ID B9URE9_9EUCA Unreviewed; 216 AA.
AC B9URE9;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ACH57028.1};
DE Flags: Fragment;
GN Name=GAPDH {ECO:0000313|EMBL:ACH57028.1};
OS Geocharax sp. 1-MBS-2007.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Astacidea;
OC Parastacoidea; Parastacidae; Geocharax.
OX NCBI_TaxID=455332 {ECO:0000313|EMBL:ACH57028.1};
RN [1] {ECO:0000313|EMBL:ACH57028.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19118635; DOI=10.1016/j.ympev.2008.11.025;
RA Schultz M.B., Smith S.A., Horwitz P., Richardson A.M., Crandall K.A.,
RA Austin C.M.;
RT "Evolution underground: a molecular phylogenetic investigation of
RT Australian burrowing freshwater crayfish (Decapoda: Parastacidae) with
RT particular focus on Engaeus Erichson.";
RL Mol. Phylogenet. Evol. 50:580-598(2009).
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 -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406}.
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DR EMBL; EU977441; ACH57028.1; -; Genomic_DNA.
DR EMBL; EU977442; ACH57029.1; -; Genomic_DNA.
DR AlphaFoldDB; B9URE9; -.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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; IPR036291; NAD(P)-bd_dom_sf.
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 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 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 1..79
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACH57028.1"
FT NON_TER 216
FT /evidence="ECO:0000313|EMBL:ACH57028.1"
SQ SEQUENCE 216 AA; 22587 MW; 6961B320A4690ECF CRC64;
IAVFNEMKPE NIPWSKAGAE YVVESTGVFT TIEKASAHFT GGAKKVVISA PSADAPMFVC
GVNLEKYSKD MTVVSNASCT TNCLAPVAKV LHENFEIVEG LMTTVHAVTA TQKTVDGPSA
KDWRGGRGAA QNIIPSSTGA AKAVGKVIPE LNGKLTGMAF RVPTPDVSVV DLTVRLGKEC
SYDDVKAAMK AASEGPLKGI LGYTEDDVVS SDFTGD
//
