G3P2_NOSS1
ID G3P2_NOSS1 Reviewed; 337 AA.
AC P58554; Q93M82;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000303|PubMed:11327708};
DE Short=GAPDH 2 {ECO:0000303|PubMed:11327708};
DE EC=1.2.1.59 {ECO:0000250|UniProtKB:P10618};
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:11327708};
GN Name=gap2; OrderedLocusNames=all5062;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-320, FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
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).
RN [3]
RP PROTEIN SEQUENCE OF 265-272, AND MASS SPECTROMETRY.
RA Singh H., Rajaram H., Apte S.K.;
RL Submitted (DEC-2008) to UniProtKB.
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 NADP. 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 NADP to NADPH. The reduced NADPH is then
CC exchanged with the second NAD, and the thioester is attacked by a
CC nucleophilic inorganic phosphate to produce BPG.
CC {ECO:0000269|PubMed:11327708}.
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:0000305|PubMed:11327708}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P80506}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Expressed in vegetative cells and heterocysts,
CC however the expression is higher in vegetative cells than in
CC heterocysts. {ECO:0000269|PubMed:11327708}.
CC -!- MASS SPECTROMETRY: Mass=37115; Method=MALDI;
CC Evidence={ECO:0000269|Ref.3};
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000019; BAB76761.1; -; Genomic_DNA.
DR EMBL; AJ251774; CAC41001.1; -; Genomic_DNA.
DR PIR; AF2438; AF2438.
DR RefSeq; WP_010999188.1; NZ_RSCN01000014.1.
DR AlphaFoldDB; P58554; -.
DR SMR; P58554; -.
DR STRING; 103690.17134200; -.
DR EnsemblBacteria; BAB76761; BAB76761; BAB76761.
DR KEGG; ana:all5062; -.
DR eggNOG; COG0057; Bacteria.
DR OMA; NAKVLAW; -.
DR OrthoDB; 944149at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000002483; 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 1: Evidence at protein level;
KW Calvin cycle; Cytoplasm; Direct protein sequencing; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145625"
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 252
FT /note="K -> N (in Ref. 2; CAC41001)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="W -> C (in Ref. 2; CAC41001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36910 MW; 6671C88D5CC7E033 CRC64;
MIRVAINGFG RIGRNFARCW LGRENTNIEL VAVNDTSDPR TNAHLLKYDS MLGKLKNVDI
TADDNSITVN GKTIKCVSDR NPENLPWKEW EIDLIIEATG VFVSKEGATK HINAGAKKVL
ITAPGKNEDG TFVMGVNHHD YDHNLHNIIS NASCTTNCLA PIAKVLNDKF GIIKGSMTTT
HSYTGDQRLL DASHRDLRRA RAAAINIVPT STGAAKAVAL VIPELKGKLN GVALRVPTPN
VSMVDFVVQV EKRTITEEVN QALKDASEGP LKGILDYSEL QLVSSDYQGT DASSIVDANL
TLVMGNDLVK VMAWYDNEWG YSQRVLDLAE LVAEKWV
