ID Q47KE5_THEFY Unreviewed; 804 AA.
AC Q47KE5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Trehalose 6-phosphate phosphorylase {ECO:0000313|EMBL:AAZ57077.1};
DE EC=2.4.1.216 {ECO:0000313|EMBL:AAZ57077.1};
GN OrderedLocusNames=Tfu_3044 {ECO:0000313|EMBL:AAZ57077.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ57077.1};
RN [1] {ECO:0000313|EMBL:AAZ57077.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YX {ECO:0000313|EMBL:AAZ57077.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Lykidis A., Richardson P.;
RT "Complete sequence of Thermobifida fusca YX.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family.
CC {ECO:0000256|ARBA:ARBA00006768}.
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DR EMBL; CP000088; AAZ57077.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47KE5; -.
DR STRING; 269800.Tfu_3044; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR KEGG; tfu:Tfu_3044; -.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_1_1_11; -.
DR OrthoDB; 9816160at2; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0050503; F:trehalose 6-phosphate phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 1.
DR Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR PANTHER; PTHR11051; GLYCOSYL HYDROLASE-RELATED; 1.
DR PANTHER; PTHR11051:SF8; PROTEIN-GLUCOSYLGALACTOSYLHYDROXYLYSINE GLUCOSIDASE; 1.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Glycosyltransferase {ECO:0000313|EMBL:AAZ57077.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAZ57077.1}.
FT DOMAIN 8..259
FT /note="Glycoside hydrolase family 65 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03636"
FT DOMAIN 314..708
FT /note="Glycoside hydrolase family 65 central catalytic"
FT /evidence="ECO:0000259|Pfam:PF03632"
FT DOMAIN 718..781
FT /note="Glycoside hydrolase family 65 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03633"
FT ACT_SITE 489
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-50"
FT BINDING 350..351
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
FT BINDING 609..610
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR036289-51"
SQ SEQUENCE 804 AA; 90255 MW; BC46A2496B763015 CRC64;
MNPWLLRYDG FDPATEGLRE ALCTLGNGVF ATRGAAPESR ADGVHYPGTY LAGCYNRLTS
IVADHEVTNE DLVNIPNWLP FTFRAADGSW LGDGAELTDQ QLELDMRRGV LTRTGTVVDK
EGRRTRLVQR RLVSMDDRHL AALETTLIPE NWAGPLTVRV GLDGRVTNSG VARYRDLNSD
HLRPGGTEGD EAGRMWLRCR TSTSDIEIVL AARTTVTTGP APQKTQVTCQ DELVEQTLEI
PAAQGEQVTV EKIVAVYSSL DHAVSNRREA ARAAVEHAAD FTGLLHRHAT AWRHLWRRCD
VTISNPEHTM VLHLHLFHIL QTLSPHTADL DVGMPARGLH GEAYRGHVFW DELFVFPFLN
TRFPQIARSL LRYRWRRLPA ARAAARAAGY RGAMFPWQSG MDGREETQRL HLNPRSGHWI
PDASHLQRHV GLAIAYNVWQ HYQVTEDVDF LLDFGAELLV DIARFFASLA TFDRSQNRYV
IRGVMGPDEY HEGYPDRDEP GLDDNAYTNI MAVWVLRRAL DVLRILPDGS RAELMERLGM
GLDELALFED VRTRMRVPFH EGVISQFAGY EHLVELDWEH YRNTYGDIRR LDRILEAEGD
TCDRYKVSKQ ADVLMLFFLL SPDEFADILT DLGYEYDPGL IPRTIHYYLA RTSHGSTLSA
AVHAWVMART RHTASWQFFV EALRSDIADV QGGTTAEGIH LGAMASTVDL VTRCYTGLEI
RHGVLHLDPE LPSEIDSLSF VLPYQGHWGI RLSFHRNEVR ISVPPSTAPP VTVHVAGQTA
RVPAGCDHVF VLGGGASQDQ GPPL
//
