G3P_METJA
ID G3P_METJA Reviewed; 343 AA.
AC Q58546;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
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; OrderedLocusNames=MJ1146;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L77117; AAB99147.1; -; Genomic_DNA.
DR PIR; A64443; A64443.
DR RefSeq; WP_010870657.1; NC_000909.1.
DR PDB; 2YYY; X-ray; 1.85 A; A/B=1-343.
DR PDBsum; 2YYY; -.
DR AlphaFoldDB; Q58546; -.
DR SMR; Q58546; -.
DR STRING; 243232.MJ_1146; -.
DR EnsemblBacteria; AAB99147; AAB99147; MJ_1146.
DR GeneID; 1452042; -.
DR KEGG; mja:MJ_1146; -.
DR eggNOG; arCOG00493; Archaea.
DR HOGENOM; CLU_069533_0_0_2; -.
DR InParanoid; Q58546; -.
DR OMA; NAIVPNP; -.
DR OrthoDB; 32079at2157; -.
DR PhylomeDB; Q58546; -.
DR BRENDA; 1.2.1.59; 3260.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; Q58546; -.
DR Proteomes; UP000000805; 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; Glycolysis; NAD; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..343
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145723"
FT ACT_SITE 144
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143..145
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 198..199
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 24..36
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:2YYY"
FT TURN 101..106
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2YYY"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 144..157
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 160..174
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 226..236
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2YYY"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:2YYY"
FT TURN 307..311
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:2YYY"
FT HELIX 329..340
FT /evidence="ECO:0007829|PDB:2YYY"
SQ SEQUENCE 343 AA; 38102 MW; 81EB5810A9C838C5 CRC64;
MPAKVLINGY GSIGKRVADA VSMQDDMEVI GVTKTKPDFE ARLAVEKGYK LFVAIPDNER
VKLFEDAGIP VEGTILDIIE DADIVVDGAP KKIGKQNLEN IYKPHKVKAI LQGGEKAKDV
EDNFNALWSY NRCYGKDYVR VVSCNTTGLC RILYAINSIA DIKKARIVLV RRAADPNDDK
TGPVNAITPN PVTVPSHHGP DVVSVVPEFE GKILTSAVIV PTTLMHMHTL MVEVDGDVSR
DDILEAIKKT PRIITVRAED GFSSTAKIIE YGRDLGRLRY DINELVVWEE SINVLENEIF
LMQAVHQESI VIPENIDCIR AMLQMEEDNF KSIEKTNKAM GIQ
