ID   SUCP_LEUME              Reviewed;         490 AA.
AC   Q59495;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   13-SEP-2023, entry version 90.
DE   RecName: Full=Sucrose phosphorylase;
DE            EC=2.4.1.7;
DE   AltName: Full=Sucrose glucosyltransferase;
OS   Leuconostoc mesenteroides.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=1245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kitao S., Koga T., Nakano E.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1368718; DOI=10.1271/bbb1961.55.1805;
RA   Koga T., Nakamura K., Shirokane Y., Mizusawa K., Kitao S., Kikuchi M.;
RT   "Purification and some properties of sucrose phosphorylase from Leuconostoc
RT   mesenteroides.";
RL   Agric. Biol. Chem. 55:1805-1810(1991).
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   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC       phosphorylase subfamily. {ECO:0000305}.
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DR   EMBL; D90314; BAA14344.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59495; -.
DR   SMR; Q59495; -.
DR   STRING; 1245.ARA02_01825; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 2.4.1.7; 839.
DR   GO; GO:0009018; F:sucrose phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11355; AmyAc_Sucrose_phosphorylase; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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   InterPro; IPR022527; Sucrose_phospho.
DR   NCBIfam; TIGR03852; sucrose_gtfA; 1.
DR   PANTHER; PTHR38784; SUCROSE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR38784:SF1; SUCROSE 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   1: Evidence at protein level;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..490
FT                   /note="Sucrose phosphorylase"
FT                   /id="PRO_0000072300"
FT   ACT_SITE        196
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   ACT_SITE        237
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         49
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         87
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         194..196
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         237
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         294..295
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         338..341
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         395
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
SQ   SEQUENCE   490 AA;  55743 MW;  841CCC244CA917BE CRC64;
     MEIQNKAMLI TYADSLGKNL KDVHQVLKED IGDAIGGVHL LPFFPSTGDR GFAPADYTRV
     DAAFGDWADV EALGEEYYLM FDFMINHISR ESVMYQDFKK NHDDSKYKDF FIRWEKFWAK
     AGENRPTQAD VDLIYKRKDK APTQEITFDD GTTENLWNTF GEEQIDIDVN SAIAKEFIKT
     TLEDMVKHGA NLIRLDAFAY AVKKVDTNDF FVEPEIWDTL NEVREILTPL KAEILPEIHE
     HYSIPKKIND HGYFTYDFAL PMTTLYTLYS GKTNQLAKWL KMSPMKQFTT LDTHDGIGVV
     DARDILTDDE IDYASEQLYK VGANVKKTYS SASYNNLDIY QINSTYYSAL GNDDAAYLLS
     RVFQVFAPGI PQIYYVGLLA GENDIALLES TKEGRNINRH YYTREEVKSE VKRPVVANLL
     KLLSWRNESP AFDLAGSITV DTPTDTTIVV TRQDENGQNK AVLTADAANK TFEIVENGQT
     VMSSDNLTQN
//