ID H0AA17_HALSG Unreviewed; 232 AA.
AC H0AA17;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=HRED_04612 {ECO:0000313|EMBL:EHK02373.1};
OS Haloredivivus sp. (strain G17).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Candidatus Haloredivivus.
OX NCBI_TaxID=1072681 {ECO:0000313|EMBL:EHK02373.1, ECO:0000313|Proteomes:UP000003484};
RN [1] {ECO:0000313|EMBL:EHK02373.1, ECO:0000313|Proteomes:UP000003484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G17 {ECO:0000313|EMBL:EHK02373.1,
RC ECO:0000313|Proteomes:UP000003484};
RA Ghai R., Pasic L., Fernandez A.B., Martin-Cuadrado A.-B., Mizuno C.M.,
RA McMahon K.D., Papke R.T., Stepanauskas R., Rodriguez-Brito B., Rohwer F.,
RA Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT "New Dominant Microbial Groups Along A Salinity Gradient.";
RL Sci. Rep. 0:0-0(2011).
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|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|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:EHK02373.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGNT01000059; EHK02373.1; -; Genomic_DNA.
DR AlphaFoldDB; H0AA17; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000003484; Unassembled WGS sequence.
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: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 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 InterPro; IPR000846; DapB_N.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
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 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|RuleBase:RU003388};
KW Glycolysis {ECO:0000256|RuleBase:RU003388};
KW NAD {ECO:0000256|RuleBase:RU003388}; NADP {ECO:0000256|RuleBase:RU003388};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003388,
KW ECO:0000313|EMBL:EHK02373.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003484}.
FT DOMAIN 2..105
FT /note="Dihydrodipicolinate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01113"
FT DOMAIN 151..229
FT /note="Glyceraldehyde 3-phosphate dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF02800"
FT NON_TER 232
FT /evidence="ECO:0000313|EMBL:EHK02373.1"
SQ SEQUENCE 232 AA; 24800 MW; 9C39CAE0952DE64E CRC64;
MVNVIVAGVG TIGKRVAEAV KNQEDMNLYG VADVSQTGGL RTVLSEEGAL HGTDLYASNH
DGKENLENQG FYVKGLLEDQ LEDVDLVVDC TPPGVDEKNK ENLYEPNNVK AVFQGGAPED
IAPVAFNADA NYDDARGEDF VKVVSCNTTS LSRTMSAIDE AFGIDNAVAS LVRRGGDIPQ
DSRGPINSTI PVTEVPSHHG PDVQAVMPEL DIKTLAVKVP VTYGHVHMVN LE
//
