ID E4UCS0_LIBSC Unreviewed; 333 AA.
AC E4UCS0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN OrderedLocusNames=CKC_02050 {ECO:0000313|EMBL:ADR52161.1};
OS Liberibacter solanacearum (strain CLso-ZC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=658172 {ECO:0000313|EMBL:ADR52161.1, ECO:0000313|Proteomes:UP000007038};
RN [1] {ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|Proteomes:UP000007038};
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RT "Complete genome sequence of Candidatus Liberibacter solanacearum CLso-
RT ZC1.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CLso-ZC1;
RA Lin H., Doddapaneni H.V., Lou B., Civerolo E.L., Chen C., Duan Y., Zhou L.,
RA Glynn J.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADR52161.1, ECO:0000313|Proteomes:UP000007038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLso-ZC1 {ECO:0000313|EMBL:ADR52161.1,
RC ECO:0000313|Proteomes:UP000007038};
RX PubMed=21552483; DOI=10.1371/journal.pone.0019135;
RA Lin H., Lou B., Glynn J.M., Doddapaneni H., Civerolo E.L., Chen C.,
RA Duan Y., Zhou L., Vahling C.M.;
RT "The Complete Genome Sequence of 'Candidatus Liberibacter solanacearum',
RT the Bacterium Associated with Potato Zebra Chip Disease.";
RL PLoS ONE 6:E19135-E19135(2011).
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; CP002371; ADR52161.1; -; Genomic_DNA.
DR RefSeq; WP_013461817.1; NC_014774.1.
DR AlphaFoldDB; E4UCS0; -.
DR STRING; 658172.CKC_02050; -.
DR KEGG; lso:CKC_02050; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_5; -.
DR Proteomes; UP000007038; 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}.
FT DOMAIN 3..151
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 151
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 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 80
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 333 AA; 36343 MW; 47E49C9BD02A188B CRC64;
MVSKVSINGF GRIGRCVLRS AVESGRDDIR IVAINDLNSI ETIAHLFRYD SVHGRFPGEV
KISGDTIDVG FGAIKVTSIR DPQNLPWNDV DIAMECTGFF TTKEKASLHL SNGSKRVLVS
APCKGADKTI VYGINHTSLN ERDVIISNAS CTTNCLVPIV YVLDKMFGIE KGYMTTVHSY
TGDQHILDAG HDDPYRSRAA AISMIPTSTG AAKSVELVLP HLKGKLDGSS VRVPTPNVSM
VDLKCVTSRN VNVDEINAAM RDFAEGDMKN ILDYVALPLV SIDFNHNAYS SIFAADQTKV
VANNLVRVLA WYDNEWGFSN RMLDTASAIA KLL
//
