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Database: UniProt
Entry: G3P_THESM
LinkDB: G3P_THESM
Original site: G3P_THESM 
ID   G3P_THESM               Reviewed;         334 AA.
AC   C6A312;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00559};
DE            Short=GAPDH {ECO:0000255|HAMAP-Rule:MF_00559};
DE            EC=1.2.1.59 {ECO:0000255|HAMAP-Rule:MF_00559};
DE   AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00559};
GN   Name=gap {ECO:0000255|HAMAP-Rule:MF_00559};
GN   OrderedLocusNames=TSIB_0949;
OS   Thermococcus sibiricus (strain MM 739 / DSM 12597).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=604354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MM 739 / DSM 12597;
RX   PubMed=19447963; DOI=10.1128/AEM.00718-09;
RA   Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V.,
RA   Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Metabolic versatility and indigenous origin of the archaeon
RT   Thermococcus sibiricus, isolated from a siberian oil reservoir, as
RT   revealed by genome analysis.";
RL   Appl. Environ. Microbiol. 75:4580-4588(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10296, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00559};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = 3-
CC         phospho-D-glyceroyl phosphate + H(+) + NADH;
CC         Xref=Rhea:RHEA:10300, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57604, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:59776; EC=1.2.1.59; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00559};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00559}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00559}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00559}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000255|HAMAP-Rule:MF_00559}.
DR   EMBL; CP001463; ACS90007.1; -; Genomic_DNA.
DR   RefSeq; WP_015849226.1; NC_012883.1.
DR   SMR; C6A312; -.
DR   STRING; 604354.TSIB_0949; -.
DR   EnsemblBacteria; ACS90007; ACS90007; TSIB_0949.
DR   GeneID; 8095943; -.
DR   KEGG; tsi:TSIB_0949; -.
DR   eggNOG; arCOG00493; Archaea.
DR   eggNOG; COG0057; LUCA.
DR   HOGENOM; HOG000223361; -.
DR   KO; K00150; -.
DR   OMA; NAIVPNP; -.
DR   OrthoDB; 32079at2157; -.
DR   BioCyc; TSIB604354:G1GV3-932-MONOMER; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000009079; 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: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   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    334       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_1000212041.
FT   NP_BIND      12     13       NAD. {ECO:0000255|HAMAP-Rule:MF_00559}.
FT   REGION      140    142       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00559}.
FT   REGION      192    193       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00559}.
FT   ACT_SITE    141    141       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00559}.
FT   BINDING     111    111       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00559}.
FT   BINDING     167    167       NAD. {ECO:0000255|HAMAP-Rule:MF_00559}.
FT   BINDING     298    298       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00559}.
SQ   SEQUENCE   334 AA;  37236 MW;  44690009DF173444 CRC64;
     MKVKVGINGY GTIGKRVGYA VSKQADMELV GVAKTKPDFE AYRAKELGIP VYAASPDFVP
     RFEKVGFEIV GTLEDLLEKV DVIVDATPGG MGEKNKALYE KAGVKAIFQG GEKASVAEVS
     FVAQANYEKA LGKDYVRVVS CNTTGLTRTL NAIKDYIDYV YAVMIRRAAD PNDIKRGPVN
     AIKPSVEVPS HHGPDVQTVI PINIETMAFI VPTTLMHVHS VMVELKKPLT REDVIKIFEN
     TTRVLLFEKE RGFDSTAQLI EFARDLHREW NNLYEIGVWK ESISVKGNRL FYIQAVHQES
     DVVPENIDAI RAMFELADKW ESIKKTNKSL GILK
//
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