ID C9YX26_STRSW Unreviewed; 484 AA.
AC C9YX26;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Putative glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:CBG75281.1};
GN OrderedLocusNames=SCAB_83281 {ECO:0000313|EMBL:CBG75281.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG75281.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG75281.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG75281.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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DR EMBL; FN554889; CBG75281.1; -; Genomic_DNA.
DR RefSeq; WP_013005720.1; NC_013929.1.
DR AlphaFoldDB; C9YX26; -.
DR STRING; 680198.SCAB_83281; -.
DR GeneID; 24311883; -.
DR KEGG; scb:SCAB_83281; -.
DR eggNOG; COG0057; Bacteria.
DR HOGENOM; CLU_030140_1_1_11; -.
DR Proteomes; UP000001444; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; 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 Reference proteome {ECO:0000313|Proteomes:UP000001444}.
FT DOMAIN 129..292
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 484 AA; 52511 MW; D128828D262F7344 CRC64;
MTVNEDSFTQ WKNREEIAES MIPIIGKLHR ERDVTILLHS RSLVNKSVVS ILKTHRFARQ
IAGEELSVTD TLPFLRTLTS LDLGPSQIDI GLLAEAHRAD DRGLSVEEFT AEAVAGATGA
NKIEGSEGRD VVLYGFGRIG RLVARLLIEK AGSGNGLRLR AIVVRGGGER AGEDIVKRAS
LLRRDSIHGQ FQGTITVDEA TSTINANGNE IKVIYAGDPS EIDYTEYGIK NAILIDNTGK
WRDRAGLSNH LRPGIDKVVL TAPGKGDVPN IVHGVNHDTI KPDERILSCA SCTTNAIVPP
LKAMADEFGV LRGHVETVHS FTNDQNLLDN YHKSDRRGRS APLNMVITET GAASAVAKAL
PDLKAPITGS SIRVPVPDVS IAILSLRLGR ETDRDEVVDY LRGVSLTSPL KRQIDFTNAP
DSVSSDFIGS RHASIVDAGA TKVDGDNAIL YLWYDNEFGY SCQVIRVVQH VSGVEYPTYP
SPAV
//
