ID A0A388MFY8_CHABU Unreviewed; 334 AA.
AC A0A388MFY8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=CBR_g68000 {ECO:0000313|EMBL:GBG93392.1};
OS Chara braunii (Braun's stonewort).
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=69332 {ECO:0000313|EMBL:GBG93392.1, ECO:0000313|Proteomes:UP000265515};
RN [1] {ECO:0000313|EMBL:GBG93392.1, ECO:0000313|Proteomes:UP000265515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S276 {ECO:0000313|EMBL:GBG93392.1,
RC ECO:0000313|Proteomes:UP000265515};
RX PubMed=30007417; DOI=10.1016/j.cell.2018.06.033;
RA Nishiyama T., Sakayama H., Vries J.D., Buschmann H., Saint-Marcoux D.,
RA Ullrich K.K., Haas F.B., Vanderstraeten L., Becker D., Lang D.,
RA Vosolsobe S., Rombauts S., Wilhelmsson P.K.I., Janitza P., Kern R.,
RA Heyl A., Rumpler F., Villalobos L.I.A.C., Clay J.M., Skokan R., Toyoda A.,
RA Suzuki Y., Kagoshima H., Schijlen E., Tajeshwar N., Catarino B.,
RA Hetherington A.J., Saltykova A., Bonnot C., Breuninger H., Symeonidi A.,
RA Radhakrishnan G.V., Van Nieuwerburgh F., Deforce D., Chang C., Karol K.G.,
RA Hedrich R., Ulvskov P., Glockner G., Delwiche C.F., Petrasek J.,
RA Van de Peer Y., Friml J., Beilby M., Dolan L., Kohara Y., Sugano S.,
RA Fujiyama A., Delaux P.-M., Quint M., TheiBen G., Hagemann M., Harholt J.,
RA Dunand C., Zachgo S., Langdale J., Maumus F., Straeten D.V.D., Gould S.B.,
RA Rensing S.A.;
RT "The Chara Genome: Secondary Complexity and Implications for Plant
RT Terrestrialization.";
RL Cell 174:448-464(2018).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBG93392.1}.
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DR EMBL; BFEA01001616; GBG93392.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A388MFY8; -.
DR STRING; 69332.A0A388MFY8; -.
DR OMA; ECTGFFC; -.
DR Proteomes; UP000265515; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP 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:0006006; P:glucose metabolic process; 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; 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 3: Inferred from homology;
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000265515}.
FT DOMAIN 3..152
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 334 AA; 35578 MW; 4668F92ED327CE44 CRC64;
MVVKIGINGF GRIGRLVLRA SLNHPQVQVV AVNDPFLDPE YIVYLFKYDT VHGKYKGEVG
LSADKKLIVD GKEIAIFALR DPSAIPWGEA GADYVVESTG VFTDKDKAAA HLKGGAKKVV
ISAPSGNAPM FVMGVNEEKY TPDLDVISNA SCTTNCLAPL AKVINDNFGI VEGLMTTVHA
VTATQKTVDG PSGKDWRGGR GAGFNIIPSG TGAAKAVGKV LPVLNGKLTG MAFRIPTADV
SVVDLTVRLE KSASYDEIKA VIKKASETDL KGILGFTEDD VVSSDFIGDA RSSIFDAKAG
IALNGNFVKL VSWYDNEWGY SNRVVELIEH ISKA
//
