ID Q18MU0_AERPX Unreviewed; 346 AA.
AC Q18MU0;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 13-SEP-2023, entry version 99.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
DE Short=GAPDH {ECO:0000256|HAMAP-Rule:MF_00559};
DE EC=1.2.1.59 {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00559};
GN Name=gapA {ECO:0000313|EMBL:BAE96802.1};
GN Synonyms=gap {ECO:0000256|HAMAP-Rule:MF_00559};
OS Aeropyrum pernix.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=56636 {ECO:0000313|EMBL:BAE96802.1};
RN [1] {ECO:0000313|EMBL:BAE96802.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2 {ECO:0000313|EMBL:BAE96798.1}, TA3
RC {ECO:0000313|EMBL:BAE96799.1}, TA4 {ECO:0000313|EMBL:BAE96800.1}, TA5
RC {ECO:0000313|EMBL:BAE96801.1}, TA6 {ECO:0000313|EMBL:BAE96802.1}, YK2
RC {ECO:0000313|EMBL:BAE96793.1}, YK3 {ECO:0000313|EMBL:BAE96794.1}, YK4
RC {ECO:0000313|EMBL:BAE96795.1}, and YK5 {ECO:0000313|EMBL:BAE96796.1};
RA Tanaka R., Hutami N., Creenverk I., Vancaniet M., Swings J., Sako Y.;
RT "Genomic diversity of hyperthermophilic archaeon Aeropyrum pernix isolated
RT from different geographical environment.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00001820, ECO:0000256|HAMAP-
CC Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
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 Evidence={ECO:0000256|ARBA:ARBA00001295, ECO:0000256|HAMAP-
CC Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869,
CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
CC ECO:0000256|RuleBase:RU003388}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|HAMAP-Rule:MF_00559,
CC ECO:0000256|RuleBase:RU003388}.
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DR EMBL; AB263783; BAE96793.1; -; Genomic_DNA.
DR EMBL; AB263784; BAE96794.1; -; Genomic_DNA.
DR EMBL; AB263785; BAE96795.1; -; Genomic_DNA.
DR EMBL; AB263786; BAE96796.1; -; Genomic_DNA.
DR EMBL; AB263788; BAE96798.1; -; Genomic_DNA.
DR EMBL; AB263789; BAE96799.1; -; Genomic_DNA.
DR EMBL; AB263790; BAE96800.1; -; Genomic_DNA.
DR EMBL; AB263791; BAE96801.1; -; Genomic_DNA.
DR EMBL; AB263792; BAE96802.1; -; Genomic_DNA.
DR AlphaFoldDB; Q18MU0; -.
DR UniPathway; UPA00109; UER00184.
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:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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 NCBIfam; TIGR01546; GAPDH-II_archae; 1.
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; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00559};
KW NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00559};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00559}.
FT DOMAIN 7..145
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 145
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 16..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 144..146
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 173
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 199..200
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 306
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
SQ SEQUENCE 346 AA; 37547 MW; A2AC72CBF9715C3D CRC64;
MSLMSVVKVG VNGFGTIGRR VALAITLQKD MKLVGVVKRT PDYAALYAAS RGIPIYTPTA
KEAEEFEKRG IKVGGTLREL LARVDVIVDA TPEGQGAKNK PLYREAGVKQ VYQGGEKPEV
AEASFSTLCN YEESKGRGSL RVVSCNTTGL LRLICTLNRE FGVESVRAVL VRRGADPKEV
KKGPIDSIVL NPPTLPSHHA VDVRTVLPWL DIKTAAVAVP TTFMHMHHVT LKLAKPVERR
EVLETLASAP RIMLVSSGDT GIKSTSQLVD AARLSRMGYD IPELVVFEES VAVDGREVML
FQAVHQESIV VPENIDAIRA VASSPLTLDE TLKATDGSLG LRKTLW
//
