G3P_BORBU
ID G3P_BORBU Reviewed; 335 AA.
AC P46795; O51084;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 138.
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; OrderedLocusNames=BB_0057;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=8557349; DOI=10.1128/iai.64.1.262-268.1996;
RA Anda P., Gebbia J.A., Backenson P.B., Coleman J.L., Benach J.L.;
RT "A glyceraldehyde-3-phosphate dehydrogenase homolog in Borrelia burgdorferi
RT and Borrelia hermsii.";
RL Infect. Immun. 64:262-268(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND SUBSTRATE
RP ANALOG, AND SUBUNIT.
RG Seattle structural genomics center for infectious disease (SSGCID);
RT "Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from
RT Borrelia burgdorferi.";
RL Submitted (MAY-2009) to the PDB data bank.
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:0000269|Ref.3}.
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; U28760; AAB53930.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66450.1; -; Genomic_DNA.
DR PIR; A70107; A70107.
DR RefSeq; NP_212191.1; NC_001318.1.
DR RefSeq; WP_002658311.1; NC_001318.1.
DR PDB; 3HJA; X-ray; 2.20 A; A/B/C/D=1-335.
DR PDBsum; 3HJA; -.
DR AlphaFoldDB; P46795; -.
DR SMR; P46795; -.
DR STRING; 224326.BB_0057; -.
DR PRIDE; P46795; -.
DR EnsemblBacteria; AAC66450; AAC66450; BB_0057.
DR GeneID; 56568160; -.
DR KEGG; bbu:BB_0057; -.
DR PATRIC; fig|224326.49.peg.455; -.
DR HOGENOM; CLU_030140_0_2_12; -.
DR OMA; NCVAPMA; -.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; P46795; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:CAFA.
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; 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 3D-structure; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..335
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145636"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000305|Ref.3"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 31
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 75
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 198
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000269|Ref.3"
FT BINDING 318
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|Ref.3"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT CONFLICT 214
FT /note="A -> P (in Ref. 1; AAB53930)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> P (in Ref. 1; AAB53930)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:3HJA"
FT TURN 270..275
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:3HJA"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:3HJA"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:3HJA"
SQ SEQUENCE 335 AA; 36255 MW; 30E94F98839819C0 CRC64;
MKLAINGFGR IGRNVFKIAF ERGIDIVAIN DLTDPKTLAH LLKYDSTFGV YNKKVESRDG
AIVVDGREIK IIAERDPKNL PWAKLGIDVV IESTGVFSSA TSDKGGYLDH VNHAGAKKVI
LTVPAKDEIK TIVLGVNDHD INSDLKAVSN ASCTTNCLAP LAKVLHESFG IEQGLMTTVH
AYTNDQRILD LPHSDLRRAR AAALSIIPTS TGAAKAVGLV LPELKGKLNG TSMRVPVPTG
SIVDLTVQLK KKDVTKEEIN SVLRKASETP ELKGILGYTE DPIVSSDIKG NSHSSIVDGL
ETMVLENGFA KILSWYDNEF GYSTRVVDLA QKLVK
