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G3PB_TOBAC
ID   G3PB_TOBAC              Reviewed;         438 AA.
AC   P09044;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase B, chloroplastic;
DE            EC=1.2.1.13;
DE   AltName: Full=NADP-dependent glyceraldehydephosphate dehydrogenase subunit B;
DE   Flags: Precursor; Fragment;
GN   Name=GAPB;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3757034; DOI=10.1016/0092-8674(86)90367-3;
RA   Shih M.-C., Lazar G., Goodman H.M.;
RT   "Evidence in favor of the symbiotic origin of chloroplasts: primary
RT   structure and evolution of tobacco glyceraldehyde-3-phosphate
RT   dehydrogenases.";
RL   Cell 47:73-80(1986).
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=1.2.1.13;
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Tetramer of either four A chains (GAPDH 2) or two A and two B
CC       chains (GAPDH 1). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- MISCELLANEOUS: Plants contain two types of GAPDH: cytosolic forms which
CC       participate in glycolysis and chloroplast forms which participate in
CC       photosynthesis. All the forms are encoded by distinct genes.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; M14418; AAA34076.1; -; mRNA.
DR   PIR; B24430; B24430.
DR   AlphaFoldDB; P09044; -.
DR   SMR; P09044; -.
DR   STRING; 4097.P09044; -.
DR   PRIDE; P09044; -.
DR   ProMEX; P09044; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR   GO; GO:0047100; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IBA:GO_Central.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
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   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   2: Evidence at transcript level;
KW   Calvin cycle; Chloroplast; NADP; Oxidoreductase; Plastid;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         <1..53
FT                   /note="Chloroplast"
FT   CHAIN           54..438
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase B,
FT                   chloroplastic"
FT                   /id="PRO_0000010428"
FT   ACT_SITE        208
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT   BINDING         64..65
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         88
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..209
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..267
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         289
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250"
FT   BINDING         372
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            235
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   438 AA;  47470 MW;  7E8DB0F68F206B09 CRC64;
     CLSKKFEVAE FAGLRSSGCV TFSNKESSFF DVVSAQLTPK TTRSTPVKGE TVAKLKVAIN
     GFGRIGRNFL RCWHGRKDSP LDVVVVNDSG GVKNASHLLK YDSMLGTFKA DVKIVDNETI
     SVDGKHIKVV SSRDPLKLPW AELGIDIVIE GTGVFVDGPG AGKHIQAGAK KVIITAPAKG
     ADIPTYVVGV NEQDYSHEVA DIISNASCTT NCLAPFVKVM DEELGIVKGT MTTTHSYTGD
     QRLLDASHRD LRRARAAALN IVPTSTGAAK AVSLVLPQLK GKLNGIALRV PTPNVSVVDL
     VVNVAKKGIT AEDVNAAFRK AADGPLKGVL AVCDEPLVSV DFRCSDVSST IDSSLTMVMG
     DDMVKVVAWY DNEWGYSQRV VDLAHLVANN WPGSCSTRKW RSHWMSFARQ ILLMRNAKSM
     NNRFCYVSSF EMDDFRSQ
 
 
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