G3P2_TRIV2
ID G3P2_TRIV2 Reviewed; 337 AA.
AC P34917; Q3MAQ0;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000250|UniProtKB:P58554};
DE Short=GAPDH 2 {ECO:0000250|UniProtKB:P58554};
DE EC=1.2.1.59 {ECO:0000250|UniProtKB:P10618};
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P58554};
GN Name=gap2; OrderedLocusNames=Ava_2318;
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).
CC -!- FUNCTION: Gap2 has a major role in carbon fixation as a component of
CC the Calvin cycle. Catalyzes the oxidative phosphorylation of
CC glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using
CC the cofactor NAD. The first reaction step involves the formation of a
CC hemiacetal intermediate between G3P and a cysteine residue, and this
CC hemiacetal intermediate is then oxidized to a thioester, with
CC concomitant reduction of NAD to NADH. The reduced NADH is then
CC exchanged with the second NAD, and the thioester is attacked by a
CC nucleophilic inorganic phosphate to produce BPG.
CC {ECO:0000250|UniProtKB:P58554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NADP(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADPH; Xref=Rhea:RHEA:10296,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:P10618};
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=1.2.1.59;
CC Evidence={ECO:0000250|UniProtKB:P10618};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000250|UniProtKB:P58554}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P80506}.
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; L07498; AAA21996.1; -; Genomic_DNA.
DR EMBL; CP000117; ABA21936.1; -; Genomic_DNA.
DR PIR; I39603; I39603.
DR AlphaFoldDB; P34917; -.
DR SMR; P34917; -.
DR STRING; 240292.Ava_2318; -.
DR PRIDE; P34917; -.
DR EnsemblBacteria; ABA21936; ABA21936; Ava_2318.
DR KEGG; ava:Ava_2318; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_3; -.
DR OMA; NAKVLAW; -.
DR UniPathway; UPA00116; -.
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:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:RHEA.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; 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 PANTHER; PTHR43148; PTHR43148; 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; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 3: Inferred from homology;
KW Calvin cycle; Cytoplasm; NADP; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145626"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 11..12
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 35
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 122
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 153..155
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 184
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 199
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 212..213
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 235
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 181
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT CONFLICT 47
FT /note="K -> N (in Ref. 1; AAA21996)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="M -> S (in Ref. 1; AAA21996)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..57
FT /note="KLKN -> VKK (in Ref. 1; AAA21996)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="A -> V (in Ref. 1; AAA21996)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> R (in Ref. 1; AAA21996)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36876 MW; 4FDCBD856B858863 CRC64;
MIRVAINGFG RIGRNFARCW LGRENSNIEL VAVNDTSDPR TNAHLLKYDS MLGKLKNVDI
TADDNSITVN GKTIKCVSDR NPENLPWKEW EIDLIIESTG VFTSKEGALK HVNAGAKKVL
ITAPGKNEDG TFVIGVNHHD YDHNVHHIIS NASCTTNCLA PIAKVLNDKF GIIKGSMTTT
HSYTGDQRLL DASHRDLRRA RAAAINIVPT STGAAKAVAL VIPELKGKLN GVALRVPTPN
VSMVDFVVQV EKRTITEEVN QALKDASEGP LKGILDYSEL QLVSSDYQGT DASSIVDASL
TLVMGNDLVK VMAWYDNEWG YSQRVLDLAE LVAEKWV
