ID A0A0X3XY02_9ACTN Unreviewed; 481 AA.
AC A0A0X3XY02;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE EC=1.2.1.- {ECO:0000256|RuleBase:RU361160};
GN ORFNames=ADL34_02535 {ECO:0000313|EMBL:KUL79799.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL79799.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL79799.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL79799.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL79799.1}.
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DR EMBL; LLZN01000002; KUL79799.1; -; Genomic_DNA.
DR RefSeq; WP_062669792.1; NZ_LLZN01000002.1.
DR AlphaFoldDB; A0A0X3XY02; -.
DR OrthoDB; 9803304at2; -.
DR Proteomes; UP000052945; Unassembled WGS sequence.
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; PTHR43454; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR43454:SF1; GP_DH_N DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361160};
KW Reference proteome {ECO:0000313|Proteomes:UP000052945}.
FT DOMAIN 129..289
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 481 AA; 52447 MW; 4C2983A227FEEE0F CRC64;
MTVNDDSFTS WKNREEIAES MIPIIGKLHR ERDVTVLLHS RSLVNKSVVS ILKTHRFARQ
IAGEELSVTE TLPFLQALAA LDLGPSQIDL GILASTYKAD DRGLTVEAFT AEAVAGATGA
NKIERGEGRD VVLYGFGRIG RLVARLLIEK SGSGNGLRLR AIVVRGGGER DIVKRASLLR
RDSIHGQFQG TITVDEASST IFANGNAIKV IYANDPSEVD YTAYGIKNAI LIDNTGKWRD
REGLSKHLRP GVDKVVLTAP GKGDVPNIVH GVNHDTIKPD EQILSCASCT TNAIVPPLKA
MDDEYGVQRG HVETVHSFTN DQNLLDNYHK SERRGRSAPL NMVITETGAA SAVAKALPDL
KARITGSSIR VPVPDVSIAI LNLQLKRETT REEVHDYLRE VSLTSPLRRQ IDFITAPDAV
SSDFIGSRHA SIVDAGALKV EGDNAILYLW YDNEFGYSCQ VIRVVQHVSG VEYPTYPAPA
V
//
