D.A., Cvitkovitch D.G., Hamilton I.R.;
RT "Sequence, expression, and function of the gene for the nonphosphorylating,
RT NADP-dependent glyceraldehyde-3-phosphate dehydrogenase of Streptococcus
RT mutans.";
RL J. Bacteriol. 177:2622-2627(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) IN COMPLEX WITH NADP, AND
RP HOMOTETRAMERIZATION.
RX PubMed=10388564; DOI=10.1006/jmbi.1999.2853;
RA Cobessi D., Tete-Favier F., Marchal S., Azza S., Branlant G., Aubry A.;
RT "Apo and holo crystal structures of an NADP-dependent aldehyde
RT dehydrogenase from Streptococcus mutans.";
RL J. Mol. Biol. 290:161-173(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE.
RX PubMed=10864505; DOI=10.1006/jmbi.2000.3824;
RA Cobessi D., Tete-Favier F., Marchal S., Branlant G., Aubry A.;
RT "Structural and biochemical investigations of the catalytic mechanism of an
RT NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.";
RL J. Mol. Biol. 300:141-152(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, AND
RP CHARACTERIZATION.
RX PubMed=16958622; DOI=10.1042/bj20060843;
RA Pailot A., D'Ambrosio K., Corbier C., Talfournier F., Branlant G.;
RT "Invariant Thr244 is essential for the efficient acylation step of the non-
RT phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus
RT mutans.";
RL Biochem. J. 400:521-530(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-
CC phosphoglycerate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58272, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.9;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10388564,
CC ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; L38521; AAA91091.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58410.1; -; Genomic_DNA.
DR PIR; A57151; A57151.
DR RefSeq; NP_721104.1; NC_004350.2.
DR RefSeq; WP_002262986.1; NC_004350.2.
DR PDB; 1EUH; X-ray; 1.82 A; A/B/C/D=1-475.
DR PDB; 1QI1; X-ray; 3.00 A; A/B/C/D=1-475.
DR PDB; 1QI6; X-ray; 2.50 A; A/B/C/D=1-475.
DR PDB; 2ESD; X-ray; 2.55 A; A/B/C/D=1-475.
DR PDB; 2EUH; X-ray; 2.60 A; A/B/C/D=1-475.
DR PDB; 2ID2; X-ray; 2.50 A; A/B/C/D=1-475.
DR PDB; 2QE0; X-ray; 2.19 A; A/B/C/D=1-475.
DR PDBsum; 1EUH; -.
DR PDBsum; 1QI1; -.
DR PDBsum; 1QI6; -.
DR PDBsum; 2ESD; -.
DR PDBsum; 2EUH; -.
DR PDBsum; 2ID2; -.
DR PDBsum; 2QE0; -.
DR AlphaFoldDB; Q59931; -.
DR SMR; Q59931; -.
DR STRING; 210007.SMU_676; -.
DR DrugBank; DB02263; D-glyceraldehyde 3-phosphate.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR PRIDE; Q59931; -.
DR EnsemblBacteria; AAN58410; AAN58410; SMU_676.
DR KEGG; smu:SMU_676; -.
DR PATRIC; fig|210007.7.peg.601; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_1_0_9; -.
DR OMA; PMPIAAW; -.
DR PhylomeDB; Q59931; -.
DR BioCyc; MetaCyc:MON-13095; -.
DR BRENDA; 1.2.1.9; 5941.
DR SABIO-RK; Q59931; -.
DR EvolutionaryTrace; Q59931; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IDA:CACAO.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..475
FT /note="NADP-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000056579"
FT ACT_SITE 250
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10864505"
FT BINDING 151
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10388564,
FT ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622"
FT BINDING 154..155
FT /ligand="substrate"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10388564,
FT ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622"
FT BINDING 180
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10388564,
FT ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622"
FT BINDING 215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10388564,
FT ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622"
FT BINDING 230..251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10388564,
FT ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622"
FT BINDING 283..285
FT /ligand="substrate"
FT BINDING 377
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10388564,
FT ECO:0000269|PubMed:10864505, ECO:0000269|PubMed:16958622"
FT BINDING 437
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10864505"
FT CONFLICT 58
FT /note="S -> A (in Ref. 1; AAA91091)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="V -> I (in Ref. 1; AAA91091)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> T (in Ref. 1; AAA91091)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1EUH"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 39..58
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 94..115
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1QI6"
FT HELIX 158..169
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:1EUH"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2ESD"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:1EUH"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 255..259
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 284..293
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 328..343
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:2QE0"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 380..389
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 391..400
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 401..410
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1EUH"
FT HELIX 457..463
FT /evidence="ECO:0007829|PDB:1EUH"
FT STRAND 465..473
FT /evidence="ECO:0007829|PDB:1EUH"
SQ SEQUENCE 475 AA; 51194 MW; F0A2770AB89552DC CRC64;
MTKQYKNYVN GEWKLSENEI KIYEPASGAE LGSVPAMSTE EVDYVYASAK KAQPAWRSLS
YIERAAYLHK VADILMRDKE KIGAVLSKEV AKGYKSAVSE VVRTAEIINY AAEEGLRMEG
EVLEGGSFEA ASKKKIAVVR REPVGLVLAI SPFNYPVNLA GSKIAPALIA GNVIAFKPPT
QGSISGLLLA EAFAEAGLPA GVFNTITGRG SEIGDYIVEH QAVNFINFTG STGIGERIGK
MAGMRPIMLE LGGKDSAIVL EDADLELTAK NIIAGAFGYS GQRCTAVKRV LVMESVADEL
VEKIREKVLA LTIGNPEDDA DITPLIDTKS ADYVEGLIND ANDKGAAALT EIKREGNLIC
PILFDKVTTD MRLAWEEPFG PVLPIIRVTS VEEAIEISNK SEYGLQASIF TNDFPRAFGI
AEQLEVGTVH INNKTQRGTD NFPFLGAKKS GAGIQGVKYS IEAMTTVKSV VFDIK
