G3P3_TRIV2
ID G3P3_TRIV2 Reviewed; 337 AA.
AC P34918; Q3M6R6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 3 {ECO:0000303|PubMed:11327708};
DE Short=GAPDH 3 {ECO:0000303|PubMed:11327708};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:11327708};
GN Name=gap3; OrderedLocusNames=Ava_3715;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8378350; DOI=10.1073/pnas.90.18.8692;
RA Martin W., Brinkmann H., Savona C., Cerff R.;
RT "Evidence for a chimeric nature of nuclear genomes: eubacterial origin of
RT eukaryotic glyceraldehyde-3-phosphate dehydrogenase genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8692-8696(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
RN [3]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=11327708; DOI=10.1006/bbrc.2001.4782;
RA Valverde F., Peleato M.L., Fillat M.F., Gomez-Moreno C., Losada M.,
RA Serrano A.;
RT "Simultaneous occurrence of two different glyceraldehyde-3-phosphate
RT dehydrogenases in heterocystous N(2)-fixing cyanobacteria.";
RL Biochem. Biophys. Res. Commun. 283:356-363(2001).
CC -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC NAD. The first reaction step involves the formation of a hemiacetal
CC intermediate between G3P and a cysteine residue, and this hemiacetal
CC intermediate is then oxidized to a thioester, with concomitant
CC reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC second NAD, and the thioester is attacked by a nucleophilic inorganic
CC phosphate to produce BPG. {ECO:0000269|PubMed:11327708}.
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:0000250|UniProtKB:P09124};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305|PubMed:11327708}.
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:11327708}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11327708}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; L07499; AAA21997.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA23320.1; -; Genomic_DNA.
DR PIR; I39604; I39604.
DR AlphaFoldDB; P34918; -.
DR SMR; P34918; -.
DR STRING; 240292.Ava_3715; -.
DR PRIDE; P34918; -.
DR EnsemblBacteria; ABA23320; ABA23320; Ava_3715.
DR KEGG; ava:Ava_3715; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_0_3; -.
DR OMA; QVKILAW; -.
DR UniPathway; UPA00109; UER00184.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002533; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
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 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Gluconeogenesis; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 3"
FT /id="PRO_0000145628"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 198
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 317
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT CONFLICT 215
FT /note="T -> K (in Ref. 1; AAA21997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37130 MW; 967BD40141E46F5C CRC64;
MKIRVGINGF GRMGRLALRA AWGWPELEFV HINEIKGGAV AAAHLLKFDS VHGRWTPEVE
AEGERVLIDS TPLSFSEYGK PEDVPWEDFG VDLVLECSGK FRTPATLDPY FKRGVQKVIV
AAPVKEEALN IVMGVNDYLY EPEKHHLLTA ASCTTNCLAP VVKVIHEGLG IKHGIITTIH
DNTNTQTLVD APHKDLRRAR ATSLSLIPTT TGSATAIALI YPELKGKLNG IAVRVPLLNA
SLTDCVFEVN RPTTVEEINA LLKAASEQAP LQGILGYEER PLVSIDYKDD PRSSIIDALS
TMVVDETQVK ILAWYDNEWG YVNRMVELAR KVALSLK
