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Database: UniProt
Entry: A0A4D6HC09_9EURY
LinkDB: A0A4D6HC09_9EURY
Original site: A0A4D6HC09_9EURY 
ID   A0A4D6HC09_9EURY        Unreviewed;       336 AA.
AC   A0A4D6HC09;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating) {ECO:0000256|ARBA:ARBA00013024};
DE            EC=1.2.1.59 {ECO:0000256|ARBA:ARBA00013024};
GN   Name=gap {ECO:0000313|EMBL:QCC51145.1};
GN   ORFNames=DV733_07775 {ECO:0000313|EMBL:QCC51145.1};
OS   Halapricum salinum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halapricum.
OX   NCBI_TaxID=1457250 {ECO:0000313|EMBL:QCC51145.1, ECO:0000313|Proteomes:UP000296706};
RN   [1] {ECO:0000313|EMBL:QCC51145.1, ECO:0000313|Proteomes:UP000296706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA1105 {ECO:0000313|EMBL:QCC51145.1,
RC   ECO:0000313|Proteomes:UP000296706};
RX   PubMed=30975999; DOI=.1038/s41467-019-09390-9;
RA   Xiong L., Liu S., Chen S., Xiao Y., Zhu B., Gao Y., Zhang Y., Chen B.,
RA   Luo J., Deng Z., Chen X., Wang L., Chen S.;
RT   "A new type of DNA phosphorothioation-based antiviral system in archaea.";
RL   Nat. Commun. 10:1688-1688(2019).
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   -!- 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   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; CP031310; QCC51145.1; -; Genomic_DNA.
DR   RefSeq; WP_049995241.1; NZ_CP031310.1.
DR   AlphaFoldDB; A0A4D6HC09; -.
DR   STRING; 1457250.GCA_000755225_01351; -.
DR   GeneID; 39847754; -.
DR   KEGG; hsn:DV733_07775; -.
DR   OrthoDB; 30535at2157; -.
DR   Proteomes; UP000296706; Chromosome.
DR   GO; GO:0043891; F:glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
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   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000296706}.
FT   DOMAIN          7..156
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        156
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         16..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         38
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         155..157
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         186
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         214..215
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         237
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         320
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            183
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   336 AA;  36162 MW;  C562EB8225DA34BB CRC64;
     MSASDPVRIG INGFGRIGRC AFRSALNNDD VEIVGINDVM DFEQMEYLAK YDSNLGNLPY
     DVSLDGDTLQ VGDNAVSLHN IQSPEELPWD DLDVDVAIES TGIFRTKDDA SAHLDAGADK
     TLISAPPKGD KPVPQFVFGV NEDEYDGEDI VSGASCTTNS VSLPMYVLLE EFGVEAAEMT
     TIHAYTGSQS IVDGPKSKTR RGRAAAENIV PTTTGASTAT TDILPELKGK FEAMAVRVPT
     PTGSITEIVV DLDGNPSVDE INAAFEEYAT GELEGSMGAT WDEVVSRDIV GWEYGSCVDL
     DQTSTTEGGD LAKIFAWYDN EMGYTSQMMR LAEYIA
//
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