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Database: UniProt
Entry: F2JRV7_CELLD
LinkDB: F2JRV7_CELLD
Original site: F2JRV7_CELLD 
ID   F2JRV7_CELLD            Unreviewed;       545 AA.
AC   F2JRV7;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Alpha,alpha-phosphotrehalase {ECO:0000313|EMBL:ADZ85137.1};
DE            EC=3.2.1.93 {ECO:0000313|EMBL:ADZ85137.1};
GN   OrderedLocusNames=Clole_3450 {ECO:0000313|EMBL:ADZ85137.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ85137.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ85137.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061}.
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DR   EMBL; CP002582; ADZ85137.1; -; Genomic_DNA.
DR   RefSeq; WP_013658413.1; NC_015275.1.
DR   AlphaFoldDB; F2JRV7; -.
DR   STRING; 642492.Clole_3450; -.
DR   KEGG; cle:Clole_3450; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_1_2_9; -.
DR   Proteomes; UP000008467; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0008788; F:alpha,alpha-phosphotrehalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005993; P:trehalose catabolic process; IEA:InterPro.
DR   CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012769; Trehalose_TreC.
DR   NCBIfam; TIGR02403; trehalose_treC; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF179; NEUTRAL AND BASIC AMINO ACID TRANSPORT PROTEIN RBAT; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:ADZ85137.1};
KW   Hydrolase {ECO:0000313|EMBL:ADZ85137.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008467}.
FT   DOMAIN          10..409
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   545 AA;  63857 MW;  418F908A53A91E35 CRC64;
     MNFKDKVIYQ IYPKSFQDTT GNGFGDLKGV TSRLNYLEEL GIDYIWLTPF FISPQRDNGY
     DVADYRNIDP LFGTMADCEE LIEEANKRSI GIMLDMVFNH TSTEHQWFQK ALAGDPEYMD
     YYFFKDGTPD QPPTNWESKF GGNAWEYVPH LKKWYLHLFD VTQADLNWEN PKVREELKEI
     IRFWKNKGVK GFRFDVVNLI SKPEVFESDK VGDGRRFYTD GSKVHAYLKE LVADTQIENM
     VTVGEMSSTT LEHCIRYSNP KEKELSMCFN FHHLKVDYKD GNKWEIMQPD FKALKTLFYN
     WQLGMQENEG WNALFWCNHD QPRVVSRLGD DENYWKESAK MLATCIHMMQ GTPYIFQGEE
     IGMTNAKYTD ISQYCDVESK NYYEIMLRNG KTKEEALAIL GARSRDNSRT PMQWNSGDHA
     GFSNSTPWLS IPENYKAINV EIEQNDADSI LAYYKKLIQI RKEHPAISEG KIEFIYKDHP
     EILAYKRSFG DEEILVLNNL GRNHTRLTAD LQLESYEKIL GNYEKADHAK ELEPFEAIIY
     RRVKR
//
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