ID   E3ZKV3_LISSE            Unreviewed;       566 AA.
AC   E3ZKV3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Sucrose phosphorylase {ECO:0000256|PIRNR:PIRNR003059};
DE            EC=2.4.1.7 {ECO:0000256|PIRNR:PIRNR003059};
DE   AltName: Full=Sucrose glucosyltransferase {ECO:0000256|PIRNR:PIRNR003059};
GN   ORFNames=NT03LS_0043 {ECO:0000313|EMBL:EFS01745.1};
OS   Listeria seeligeri FSL N1-067.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=702453 {ECO:0000313|EMBL:EFS01745.1};
RN   [1] {ECO:0000313|EMBL:EFS01745.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFS01745.1};
RX   PubMed=21126366; DOI=10.1186/1471-2164-11-688;
RA   den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H.,
RA   Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.;
RT   "Comparative genomics of the bacterial genus Listeria: Genome evolution is
RT   characterized by limited gene acquisition and limited gene loss.";
RL   BMC Genomics 11:688-688(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + sucrose = alpha-D-glucose 1-phosphate + D-
CC         fructose; Xref=Rhea:RHEA:24048, ChEBI:CHEBI:17992, ChEBI:CHEBI:37721,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.7;
CC         Evidence={ECO:0000256|PIRNR:PIRNR003059};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC       phosphorylase subfamily. {ECO:0000256|PIRNR:PIRNR003059}.
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:EFS01745.1}.
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DR   EMBL; ADXJ01000024; EFS01745.1; -; Genomic_DNA.
DR   RefSeq; WP_003744869.1; NZ_CM001051.1.
DR   AlphaFoldDB; E3ZKV3; -.
DR   PATRIC; fig|702453.3.peg.29; -.
DR   HOGENOM; CLU_021358_0_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000004302; Chromosome.
DR   GO; GO:0009018; F:sucrose phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11356; AmyAc_Sucrose_phosphorylase-like_1; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR033746; GGa_phosphorylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR016377; Sucrose_GGa_phosphorylase-rel.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF214; GLUCOSYLGLYCERATE PHOSPHORYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF003059; Sucrose_phosphorylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR003059};
KW   Transferase {ECO:0000256|PIRNR:PIRNR003059}.
FT   DOMAIN          64..478
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         225..227
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         335..336
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         441
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ   SEQUENCE   566 AA;  64627 MW;  54ED74027A7B51FA CRC64;
     MTNLIKRLSR LYSEDVANSL APRIEARVNE TKQQKLIRKD KWDEKDVVLI TYGDQFQEES
     VKNLISFKKM YDKYLKSTFE VVHFLPFYPY SSDDGFSVID YKQVNPVLGD WADVREMEKS
     ARLMFDFVCN HMSAKSDWFK RYLAGDKEFA NFFVEMNPET DLSSVTRPRA TPVLTPFKFD
     SGEEKYIWTT FSDDQIDLNF ANPEVLYKMI DVLLFYLEQG AEYVRLDAVG FMWKVPGTSS
     IHLDETHEIV KLFRDLVDMA APGTIIITET NVPHLDNISY FGDGEKEAHM VYQFPLPPLV
     LHAIHHGNAS FLSGWARELE LPTGKRTFFN FLASHDGIGL NPVRGIIPET EILALVKDLE
     QEGALVSYKQ NPDGSKSPYE INVTYMDALN KQSDSDAVRL RRFVVAHAVL FSIPGVPAVY
     VQSILGSRND IAGVEKTGQN RSINRKKYQL SEISTELESQ DTLRKATYEA LTKLINVRKS
     ESLFHPEIEM EVIDSTAELF VIKRSSGAES LILIHNLSEN EVNYSLDSGI YINICTNSTI
     TGSDSIRLSG YEFCWLKTKN CREEQK
//