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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//