ID A0A0A8E897_9COXI Unreviewed; 335 AA.
AC A0A0A8E897;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN Name=gapA {ECO:0000313|EMBL:AJC50184.1};
GN ORFNames=Z664_00210 {ECO:0000313|EMBL:AJC50184.1};
OS Coxiella endosymbiont of Amblyomma americanum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=325775 {ECO:0000313|EMBL:AJC50184.1, ECO:0000313|Proteomes:UP000059222};
RN [1] {ECO:0000313|EMBL:AJC50184.1, ECO:0000313|Proteomes:UP000059222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C904 {ECO:0000313|EMBL:AJC50184.1};
RA Raghavan R., Smith T.A.;
RT "Endosymbiont of Amblyomma americanum.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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; CP007541; AJC50184.1; -; Genomic_DNA.
DR RefSeq; WP_039669757.1; NZ_CP007541.1.
DR AlphaFoldDB; A0A0A8E897; -.
DR STRING; 325775.Z664_00210; -.
DR KEGG; cea:Z664_00210; -.
DR HOGENOM; CLU_030140_0_2_6; -.
DR Proteomes; UP000059222; Chromosome.
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; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR PANTHER; PTHR43148:SF2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000059222}.
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 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 124
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 317
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"
SQ SEQUENCE 335 AA; 37020 MW; 84E12889E8CE9FBB CRC64;
MSYKIAINGC GRIGRNILRA FYESKKQYDF KIIAINDLGD INTNVHLIKY DSVHGKFPAN
IGVDREELIV INGDKIRLFS IKNPEFLPWK ALGIDVVLEC TGVFASKEKS KAHLAAGAEK
VLISAPAGNN VKTIVFGVNE HLLNQKDKIV SNASCTTNCL APLIKVLDDA IGIKRGLMVT
IHAYTNDQNL TDSYHKDLHR ARAATQSMIP TSTGATAAVE LVLPQLKGKL DGYAVRVPTV
NVSMVDFTFD AKKTVKVLEM HSVIKETADS KMQGILGYNE DPLVSIDFNH DPRSSIFDAG
QTRIIDKLVK IIAWYDNEWG FSNRMLDVTD ALLKC
//