ID A0A0E3S248_9EURY Unreviewed; 335 AA.
AC A0A0E3S248;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=MSLAZ_1558 {ECO:0000313|EMBL:AKB74819.1};
OS Methanosarcina lacustris Z-7289.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB74819.1, ECO:0000313|Proteomes:UP000033072};
RN [1] {ECO:0000313|EMBL:AKB74819.1, ECO:0000313|Proteomes:UP000033072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z-7289 {ECO:0000313|EMBL:AKB74819.1,
RC ECO:0000313|Proteomes:UP000033072};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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, 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; CP009515; AKB74819.1; -; Genomic_DNA.
DR RefSeq; WP_048125955.1; NZ_CP009515.1.
DR AlphaFoldDB; A0A0E3S248; -.
DR STRING; 1434111.MSLAZ_1558; -.
DR GeneID; 24806310; -.
DR KEGG; mls:MSLAZ_1558; -.
DR PATRIC; fig|1434111.4.peg.2031; -.
DR HOGENOM; CLU_069533_0_0_2; -.
DR OrthoDB; 295712at2157; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000033072; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; 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; 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 4..141
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 141
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559,
FT ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 111
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 140..142
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 169
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 195..196
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
FT BINDING 300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00559"
SQ SEQUENCE 335 AA; 36342 MW; 9275FC772C4ECED7 CRC64;
MAKAKIAVNG YGTIGKRVAD AVRAQNDMEI IGISKTKPNY EAAVAHQLGY DIYAPAANLE
AFEKAGMPAA GSIEEMVEKS DLVADCTPGG VGEANKALYE KAGVKAIWQG GEKHELTGFS
FNAVSNYEGA LGLDFVRVVS CNTTGLCRVI YPIDKAFGIK KVRATLARRA ADPNDVKKGP
INAIVPEPIK LPSHHGPDVK TVIPHINITS AAMKIPTTLM HLHTVNMELE KECTAEDVRK
VLGSQSRIRF VGQGISSTAE IIEVARDIKR PRNDMWENCI WTDSVTMHEG ELYFFQAIHQ
ESIVVPENVD AIRAMMELES DGAKSIAKTN KAIGL
//
