ID G7VDV7_9CREN Unreviewed; 343 AA.
AC G7VDV7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 66.
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=P186_0070 {ECO:0000313|EMBL:AET31539.1};
OS Pyrobaculum ferrireducens.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET31539.1, ECO:0000313|Proteomes:UP000005867};
RN [1] {ECO:0000313|EMBL:AET31539.1, ECO:0000313|Proteomes:UP000005867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1860 {ECO:0000313|EMBL:AET31539.1,
RC ECO:0000313|Proteomes:UP000005867};
RX PubMed=22247528; DOI=10.1128/JB.06465-11;
RA Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT pyrobaculum able to grow with various electron acceptors.";
RL J. Bacteriol. 194:727-728(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; CP003098; AET31539.1; -; Genomic_DNA.
DR AlphaFoldDB; G7VDV7; -.
DR STRING; 1104324.P186_0070; -.
DR KEGG; pyr:P186_0070; -.
DR eggNOG; arCOG00493; Archaea.
DR HOGENOM; CLU_069533_0_0_2; -.
DR OrthoDB; 295712at2157; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000005867; 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|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00559};
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 1..139
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 172..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 139
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 138..140
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 343 AA; 37745 MW; 9A7B22BC720B0110 CRC64;
MKVGIVGYGT IGKRIADAVA AQDDMKISGV LKVTPDYEAK VALERGFRVY TLPDRLDKFR
KAGIEPAGTI EDLIKASDVI IDASPEDVGR DNKEKYYSRF DKPVVFQGGE DADVAEVSFN
ALANYEEARG RRYVRVVSCN TTGITRVLTS LMLNGIGIKK ARIFIARRGA DPKEHKKGPI
NDVVPNPASV PSHHGPDVQT ILRNVDIVTM AVAVPVTIMH MHMAYVELDG GYTRDAVLEA
FAKTPRLFLA DVGAGLLSLA QIIEYARDLG RPRGDFPEVA IFRDSVTVRG GELYLMYGVH
QESIVVPENI DVIRAIFGVM PKWPSIEKTD KTLKLITEGK RYG
//
