G3P2_SYNY3
ID G3P2_SYNY3 Reviewed; 337 AA.
AC P80505;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000303|PubMed:9226260};
DE EC=1.2.1.59 {ECO:0000269|PubMed:9226260};
DE AltName: Full=GAPDH 2 {ECO:0000303|PubMed:9226260};
DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:9226260};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:9226260};
GN Name=gap2; OrderedLocusNames=sll1342;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP AND SUBSTRATE SPECIFICITY.
RC STRAIN=strain PCC 6803 / Kazusa;
RX PubMed=9226260; DOI=10.1128/jb.179.14.4513-4522.1997;
RA Valverde F., Losada M., Serrano A.;
RT "Functional complementation of an Escherichia coli gap mutant supports an
RT amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate
RT dehydrogenase of Synechocystis sp. strain PCC 6803.";
RL J. Bacteriol. 179:4513-4522(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schubert M., Brinkmann H., Cerff R.;
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [4]
RP PROTEIN SEQUENCE OF 2-11.
RA Valverde F., Serrano A.;
RL Submitted (NOV-1995) to UniProtKB.
CC -!- FUNCTION: Involved in photosynthetic carbon assimilation. Catalyzes the
CC NAD(P)-dependent oxidative phosphorylation of glyceraldehyde 3-
CC phosphate (G3P) to 1,3-bisphosphoglycerate (BPG). The first reaction
CC step involves the formation of a hemiacetal intermediate between G3P
CC and a cysteine residue, and this hemiacetal intermediate is then
CC oxidized to a thioester, with concomitant reduction of NAD to NADH. The
CC reduced NADH is then exchanged with the second NAD, and the thioester
CC is attacked by a nucleophilic inorganic phosphate to produce BPG. It
CC can use both NADP and NAD. {ECO:0000269|PubMed:9226260}.
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:0000269|PubMed:9226260};
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:0000269|PubMed:9226260};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9226260}.
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; X83564; CAA58550.1; -; Genomic_DNA.
DR EMBL; X86376; CAA60135.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA18633.1; -; Genomic_DNA.
DR PIR; S54141; S54141.
DR AlphaFoldDB; P80505; -.
DR SMR; P80505; -.
DR IntAct; P80505; 3.
DR STRING; 1148.1653722; -.
DR PaxDb; P80505; -.
DR PRIDE; P80505; -.
DR EnsemblBacteria; BAA18633; BAA18633; BAA18633.
DR KEGG; syn:sll1342; -.
DR eggNOG; COG0057; Bacteria.
DR InParanoid; P80505; -.
DR OMA; NAKVLAW; -.
DR PhylomeDB; P80505; -.
DR SABIO-RK; P80505; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000001425; 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; IBA:GO_Central.
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 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 Cytoplasm; Direct protein sequencing; Glycolysis; NAD; NADP;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..337
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000145709"
FT ACT_SITE 154
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 121
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
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="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 181
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT CONFLICT 57
FT /note="A -> G (in Ref. 1; CAA58550)"
FT /evidence="ECO:0000305"
FT CONFLICT 162..163
FT /note="FG -> IA (in Ref. 2; CAA60135/BAA18633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36512 MW; FC8FF0E7FEAC1585 CRC64;
MTRVAINGFG RIGRNFLRCW LGRTDSQLEV VGINDTSDPR TNAHLLRYDS MLGKLDADIS
ADENSITVNG KTIKCVSDRN PLNLPWAEWN VDLVIEATGV FVTHEGATKH VQAGAKKVLI
TAPGKGPNIG TYVVGVNAHE YKHEEYEVIS NASCTTNCLA PFGKVINDNF GIIKGTMTTT
HSYTGDQRIL DASHRDLRRA RAAAVNIVPT STGAAKAVAL VIPELQGKLN GIALRVPTPN
VSVVDLVVQV EKNTIAEQVN GVLKEAANTS LKGVLEYTDL ELVSSDFRGT DCSSTVDGSL
TMVMGGDMVK VIAWYDNEWG YSQRVVDLAE IVAKNWK
