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Database: UniProt
Entry: A0A081NU86_9BACL
LinkDB: A0A081NU86_9BACL
Original site: A0A081NU86_9BACL 
ID   A0A081NU86_9BACL        Unreviewed;       348 AA.
AC   A0A081NU86;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000256|ARBA:ARBA00039578};
GN   ORFNames=ET33_28505 {ECO:0000313|EMBL:KEQ22009.1};
OS   Paenibacillus tyrfis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1501230 {ECO:0000313|EMBL:KEQ22009.1, ECO:0000313|Proteomes:UP000028123};
RN   [1] {ECO:0000313|EMBL:KEQ22009.1, ECO:0000313|Proteomes:UP000028123}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSt1 {ECO:0000313|EMBL:KEQ22009.1,
RC   ECO:0000313|Proteomes:UP000028123};
RA   Aw Y.K., Ong K.S., Gan H.M., Lee S.M.;
RT   "Draft genome sequence of Paenibacillus sp. MSt1.";
RL   Submitted (JUN-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEQ22009.1}.
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DR   EMBL; JNVM01000047; KEQ22009.1; -; Genomic_DNA.
DR   RefSeq; WP_036692738.1; NZ_JNVM01000047.1.
DR   AlphaFoldDB; A0A081NU86; -.
DR   eggNOG; COG0057; Bacteria.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000028123; Unassembled WGS sequence.
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   GO; GO:0050661; F:NADP binding; 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; 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.
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:KEQ22009.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028123}.
FT   DOMAIN          3..154
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   ACT_SITE        154
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         80
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         153..155
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         184
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         212..213
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         235
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-2"
FT   BINDING         316
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   SITE            181
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-4"
SQ   SEQUENCE   348 AA;  38094 MW;  3E7F9B4FC5FD5056 CRC64;
     MTGTIGVSGM GRIGRLLVRR AFDTDDNGMG LQAINSLYPA GTIAHLLKYD TIHGTWKADI
     REEGNDLIIN GKRIRIVFER DPAAISWKDL GVDLAIDATG KFNDREGASR HLTAGASKVL
     ITAPGKRMDL TVVMGVNDSR YNAKEHTLLS AASCTTNCVA PVLHVLDQAF QVKNGWMTTV
     HSYTNDQKHM DNPHSDLRRA RACTQSIIPT STGVGKALID VLPHLAPHVN GISVRVPTPD
     VSLVDLTVQV KRPVRLEEVQ AAFRQAAEGP MARYLGYSNE PLVSSDFIGC DQSAVIDGQS
     LMVAEDQIKV LAWYDNEWAY ASRVMDLAKV VSETMKKESD EAWKEALV
//
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