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Database: UniProt
Entry: Q8Y3U6_LISMO
LinkDB: Q8Y3U6_LISMO
Original site: Q8Y3U6_LISMO 
ID   Q8Y3U6_LISMO            Unreviewed;       560 AA.
AC   Q8Y3U6;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 115.
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   OrderedLocusNames=lmo2735 {ECO:0000313|EMBL:CAD00948.1};
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963 {ECO:0000313|EMBL:CAD00948.1, ECO:0000313|Proteomes:UP000000817};
RN   [1] {ECO:0000313|EMBL:CAD00948.1, ECO:0000313|Proteomes:UP000000817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.D.,
RA   Fsihi H., Portillo F.G., Garrido P., Gautier L., Goebel W., Gomez-Lopez N.,
RA   Hain T., Hauf J., Jackson D., Jones L.M., Kaerst U., Kreft J., Kuhn M.,
RA   Kunst F., Kurapkat G., Madueno E., Maitournam A., Vicente J.M., Ng E.,
RA   Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.C.,
RA   Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA   Vazquez-Boland J.A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
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DR   EMBL; AL591984; CAD00948.1; -; Genomic_DNA.
DR   PIR; AF1416; AF1416.
DR   RefSeq; NP_466257.1; NC_003210.1.
DR   RefSeq; WP_010990053.1; NZ_CP023861.1.
DR   AlphaFoldDB; Q8Y3U6; -.
DR   STRING; 169963.gene:17595452; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PaxDb; 169963-lmo2735; -.
DR   EnsemblBacteria; CAD00948; CAD00948; CAD00948.
DR   GeneID; 987075; -.
DR   KEGG; lmo:lmo2735; -.
DR   PATRIC; fig|169963.11.peg.2801; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_021358_0_0_9; -.
DR   OrthoDB; 9805159at2; -.
DR   PhylomeDB; Q8Y3U6; -.
DR   BioCyc; LMON169963:LMO2735-MONOMER; -.
DR   Proteomes; UP000000817; 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   Reference proteome {ECO:0000313|Proteomes:UP000000817};
KW   Transferase {ECO:0000256|PIRNR:PIRNR003059}.
FT   DOMAIN          51..480
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   BINDING         98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         226..228
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         336..337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT   BINDING         444
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ   SEQUENCE   560 AA;  63933 MW;  0EB91E0E2F50F580 CRC64;
     MQTELVNQIE VKLRKIYQAA YQPAYLEKML ACAENYSNNT RGSIDTISEK NVYLIAYGDS
     IFEKNKHPLQ TLNEFLQEYA QDAITDVHLL PIFPSTSDDG FSVTDYKQID EQLGDWDDVQ
     KMSENFRVML DFVANHMSKS SDWFKRFSDN EAPYNQFFIE KDSQFDYKNV TRPRTSPLFH
     KYENGKELWT TFSEDQLDLN VRNIDCLVAL TDVLLFYASK QATSIRLDAI GFLWKTSGTT
     CMHLPETHEI ISLWRLLIDE LYPNLQIITE TNVPHEENIS YFGDGKNEAN MVYQFPLPPL
     VLHTFTCHDT TKLSKWAKSI SQVSDTATYF NFLASHDGIG MRPATGILSD EEINSLVQKA
     VQNGGQVSYK DNADGTQSVY ELNINYGEAL QNLDEDTTEE LVTKKIIAAH SILLTLQGVP
     AIYYHSLLGS KNDLVGYEES GINRRINREK LEKNQLVHEL KTDTYRKTIF TSLKKLVQIR
     RNHTAFSPFA TQEILDLGPD VFAIKRESEG ECIYGIINVT SHDISKKVAF SGTNLLANQP
     VTSELELTAY EVVWIKKAVQ
//
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