ID A7TZ41_LEPSM Unreviewed; 332 AA.
AC A7TZ41;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
GN Name=G3P {ECO:0000313|EMBL:ACO12994.1};
GN Synonyms=GAPDH {ECO:0000313|EMBL:CDW37745.1};
OS Lepeophtheirus salmonis (Salmon louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Hexanauplia; Copepoda; Siphonostomatoida; Caligidae; Lepeophtheirus.
OX NCBI_TaxID=72036 {ECO:0000313|EMBL:ABU41037.1};
RN [1] {ECO:0000313|EMBL:ABU41037.1}
RP NUCLEOTIDE SEQUENCE.
RA Eichner C., Frost P., Dysvik B., Kristiansen B., Jonassen I., Nilsen F.;
RT "Salmon louse (Lepeophtheirus salmonis) transcriptomes during post molting
RT maturation and egg production, revealed using EST-sequencing and microarray
RT analysis.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACO12994.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pacific form {ECO:0000313|EMBL:ACO12994.1};
RC TISSUE=Whole {ECO:0000313|EMBL:ACO12994.1};
RA Yasuike M., von Schalburg K., Cooper G., Leong J., Jones S.R.M., Koop B.F.;
RT "Lepeophtheirus salmonis ESTs and full-length cDNAs.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADD38101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Atlantic form {ECO:0000313|EMBL:ADD38101.1};
RC TISSUE=Mixed tissue {ECO:0000313|EMBL:ADD38101.1};
RA Yasuike M., von Schalburg K., Cooper G., Leong J., Nilsen F., Jones S.R.M.,
RA Koop B.F.;
RT "Atlantic Lepeophtheirus salmonis ESTs and full-length cDNAs.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CDW37745.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole organism {ECO:0000313|EMBL:CDW37745.1};
RA Chronopoulou M.;
RL Submitted (MAY-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=1.2.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001810,
CC ECO:0000256|RuleBase:RU361160};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869,
CC ECO:0000256|RuleBase:RU361160}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
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; EF490852; ABU41037.1; -; mRNA.
DR EMBL; BT078570; ACO12994.1; -; mRNA.
DR EMBL; BT121171; ADD38101.1; -; mRNA.
DR EMBL; HACA01020384; CDW37745.1; -; Transcribed_RNA.
DR AlphaFoldDB; A7TZ41; -.
DR EnsemblMetazoa; XM_040710830.1; XP_040566764.1; LOC121116567.
DR EnsemblMetazoa; XM_040710832.1; XP_040566766.1; LOC121116567.
DR OrthoDB; 275384at2759; -.
DR UniPathway; UPA00109; UER00184.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01534; GAPDH-I; 1.
DR PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR10836:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Glycolysis {ECO:0000256|RuleBase:RU361160};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000149-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160}.
FT DOMAIN 2..149
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 148..150
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 179
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 208..209
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 231
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 176
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 332 AA; 35734 MW; B4385A4BCCD13B63 CRC64;
MVKVGINGFG RIGRLVLRAA LDHGVDVVAV NDPFIPVDYM AYMFKYDSTH GMCKKDISYS
DGKLIIDGKK ITVFGERDPA NIKWGEAGAD YVVESTGVFT TIEKANAHIQ GGAKRVIISA
PSADAPMFVM GVNHESYDPS MKVISNASCT TNCLAPLAKV IHDNFGIEQG LMTTVHAVTA
TQKTVDGPSA KNWRDGRGAG QNIIPASTGA AKAVGKVIPD LNGKLTGMAF RVPTPDVSVV
DLTVILKKGA TYEEICAKIK EYSEGPMKGI LGYTEDAVVS CDFTSDPRSS IFDAKAGIQL
SNNFVKLVSW YDNEYGYSNR VVDLVKYIAT QE
//
