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Database: UniProt
Entry: A0A256YS70_9ARCH
LinkDB: A0A256YS70_9ARCH
Original site: A0A256YS70_9ARCH 
ID   A0A256YS70_9ARCH        Unreviewed;       311 AA.
AC   A0A256YS70;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU003388};
DE            EC=1.2.1.59 {ECO:0000256|RuleBase:RU003388};
DE   Flags: Fragment;
GN   ORFNames=B6U78_00685 {ECO:0000313|EMBL:OYT42680.1};
OS   Candidatus Aenigmarchaeota archaeon ex4484_224.
OC   Archaea; Candidatus Aenigmarchaeota.
OX   NCBI_TaxID=2012503 {ECO:0000313|EMBL:OYT42680.1, ECO:0000313|Proteomes:UP000217063};
RN   [1] {ECO:0000313|Proteomes:UP000217063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K.W., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (JUN-2017) 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,
CC         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,
CC         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|RuleBase:RU003388}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|RuleBase:RU003388}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003388}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU003388}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OYT42680.1}.
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DR   EMBL; NJEA01000003; OYT42680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A256YS70; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000217063; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:RHEA.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_00559; G3P_dehdrog_arch; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
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; 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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU003388};
KW   Glycolysis {ECO:0000256|RuleBase:RU003388};
KW   NAD {ECO:0000256|RuleBase:RU003388};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU003388};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003388}.
FT   DOMAIN          5..151
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        151
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   NON_TER         311
FT                   /evidence="ECO:0000313|EMBL:OYT42680.1"
SQ   SEQUENCE   311 AA;  35110 MW;  2421FD8AE5113391 CRC64;
     MKTKVKVAVN GVGTIGKRVA YAVKLQKDME LKALIGYSPN PILRNQLEPN GPLYGTELWA
     TDKEALKRLQ EGGMFVHGTL EELLRNGAVD IIVDATPAGV GRWYRDNVYS KFGVKAIFQG
     GEKSDVGEMS FNAIVNYEEA LGKQFVRVPS CNTTGLIRTL HAIDSKIGIE YAFVALARRA
     ADPWEYRKGP INAVEFTKVP SHHAPDVKTV LKHLNIFSMA IKIPTTLAHT HIVEVTTKKE
     TSKEEVIEAF EKQTRVILLD IEDYPSTSLI IEKFRDYLRP RYDMYEIVVL RDSINVEGRK
     VRWFHVVHQE A
//
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