ID D1ATE3_ANACI Unreviewed; 334 AA.
AC D1ATE3;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:ACZ48821.1};
DE EC=1.2.1.12 {ECO:0000313|EMBL:ACZ48821.1};
GN Name=gap {ECO:0000313|EMBL:ACZ48821.1};
GN OrderedLocusNames=ACIS_00119 {ECO:0000313|EMBL:ACZ48821.1};
OS Anaplasma centrale (strain Israel) (Anaplasma marginale subsp. centrale
OS (strain Israel)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=574556 {ECO:0000313|EMBL:ACZ48821.1, ECO:0000313|Proteomes:UP000000630};
RN [1] {ECO:0000313|EMBL:ACZ48821.1, ECO:0000313|Proteomes:UP000000630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Israel {ECO:0000313|EMBL:ACZ48821.1,
RC ECO:0000313|Proteomes:UP000000630};
RX PubMed=19854912; DOI=10.1128/JB.01330-09;
RA Herndon D.R., Palmer G.H., Shkap V., Knowles D.P. Jr., Brayton K.A.;
RT "Complete genome sequence of Anaplasma marginale subsp. centrale.";
RL J. Bacteriol. 192:379-380(2010).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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DR EMBL; CP001759; ACZ48821.1; -; Genomic_DNA.
DR RefSeq; WP_012880308.1; NC_013532.1.
DR AlphaFoldDB; D1ATE3; -.
DR STRING; 574556.ACIS_00119; -.
DR KEGG; acn:ACIS_00119; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_5; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000000630; Chromosome.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
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:0000313|EMBL:ACZ48821.1}.
FT DOMAIN 2..153
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-1"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 152..154
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 183
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 180
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 334 AA; 36260 MW; 31E21304D019A2A1 CRC64;
MLRIGINGLG RIGRCLFRML FENNIPDMEL VAVNGSSSLE LHKHLLKNDS VHGKFGSDID
IKDGGFFEVS GKTVKFFKEK QPQDIPWEDV GVNVVLECTG KFNNKESSEL HLGGTVRKVV
VSAPVTNADI QVIFGVNEGD IDGSHDVISV GSCTTNCAAH VVKAMDEAFG IEGGFVTTVH
AYTNDQNHVD GSHKDLRRAR ACGLSMIPTT TGASIALEAL FPRLSGKLSA SSIRVPTPNV
SVVDFAFVSS FKTTVELING ALLKAATARP DVLMASNEPL VSSDFNHTTY SAVFDLMETY
ANNGNVSRVL AWYDNEWAFA ARMIDVSREL SRFL
//
