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Database: UniProt
Entry: Q84I01_NEIGO
LinkDB: Q84I01_NEIGO
Original site: Q84I01_NEIGO 
ID   Q84I01_NEIGO            Unreviewed;       341 AA.
AC   Q84I01;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   13-SEP-2023, entry version 90.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
DE   Flags: Fragment;
GN   Name=gpdh {ECO:0000313|EMBL:AAO19950.1};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485 {ECO:0000313|EMBL:AAO19950.1};
RN   [1] {ECO:0000313|EMBL:AAO19950.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12517848; DOI=10.1128/JCM.41.1.197-204.2003;
RA   Viscidi R.P., Demma J.C.;
RT   "Genetic diversity of Neisseria gonorrhoeae housekeeping genes.";
RL   J. Clin. Microbiol. 41:197-204(2003).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; AF520281; AAO19950.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q84I01; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR43148:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000149-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160}.
FT   DOMAIN          3..155
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         81
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         154..156
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         185
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         213..214
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         236
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         319
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            182
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
FT   NON_TER         341
FT                   /evidence="ECO:0000313|EMBL:AAO19950.1"
SQ   SEQUENCE   341 AA;  36678 MW;  FDBAAB2997757AA8 CRC64;
     MGIKVAINGY GRIGRQVLRS IYDYQIQDQL QIVAVNASGS LETNAHLTKF DTVHGRFEAD
     VSHDGGNLIV NGDKIPFFST RNPAELPWKE LGVDLVMECT GAFTSKEKAK IHLESGAKKV
     LISAPGGDDV DATVVYGVND SVLTADMTVV SNASCTTNCL SPVAKVLSES VGIVKGAMTT
     IHALTNDQTV TDVRHKDLRR ARSGVENMIP TKTGAAKAVG LVLPELKGRL DGLAIRVPTV
     NVSLVDLSLQ AARDTTVEEI NALMKAASEA GALKGVLGYN TLPLVSMDFN HTTEASHFDA
     TLTKVVDGNM VKVFAWYDNE WGFSCQMLNT ARRMFGLEVR P
//
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