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Database: UniProt
Entry: A0A2X0IUG2_9ACTN
LinkDB: A0A2X0IUG2_9ACTN
Original site: A0A2X0IUG2_9ACTN 
ID   A0A2X0IUG2_9ACTN        Unreviewed;       333 AA.
AC   A0A2X0IUG2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN   Name=gap {ECO:0000313|EMBL:RAG87011.1};
GN   ORFNames=DN069_03360 {ECO:0000313|EMBL:RAG87011.1};
OS   Streptacidiphilus pinicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=2219663 {ECO:0000313|EMBL:RAG87011.1, ECO:0000313|Proteomes:UP000248889};
RN   [1] {ECO:0000313|EMBL:RAG87011.1, ECO:0000313|Proteomes:UP000248889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMS16-CNU450 {ECO:0000313|EMBL:RAG87011.1,
RC   ECO:0000313|Proteomes:UP000248889};
RA   Roh S.G., Park S., Kim M.-K., Yun B.-R., Park J., Kim M.J., Kim Y.S.,
RA   Kim S.B.;
RT   "Streptacidiphilus pinicola sp. nov., isolated from pine grove soil.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC       phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC       NAD. The first reaction step involves the formation of a hemiacetal
CC       intermediate between G3P and a cysteine residue, and this hemiacetal
CC       intermediate is then oxidized to a thioester, with concomitant
CC       reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC       second NAD, and the thioester is attacked by a nucleophilic inorganic
CC       phosphate to produce BPG. {ECO:0000256|ARBA:ARBA00003501}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001810};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
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:RAG87011.1}.
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DR   EMBL; QKYN01000014; RAG87011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2X0IUG2; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000248889; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProt.
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; 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:SF2; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43148; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000248889}.
FT   DOMAIN          2..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         11..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT   BINDING         34
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         314
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   333 AA;  35045 MW;  89CE094884A2777A CRC64;
     MTRIAVNGFG RIGRNVLRAL LERDSKLEVV AVNDLTEPAT LARLLAYDTT AGRLGRPVTV
     DGDALVVDGR RITVTAERDP AQLPWAELGV DVVLEATGRF TAATAARAHL TAGARKVLVS
     APSDGADVTL AYGVNSDAYD PERHTVISNA SCTTNALAPL AGVLDDLAGI EHGFMTTVHA
     YTQEQNLQDG PHRDARRARA AAVNIVPTTT GAAKAIGLVL PQLDGKLSGD SIRVPVPVGS
     IVELNTTVAR DVTRDEVLEA YRAAAAGPLA GVLEYSDDPL VSADITGNPA SSIFDSALTR
     VDGRHVKVVA WYDNEWGFSN RVVDTLDLIA AGL
//
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