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Database: UniProt
Entry: A0A218P8J6_9EURY
LinkDB: A0A218P8J6_9EURY
Original site: A0A218P8J6_9EURY 
ID   A0A218P8J6_9EURY        Unreviewed;       334 AA.
AC   A0A218P8J6;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   08-MAY-2019, entry version 11.
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   ORFNames=A3L08_07140 {ECO:0000313|EMBL:ASJ07112.1};
OS   Thermococcus pacificus.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=71998 {ECO:0000313|EMBL:ASJ07112.1, ECO:0000313|Proteomes:UP000197418};
RN   [1] {ECO:0000313|EMBL:ASJ07112.1, ECO:0000313|Proteomes:UP000197418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P-4 {ECO:0000313|EMBL:ASJ07112.1,
RC   ECO:0000313|Proteomes:UP000197418};
RA   Oger P.M.;
RT   "Complete genome sequence of Thermococcus pacificus type strain P4.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC         Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
CC         ECO:0000256|SAAS:SAAS01127777};
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:0000256|HAMAP-
CC         Rule:MF_00559, ECO:0000256|SAAS:SAAS01127759};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|HAMAP-
CC       Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
CC       ECO:0000256|SAAS:SAAS01167718}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176914}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176915}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family. {ECO:0000256|HAMAP-Rule:MF_00559,
CC       ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176910}.
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DR   EMBL; CP015102; ASJ07112.1; -; Genomic_DNA.
DR   KEGG; tpaf:A3L08_07140; -.
DR   KO; K00150; -.
DR   BioCyc; GCF_002214485:A3L08_RS07140-MONOMER; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000197418; 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: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   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 {ECO:0000313|Proteomes:UP000197418};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176917};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01167717};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
KW   ECO:0000256|SAAS:SAAS01176916};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00559, ECO:0000256|RuleBase:RU003388,
KW   ECO:0000256|SAAS:SAAS01167721};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00559,
KW   ECO:0000256|RuleBase:RU003388, ECO:0000256|SAAS:SAAS01176912}.
FT   DOMAIN        3    141       Gp_dh_N. {ECO:0000259|SMART:SM00846}.
FT   NP_BIND      12     13       NAD. {ECO:0000256|HAMAP-Rule:MF_00559,
FT                                ECO:0000256|PIRSR:PIRSR000149-3}.
FT   REGION      140    142       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   REGION      192    193       Glyceraldehyde 3-phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   ACT_SITE    141    141       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00559, ECO:0000256|PIRSR:PIRSR000149-
FT                                1}.
FT   BINDING     111    111       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     167    167       NAD. {ECO:0000256|HAMAP-Rule:MF_00559}.
FT   BINDING     298    298       NAD; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00559}.
SQ   SEQUENCE   334 AA;  37120 MW;  8123C7BFD99B7700 CRC64;
     MKVKVGINGY GTIGKRVAYA VSKQDDMELI GVTKTKPDFE AYRAKELGIP VYAASEDFLP
     RFEKAGFEVA GTLNDLLEKV DVIVDATPGG MGAKNKALYE KAGVKAIFEG GEKASTAEVS
     FVAQANYEKA LGKDYVRVVS CNTTGLTRTL SALQKYIDYV YAVMIRRAAD PNDSRRGPVN
     AITPSVTVPS HHGPDVQTVI PINIETSAFV VPTTLMHVHS VMIELKKPIT EKDVIEVFEN
     TTRVLLFEKE KGFDSTAQLI EFARDLHREW NNLYEIAVWK ESISVRGNRL FYIQAVHQES
     DVVPENVDAI RAMFELADKW ESIKKTNRSL GILK
//
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