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Database: UniProt/TrEMBL
Entry: I7BRV8_NATSJ
LinkDB: I7BRV8_NATSJ
Original site: I7BRV8_NATSJ 
ID   I7BRV8_NATSJ            Unreviewed;       338 AA.
AC   I7BRV8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 68.
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   OrderedLocusNames=NJ7G_0220 {ECO:0000313|EMBL:AFO55475.1};
OS   Natrinema sp. (strain J7-2).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natrinema.
OX   NCBI_TaxID=406552 {ECO:0000313|EMBL:AFO55475.1, ECO:0000313|Proteomes:UP000006507};
RN   [1] {ECO:0000313|EMBL:AFO55475.1, ECO:0000313|Proteomes:UP000006507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J7-2 {ECO:0000313|EMBL:AFO55475.1,
RC   ECO:0000313|Proteomes:UP000006507};
RX   PubMed=22911826; DOI=10.1371/journal.pone.0041621;
RA   Feng J., Liu B., Zhang Z., Ren Y., Li Y., Gan F., Huang Y., Chen X.,
RA   Shen P., Wang L., Tang B., Tang X.F.;
RT   "The complete genome sequence of Natrinema sp. J7-2, a haloarchaeon capable
RT   of growth on synthetic media without amino acid supplements.";
RL   PLoS ONE 7:E41621-E41621(2012).
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; CP003412; AFO55475.1; -; Genomic_DNA.
DR   RefSeq; WP_008456575.1; NC_018224.1.
DR   AlphaFoldDB; I7BRV8; -.
DR   STRING; 406552.NJ7G_0220; -.
DR   GeneID; 13352481; -.
DR   KEGG; nat:NJ7G_0220; -.
DR   PATRIC; fig|406552.5.peg.181; -.
DR   eggNOG; arCOG00493; Archaea.
DR   HOGENOM; CLU_069533_0_0_2; -.
DR   OMA; DCIRAML; -.
DR   OrthoDB; 295712at2157; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000006507; 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          2..140
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        140
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559,
FT                   ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         11..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         110
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         139..141
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         194..195
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT   BINDING         301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
SQ   SEQUENCE   338 AA;  36625 MW;  12EADAB1E88C183A CRC64;
     MQQVAINGYG TIGKRVADAV RQQPDMEVLG VAKTRPNFEA ETAIDKGFPL YAAVEEREEL
     FAEAGLEIAG PVEDLVAEAD VVVDATPSGI GAQNKALYEE YDTPALYQGG EDADLVDVSF
     NARSNFEDAV DADHVRVVSC NTTGLSRVIA PLREEYGVEK VRATLVRRGG DPGQSDRGPI
     NDILPNPVTI PSHHGPDVET IFPDLDIDTL GMKVPATLMH MHSLNITLEE DVDAAAVRDL
     FADESRLFLI PERMDIDGSG KLKEYALDAG RPRGDLWENC LWAESISTEG RDFYCFQGIH
     QESDVVPENV DAIRAVTGAA DAEESIATTD EALGIGLR
//
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