ID J1ZS57_9ACTN Unreviewed; 334 AA.
AC J1ZS57;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:EJJ04421.1, ECO:0000313|EMBL:QTZ91354.1};
GN Name=gap {ECO:0000313|EMBL:QTZ91354.1};
GN ORFNames=SU9_007605 {ECO:0000313|EMBL:QTZ91354.1}, SU9_23917
GN {ECO:0000313|EMBL:EJJ04421.1};
OS Streptomyces auratus AGR0001.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1160718 {ECO:0000313|EMBL:EJJ04421.1};
RN [1] {ECO:0000313|EMBL:EJJ04421.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AGR0001 {ECO:0000313|EMBL:EJJ04421.1};
RX PubMed=22965094; DOI=10.1128/JB.01155-12;
RA Han X., Li M., Ding Z., Zhao J., Ji K., Wen M., Lu T.;
RT "Genome Sequence of Streptomyces auratus Strain AGR0001, a Phoslactomycin-
RT Producing Actinomycete.";
RL J. Bacteriol. 194:5472-5473(2012).
RN [2] {ECO:0000313|EMBL:QTZ91354.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AGR0001 {ECO:0000313|EMBL:QTZ91354.1};
RA Wen M.-L., Han X.-L., Xiong J.;
RL Submitted (APR-2021) 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}.
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DR EMBL; AJGV01000144; EJJ04421.1; -; Genomic_DNA.
DR EMBL; CP072931; QTZ91354.1; -; Genomic_DNA.
DR RefSeq; WP_006606292.1; NZ_CP072931.1.
DR AlphaFoldDB; J1ZS57; -.
DR STRING; 1160718.SU9_23917; -.
DR KEGG; sauh:SU9_007605; -.
DR PATRIC; fig|1160718.3.peg.4838; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_0_2_11; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000009036; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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; 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|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000149-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000009036}.
FT DOMAIN 3..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 12..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000149-3"
FT BINDING 121
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; 36301 MW; DB35E1F9CF8F4A02 CRC64;
MTIRVGINGF GRIGRNYFRA LLEQGADIEI VGVNDLTDNA TLVHLLKYDT ILGRLKQDVS
HTDDTITVGN QTFKTMAERD PANLPWAALG ADIVIESTGI FTKKADAEKH IQAGAKKVLI
SAPAKDEDIT IVMGVNNDKY DAAKHHVISN ASCTTNCVAP MAKVLDENFG IVKGLMTTVH
AYTNDQRILD FPHSDLRRAR AAAENIIPTS TGAAKATALV LPQLKGKLDG IAMRVPVPTG
SVTDLVLELD REVTRDEINT AFQKAAEGQL KGILEYTEDP IVSSDIVNFP ASCTFDSKLT
MSQGKQVKVV GWYDNEWGYS NRLVDLTTFV GGQL
//
