ID   M3E098_9ACTN            Unreviewed;       481 AA.
AC   M3E098;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:EMF26746.1};
DE            EC=1.2.1.12 {ECO:0000313|EMBL:EMF26746.1};
GN   ORFNames=H114_22605 {ECO:0000313|EMBL:EMF26746.1};
OS   Streptomyces gancidicus BKS 13-15.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces pseudogriseolus group.
OX   NCBI_TaxID=1284664 {ECO:0000313|EMBL:EMF26746.1, ECO:0000313|Proteomes:UP000011732};
RN   [1] {ECO:0000313|EMBL:EMF26746.1, ECO:0000313|Proteomes:UP000011732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BKS 13-15 {ECO:0000313|EMBL:EMF26746.1,
RC   ECO:0000313|Proteomes:UP000011732};
RX   PubMed=23599292;
RA   Kumar S., Kaur N., Singh N.K., Raghava G.P., Mayilraj S.;
RT   "Draft Genome Sequence of Streptomyces gancidicus Strain BKS 13-15.";
RL   Genome Announc. 1:E00150-13(2013).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {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:EMF26746.1}.
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DR   EMBL; AOHP01000099; EMF26746.1; -; Genomic_DNA.
DR   RefSeq; WP_006134512.1; NZ_AOHP01000099.1.
DR   AlphaFoldDB; M3E098; -.
DR   PATRIC; fig|1284664.3.peg.4532; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000011732; 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   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; IPR036291; NAD(P)-bd_dom_sf.
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:0000313|EMBL:EMF26746.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011732}.
FT   DOMAIN          129..289
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   481 AA;  52485 MW;  13AD2F680C6F7664 CRC64;
     MTVNEDSFTN WKHREEIAES MIPIIGKLHR ERDVTVLLHS RSLVNKSVVS ILKTHRFARQ
     IAGEELSVTE TLPFLQALTT LDLGPSQIDI GLLAEAYRAD DQGKSVAEFT AEAVAGATGE
     NKIERREPRD VVLYGFGRIG RLLARLLIEK SGSGNGLRLR AIVVRRGGEQ DIVKRASLLR
     RDSVHGQFQG TITVDEANSA IVANGNVVKV IYADDPAQID YTAYGIDNAI LIDNTGRWRD
     REGLSQHLRP GVDKVVLTAP GKGDVPNIVH GVNHDTLKPD ERILSCASCT TNAIVPPLKA
     MADEYGVLRG HVETVHSFTN DQNLLDNYHK SERRGRSAPL NMVITETGAA SAVAKALPDL
     KAPITGSSIR VPVPDVSIAI LNLQLGRATN REEVLDHLRN VSLTSPLKRQ IDFISAPDAV
     SSDFIGSRHA SIVDAGALKV DGDNAILYLW YDNEFGYSCQ VVRVVQYVSG VEYPTYPAPA
     A
//