ID   TREPP_LACLA             Reviewed;         769 AA.
AC   Q9CID5; Q9ZAG0;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Trehalose 6-phosphate phosphorylase;
DE            Short=TrePP;
DE            EC=2.4.1.216;
GN   Name=trePP; OrderedLocusNames=LL0428; ORFNames=L39593;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9, AND
RP   CHARACTERIZATION.
RC   STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX   PubMed=11553642; DOI=10.1074/jbc.m108279200;
RA   Andersson U., Levander F., Raedstroem P.;
RT   "Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway
RT   for trehalose utilization in Lactococcus lactis.";
RL   J. Biol. Chem. 276:42707-42713(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Catalyzes the conversion of trehalose 6-phosphate into
CC       glucose 1-phosphate and glucose 6-phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose 6-phosphate + phosphate = beta-D-glucose
CC         1-phosphate + D-glucose 6-phosphate; Xref=Rhea:RHEA:20864,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57684, ChEBI:CHEBI:58429,
CC         ChEBI:CHEBI:61548; EC=2.4.1.216;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.3.;
CC       Temperature dependence:
CC         Optimum temperature is 35 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR   EMBL; Y18267; CAA77100.1; -; Genomic_DNA.
DR   EMBL; AE005176; AAK04526.1; -; Genomic_DNA.
DR   PIR; D86678; D86678.
DR   RefSeq; NP_266584.1; NC_002662.1.
DR   RefSeq; WP_010905330.1; NC_002662.1.
DR   AlphaFoldDB; Q9CID5; -.
DR   SMR; Q9CID5; -.
DR   STRING; 272623.L39593; -.
DR   CAZy; GH65; Glycoside Hydrolase Family 65.
DR   PaxDb; Q9CID5; -.
DR   PRIDE; Q9CID5; -.
DR   EnsemblBacteria; AAK04526; AAK04526; L39593.
DR   KEGG; lla:L39593; -.
DR   PATRIC; fig|272623.7.peg.466; -.
DR   eggNOG; COG1554; Bacteria.
DR   HOGENOM; CLU_006285_1_1_9; -.
DR   OMA; WIPDNSR; -.
DR   BioCyc; MetaCyc:MON-5861; -.
DR   BRENDA; 2.4.1.216; 2903.
DR   SABIO-RK; Q9CID5; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0050503; F:trehalose 6-phosphate phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.70.98.40; -; 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   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; SSF48208; SSF48208; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11553642"
FT   CHAIN           2..769
FT                   /note="Trehalose 6-phosphate phosphorylase"
FT                   /id="PRO_0000108014"
FT   ACT_SITE        480
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         342..343
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   BINDING         589..590
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT   VARIANT         703
FT                   /note="E -> D (in strain: ATCC 19435)"
SQ   SEQUENCE   769 AA;  87267 MW;  562D096E3A6CBB72 CRC64;
     MTEKDWIIQY DKKEVGKRSY GQESLMSLGN GYLGLRGAPL WSTCSDNHYP GLYVAGVFNR
     TSTEVAGHDV INEDMVNWPN PQLIKVYIDG ELVDFEASVE KQATIDFKNA LQIERYQVKL
     AKGNLTLVTT KFVDPINFHD FGFVGEIIAD FSCKLRIETF TDGSVLNQNV ERYRAFDSKE
     FEVTKISKGL LVAKTRTSEI ELAIASKSFL NGLAFPKIDS ENDEILAEAI EIDLQKNQEV
     QFDKTIVIAS SYESKNPVEF VLTELSATSV SKIQENNTNY WEKVWSDADI VIESDHEDLQ
     RMVRMNIFHI RQAAQHGANQ FLDASVGSRG LTGEGYRGHI FWDEIFVLPY YAANEPETAR
     DLLLYRINRL TAAQENAKVD GEKGAMFPWQ SGLIGDEQSQ FVHLNTVNNE WEPDNSRRQR
     HVSLAIVYNL WIYSQLTEDE SILTDGGLDL IIETTKFWLN KAELGDDGRY HIDGVMGPDE
     YHEAYPGQEG GICDNAYTNL MLTWQLNWLT ELSEKGFEIP KELLEKAQKV RKKLYLDIDE
     NGVIAQYAKY FELKEVDFAA YEAKYGDIHR IDRLMKAEGI SPDEYQVAKQ ADTLMLIYNL
     GQEHVTKLVK QLAYELPENW LKVNRDYYLA RTVHGSTTSR PVFAGIDVKL GDFDEALDFL
     ITAIGSDYYD IQGGTTAEGV HIGVMGETLE VIQNEFAGLS LREGQFAIAP YLPKSWTKLK
     FNQIFRGTKV EILIENGQLL LTASADLLTK VYDDEVQLKA GVQTKFDLK