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Database: UniProt
Entry: A0A0W0ZZF8_9GAMM
LinkDB: A0A0W0ZZF8_9GAMM
Original site: A0A0W0ZZF8_9GAMM 
ID   A0A0W0ZZF8_9GAMM        Unreviewed;       426 AA.
AC   A0A0W0ZZF8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=glucan 1,4-alpha-glucosidase {ECO:0000256|ARBA:ARBA00012593};
DE            EC=3.2.1.3 {ECO:0000256|ARBA:ARBA00012593};
GN   ORFNames=Ltuc_2345 {ECO:0000313|EMBL:KTD74498.1};
OS   Legionella tucsonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=40335 {ECO:0000313|EMBL:KTD74498.1, ECO:0000313|Proteomes:UP000054693};
RN   [1] {ECO:0000313|EMBL:KTD74498.1, ECO:0000313|Proteomes:UP000054693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49180 {ECO:0000313|EMBL:KTD74498.1,
RC   ECO:0000313|Proteomes:UP000054693};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues
CC         successively from non-reducing ends of the chains with release of
CC         beta-D-glucose.; EC=3.2.1.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001863};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family.
CC       {ECO:0000256|ARBA:ARBA00006188}.
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:KTD74498.1}.
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DR   EMBL; LNZA01000001; KTD74498.1; -; Genomic_DNA.
DR   RefSeq; WP_058521452.1; NZ_LNZA01000001.1.
DR   AlphaFoldDB; A0A0W0ZZF8; -.
DR   STRING; 40335.Ltuc_2345; -.
DR   PATRIC; fig|40335.7.peg.2502; -.
DR   OrthoDB; 5641212at2; -.
DR   Proteomes; UP000054693; Unassembled WGS sequence.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005976; P:polysaccharide metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR000165; Glucoamylase.
DR   PANTHER; PTHR31616:SF11; GLUCOAMYLASE, INTRACELLULAR SPORULATION-SPECIFIC; 1.
DR   PANTHER; PTHR31616; TREHALASE; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 2.
DR   PRINTS; PR00736; GLHYDRLASE15.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000313|EMBL:KTD74498.1};
KW   Hydrolase {ECO:0000313|EMBL:KTD74498.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054693}.
FT   DOMAIN          32..344
FT                   /note="GH15-like"
FT                   /evidence="ECO:0000259|Pfam:PF00723"
FT   DOMAIN          362..407
FT                   /note="GH15-like"
FT                   /evidence="ECO:0000259|Pfam:PF00723"
SQ   SEQUENCE   426 AA;  48788 MW;  85E2EE3095110366 CRC64;
     MIFFVSQAIS SVFSLEEIQK LRQHFFVNIQ SNGAIVAAPS KHNPDYYYDW IRDSAIAMDL
     IETWYESSQT FGYKERLFNY VSWTQKLQHQ HNPSPGQDIL GEPKFYIDGY PFEGPWGRPQ
     NDGPALRASV LIRFAQKLLD NNETEYVQAN LYNNNLDPHS MGVIKMDLEY TAHHWSDKNY
     DLWEEVFGHH FFTAMTQQKA LFEGAALARR LNDNEAAVYY EQQARLINTR LNQHFDPDHK
     TIQATLLPHP GPQKTLELDS SVILGILFNP QTNGDLSPSS IYVQNTVKAL YDQFNSMFPI
     NNKHSGEILF GRYPGDTYDG YQTNSIGNPW FILTATMAEY YYTLADNLPL INQGEIAKNI
     QTGDNYLKLI KKYAPDMKLS EQVNLNTGVQ QGAPSLTWSY VAVLRAVELR EKLTSKSNHS
     SLKIVN
//
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