G3P_CHLTR
ID G3P_CHLTR Reviewed; 334 AA.
AC P0CE13; O84513; Q46450;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
GN Name=gap; Synonyms=gapA; OrderedLocusNames=CT_505;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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:0000250|UniProtKB:P00362}.
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}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; AE001273; AAC68106.1; -; Genomic_DNA.
DR PIR; G71504; G71504.
DR RefSeq; NP_220020.1; NC_000117.1.
DR RefSeq; WP_009871869.1; NC_000117.1.
DR PDB; 6OK4; X-ray; 2.40 A; A/B/C/D=1-334.
DR PDB; 6WYC; X-ray; 1.50 A; A/B/C/D=1-334.
DR PDB; 6X2E; X-ray; 1.80 A; A/B/C/D=1-334.
DR PDBsum; 6OK4; -.
DR PDBsum; 6WYC; -.
DR PDBsum; 6X2E; -.
DR AlphaFoldDB; P0CE13; -.
DR SMR; P0CE13; -.
DR STRING; 813.O172_02790; -.
DR EnsemblBacteria; AAC68106; AAC68106; CT_505.
DR GeneID; 884280; -.
DR KEGG; ctr:CT_505; -.
DR PATRIC; fig|272561.5.peg.549; -.
DR HOGENOM; CLU_030140_0_3_0; -.
DR InParanoid; P0CE13; -.
DR OMA; NCVAPMA; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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; PTHR10836; PTHR10836; 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 3D-structure; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145643"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:6WYC"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:6WYC"
FT TURN 84..88
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6WYC"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:6WYC"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:6X2E"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:6WYC"
FT TURN 266..271
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:6WYC"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6WYC"
FT STRAND 299..312
FT /evidence="ECO:0007829|PDB:6WYC"
FT HELIX 316..331
FT /evidence="ECO:0007829|PDB:6WYC"
SQ SEQUENCE 334 AA; 36275 MW; 3F4DEED6F073ADCD CRC64;
MRIVINGFGR IGRLVLRQIL KRNSPIEVVA INDLVAGDLL TYLFKYDSTH GSFAPQATFS
DGCLVMGERK VHFLAEKDVQ KLPWKDLDVD VVVESTGLFV NRDDVAKHLD SGAKRVLITA
PAKGDVPTFV MGVNHQQFDP ADVIISNASC TTNCLAPLAK VLLDNFGIEE GLMTTVHAAT
ATQSVVDGPS RKDWRGGRGA FQNIIPASTG AAKAVGLCLP ELKGKLTGMA FRVPVADVSV
VDLTVKLSSA TTYEAICEAV KHAANTSMKN IMYYTEEAVV SSDFIGCEYS SVFDAQAGVA
LNDRFFKLVA WYDNEIGYAT RIVDLLEYVQ ENSK
