ID   C7SP44_9BILA            Unreviewed;       196 AA.
AC   C7SP44;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Glyceraldehyde 3-phosphate dehydrogenase {ECO:0000313|EMBL:ACU68940.1};
DE   Flags: Fragment;
OS   Hemichordata sp. MR-2009.
OC   Eukaryota; Metazoa; Hemichordata.
OX   NCBI_TaxID=662529 {ECO:0000313|EMBL:ACU68940.1};
RN   [1] {ECO:0000313|EMBL:ACU68940.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19602542; DOI=10.1093/molbev/msp150;
RA   Paps J., Baguna J., Riutort M.;
RT   "Bilaterian phylogeny: a broad sampling of 13 nuclear genes provides a new
RT   Lophotrochozoa phylogeny and supports a paraphyletic basal acoelomorpha.";
RL   Mol. Biol. Evol. 26:2397-2406(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; FJ555363; ACU68940.1; -; mRNA.
DR   AlphaFoldDB; C7SP44; -.
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   2: Evidence at transcript level;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          3..81
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:ACU68940.1"
FT   NON_TER         196
FT                   /evidence="ECO:0000313|EMBL:ACU68940.1"
SQ   SEQUENCE   196 AA;  20888 MW;  D463F926786A4FB2 CRC64;
     HAISVFQEMI PTNIKWADNG AEYIVDSTGV FTTMDKAKAH FEGGAKKVII SAPSADAPMF
     VIGVNEDKYE KSMNIVSNAS CTTNCLAPLA KVINDNYGIE EGLMSTIHAY TATQKTVDGP
     SGKNWRDGRG AAQNIIPAST GAAKAVGKVI PELNGKLTGM AFRVPVPDVS VVDLTCRLKK
     KAKYDDIKAV IKKAAE
//