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Database: UniProt/TrEMBL
Entry: C5A7F7_THEGJ
LinkDB: C5A7F7_THEGJ
Original site: C5A7F7_THEGJ 
ID   C5A7F7_THEGJ            Unreviewed;       335 AA.
AC   C5A7F7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 97.
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=gap {ECO:0000256|HAMAP-Rule:MF_00559,
GN   ECO:0000313|EMBL:ACS34169.1};
GN   OrderedLocusNames=TGAM_1667 {ECO:0000313|EMBL:ACS34169.1};
OS   Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS34169.1, ECO:0000313|Proteomes:UP000001488};
RN   [1] {ECO:0000313|EMBL:ACS34169.1, ECO:0000313|Proteomes:UP000001488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15229 / JCM 11827 / EJ3
RC   {ECO:0000313|Proteomes:UP000001488};
RX   PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA   Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA   Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT   "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT   the most radioresistant organism known amongst the Archaea.";
RL   Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS34169.1; -; Genomic_DNA.
DR   RefSeq; WP_015859280.1; NC_012804.1.
DR   AlphaFoldDB; C5A7F7; -.
DR   STRING; 593117.TGAM_1667; -.
DR   PaxDb; 593117-TGAM_1667; -.
DR   GeneID; 7987577; -.
DR   KEGG; tga:TGAM_1667; -.
DR   PATRIC; fig|593117.10.peg.1673; -.
DR   eggNOG; arCOG00493; Archaea.
DR   HOGENOM; CLU_069533_0_0_2; -.
DR   OMA; DCIRAML; -.
DR   OrthoDB; 295712at2157; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000001488; 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: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|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388};
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          4..142
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        142
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559,
FT                   ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         13..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         112
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         141..143
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         168
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         193..194
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         299
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
SQ   SEQUENCE   335 AA;  37299 MW;  3A0027BAEBA64151 CRC64;
     MARVKVGING YGTIGKRVAY AVTKQDDMKL IGVTKTKPDF EAYRAMELGI PVYAASEEFL
     PRFEKANFEV AGTLEDLLTE VDVIVDATPG GMGAKNKALY EKAGVKAVFQ GGEKANVAEV
     SFVAQANYEK ALGKDYVRVV SCNTTGLTRT LSAIQEYIDY VYAVMIRRAA DPNDTKRGPI
     NAITPSVTVP SHHGPDVQTV IPINIETSAF VVPTTLMHVH SIMVELKKPV EAKDVVDIFE
     NTTRVLLFEK EKGFESTAHI IEFARDLHRE WNNLYEIAVW KESISVRGNR LFYIQAVHQE
     SDVVPENIDA IRAMFELAEK WESIRKTNES LGILK
//
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