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Database: UniProt
Entry: A0A1Q5MTL6_9ACTN
LinkDB: A0A1Q5MTL6_9ACTN
Original site: A0A1Q5MTL6_9ACTN 
ID   A0A1Q5MTL6_9ACTN        Unreviewed;       484 AA.
AC   A0A1Q5MTL6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000313|EMBL:OKK17574.1};
GN   ORFNames=AMK16_22515 {ECO:0000313|EMBL:OKK17574.1};
OS   Streptomyces sp. CB00455.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK17574.1, ECO:0000313|Proteomes:UP000185643};
RN   [1] {ECO:0000313|EMBL:OKK17574.1, ECO:0000313|Proteomes:UP000185643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB00455 {ECO:0000313|EMBL:OKK17574.1,
RC   ECO:0000313|Proteomes:UP000185643};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKK17574.1}.
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DR   EMBL; LIVQ01000005; OKK17574.1; -; Genomic_DNA.
DR   RefSeq; WP_073918555.1; NZ_LIVQ01000005.1.
DR   AlphaFoldDB; A0A1Q5MTL6; -.
DR   STRING; 1703927.AMK16_22515; -.
DR   OrthoDB; 9803304at2; -.
DR   Proteomes; UP000185643; Unassembled WGS sequence.
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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185643}.
FT   DOMAIN          129..292
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   484 AA;  52567 MW;  3C58104B14735738 CRC64;
     MTVNDDSFTN WKNREEIAES MIPIIGKLHR ERDVTVLLHS RSLVNKSVVS ILKTHRFARQ
     IAGEELSVTE TLPFLQALAA LDLGPSQIDI GMLAATYKSD DRGLSVQDFT AEAVVGATGA
     NKIERSESRD VVLYGFGRIG RLVARLLIEK AGSGNGLRLR AIVVRGGGGR AAEDLVKRAS
     LLRRDSIHGQ FQGTITVDEA SSKIIANGNE IKVIYANDPS EVDYTAYGIK DAILIDNTGK
     WRDREGLSKH LRPGVAKVVL TAPGKGDVPN IVHGVNHDTI KPDEQILSCA SCTTNAIVPP
     LKAMADEYGV LRGHVETVHS FTNDQNLLDN YHGSDRRGRS APLNMVLTET GAASAVAKAL
     PDLKARITGS SIRVPVPNVS IAILNLRLGR ETTREEVLDH LRDVSLNSPL KRQIDFISAP
     DAVSSDFIGS RHSSIIDAGA TKVEGDDAIL YLWYDNEFGY SCQVIRVVQH VSGVEYPTYP
     VPAV
//
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