G3P_SACS2
ID G3P_SACS2 Reviewed; 340 AA.
AC P39460;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.59;
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
GN Name=gap; Synonyms=agaPD; OrderedLocusNames=SSO0528; ORFNames=C22_023;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=DSM 5833 / MT-4;
RX PubMed=8259927; DOI=10.1007/bf00557333;
RA Arcari P., Russo A.D., Ianniciello G., Gallo M., Bocchini V.;
RT "Nucleotide sequence and molecular evolution of the gene coding for
RT glyceraldehyde-3-phosphate dehydrogenase in the thermoacidophilic
RT archaebacterium Sulfolobus solfataricus.";
RL Biochem. Genet. 31:241-251(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8521845; DOI=10.1111/j.1432-1033.1995.800_3.x;
RA Jones C.E., Fleming T.M., Cowan D.A., Littlechild J.A., Piper P.W.;
RT "The phosphoglycerate kinase and glyceraldehyde-3-phosphate dehydrogenase
RT genes from the thermophilic archaeon Sulfolobus solfataricus overlap by 8-
RT bp. Isolation, sequencing of the genes and expression in Escherichia
RT coli.";
RL Eur. J. Biochem. 233:800-808(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=10701121; DOI=10.1139/g99-108;
RA Charlebois R.L., Singh R.K., Chan-Weiher C.C.-Y., Allard G., Chow C.,
RA Confalonieri F., Curtis B., Duguet M., Erauso G., Faguy D., Gaasterland T.,
RA Garrett R.A., Gordon P., Jeffries A.C., Kozera C., Kushwaha N., Lafleur E.,
RA Medina N., Peng X., Penny S.L., She Q., St Jean A., van der Oost J.,
RA Young F., Zivanovic Y., Doolittle W.F., Ragan M.A., Sensen C.W.;
RT "Gene content and organization of a 281-kbp contig from the genome of the
RT extremely thermophilic archaeon, Sulfolobus solfataricus P2.";
RL Genome 43:116-136(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
RX PubMed=10448043; DOI=10.1006/jmbi.1999.3003;
RA Isupov M.N., Fleming T.M., Dalby A.R., Crowhurst G.S., Bourne P.C.,
RA Littlechild J.A.;
RT "Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the
RT hyperthermophilic archaeon Sulfolobus solfataricus.";
RL J. Mol. Biol. 291:651-660(1999).
CC -!- FUNCTION: Can use both NAD and NADP as cofactors, but exhibits a marked
CC preference for NADP.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X66409; CAA47040.1; -; Genomic_DNA.
DR EMBL; X80178; CAA56460.1; -; Genomic_DNA.
DR EMBL; Y18930; CAB57771.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK40848.1; -; Genomic_DNA.
DR PIR; S51230; S51230.
DR PIR; S63529; S63529.
DR RefSeq; WP_009991048.1; NC_002754.1.
DR PDB; 1B7G; X-ray; 2.05 A; O/Q=1-340.
DR PDBsum; 1B7G; -.
DR AlphaFoldDB; P39460; -.
DR SMR; P39460; -.
DR STRING; 273057.SSO0528; -.
DR EnsemblBacteria; AAK40848; AAK40848; SSO0528.
DR GeneID; 44129550; -.
DR KEGG; sso:SSO0528; -.
DR PATRIC; fig|273057.12.peg.527; -.
DR eggNOG; arCOG00493; Archaea.
DR HOGENOM; CLU_069533_0_0_2; -.
DR InParanoid; P39460; -.
DR OMA; NAIVPNP; -.
DR PhylomeDB; P39460; -.
DR BRENDA; 1.2.1.12; 6163.
DR BRENDA; 1.2.1.13; 6163.
DR SABIO-RK; P39460; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P39460; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR InterPro; IPR000846; DapB_N.
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; IPR006436; Glyceraldehyde-3-P_DH_2_arc.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01113; DapB_N; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01546; GAPDH-II_archae; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW Glycolysis; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..340
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145735"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138..140
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 193..194
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT DISULFID 123..149
FT CONFLICT 48
FT /note="I -> Y (in Ref. 1; CAA47040)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="V -> AL (in Ref. 1; CAA47040)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..73
FT /note="ED -> DY (in Ref. 1; CAA47040)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="K -> N (in Ref. 1; CAA47040)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1B7G"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 139..152
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 157..169
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 219..229
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:1B7G"
FT TURN 300..303
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 304..315
FT /evidence="ECO:0007829|PDB:1B7G"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:1B7G"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1B7G"
SQ SEQUENCE 340 AA; 37596 MW; 609C9260C3062B6D CRC64;
MINVAVNGYG TIGKRVADAI IKQPDMKLVG VAKTSPNYEA FIAHRRGIRI YVPQQSIKKF
EESGIPVAGT VEDLIKTSDI VVDTTPNGVG AQYKPIYLQL QRNAIFQGGE KAEVADISFS
ALCNYNEALG KKYIRVVSCN TTALLRTICT VNKVSKVEKV RATIVRRAAD QKEVKKGPIN
SLVPDPATVP SHHAKDVNSV IRNLDIATMA VIAPTTLMHM HFINITLKDK VEKKDILSVL
ENTPRIVLIS SKYDAEATAE LVEVARDLKR DRNDIPEVMI FSDSIYVKDD EVMLMYAVHQ
ESIVVPENID AIRASMKLMS AEDSMRITNE SLGILKGYLI
