ID A0A0J6EEY0_9BACI Unreviewed; 340 AA.
AC A0A0J6EEY0; A0A0J6F124;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-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 ORFNames=AB447_213920 {ECO:0000313|EMBL:KRT94747.1}, COP00_09045
GN {ECO:0000313|EMBL:ATH92746.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:KRT94747.1, ECO:0000313|Proteomes:UP000036168};
RN [1] {ECO:0000313|EMBL:KRT94747.1, ECO:0000313|Proteomes:UP000036168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT94747.1,
RC ECO:0000313|Proteomes:UP000036168};
RX PubMed=26297378; DOI=10.1099/ijsem.0.000462;
RA Kim S.J., Dunlap C.A., Kwon S.W., Rooney A.P.;
RT "Bacillus glycinifermentans sp. nov., isolated from fermented soybean
RT paste.";
RL Int. J. Syst. Evol. Microbiol. 65:3586-3590(2015).
RN [2] {ECO:0000313|EMBL:KRT94747.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GO-13 {ECO:0000313|EMBL:KRT94747.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ATH92746.1, ECO:0000313|Proteomes:UP000218414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBN06P03352 {ECO:0000313|EMBL:ATH92746.1,
RC ECO:0000313|Proteomes:UP000218414};
RA Yu W.-S., Do H.-N., Cheong H.-M., Hwang K.-J.;
RT "Whole genome sequencing of Bacillus glycinfermentans NCCP 15922.";
RL Submitted (SEP-2017) 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}.
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DR EMBL; CP023481; ATH92746.1; -; Genomic_DNA.
DR EMBL; LECW02000005; KRT94747.1; -; Genomic_DNA.
DR RefSeq; WP_048353882.1; NZ_LECW02000005.1.
DR AlphaFoldDB; A0A0J6EEY0; -.
DR STRING; 1664069.BGLY_3440; -.
DR PATRIC; fig|1664069.3.peg.173; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000036168; Unassembled WGS sequence.
DR Proteomes; UP000218414; 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..152
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT ACT_SITE 152
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 78
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 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 210..211
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT BINDING 233
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 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ SEQUENCE 340 AA; 37109 MW; EE22E4BA460B2327 CRC64;
MKVKVAINGF GRIGRMVFRK AMLDDQIDIA VINASYPAET LAHLIKYDTN HGRYELDVKA
CGDHLLVNGK KVLLTSQRDP KFLPWAEHDI DIVVEATGKF NSKEKAEAHI EAGAKKVILT
APGKNEDITI VMGVNEGDFD AERHTIISNA SCTTNCLAPV AKVLDDAFGI ENGLVTTVHA
FTNDQKNIDN PHKDLRRARA CGSSIIPTTT GAAKALSLVM PHLKGRMHGL ALRVPVPNVS
LVDLVADLKS DVTAEDINEA FRMAAAGSMA GIIDVCDEPL VSSDFNTNPF SAVIDSLSTM
VLENRKMKVL AWYDNEWGYS CRVVDLIRYV ASRMKHPSAV
//
