ID   SUCP_AGRVI              Reviewed;         488 AA.
AC   P33910;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Sucrose phosphorylase;
DE            EC=2.4.1.7;
DE   AltName: Full=Sucrose glucosyltransferase;
OS   Agrobacterium vitis (Rhizobium vitis).
OG   Plasmid pTi2608.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium.
OX   NCBI_TaxID=373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2608;
RX   PubMed=8012038; DOI=10.1094/mpmi-7-0164;
RA   Fournier P., de Ruffray P., Otten L.;
RT   "Natural instability of Agrobacterium vitis Ti plasmid due to unusual
RT   duplication of a 2.3-kb DNA fragment.";
RL   Mol. Plant Microbe Interact. 7:164-172(1994).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC       phosphorylase subfamily. {ECO:0000305}.
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DR   EMBL; Z22732; CAA80424.1; -; Genomic_DNA.
DR   EMBL; Z22733; CAA80426.1; -; Genomic_DNA.
DR   EMBL; Z22734; CAA80428.1; -; Genomic_DNA.
DR   PIR; S37466; S37466.
DR   AlphaFoldDB; P33910; -.
DR   SMR; P33910; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0009018; F:sucrose phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11355; AmyAc_Sucrose_phosphorylase; 1.
DR   Gene3D; 3.90.400.10; -; 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   Pfam; PF00128; Alpha-amylase; 1.
DR   PIRSF; PIRSF003059; Sucrose_phosphorylase; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   TIGRFAMs; TIGR03852; sucrose_gtfA; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Plasmid; Transferase.
FT   CHAIN           1..488
FT                   /note="Sucrose phosphorylase"
FT                   /id="PRO_0000072298"
FT   ACT_SITE        193
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   ACT_SITE        233
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         50
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         88
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         191..193
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         233
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         290..291
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         341..344
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT   BINDING         398
FT                   /ligand="sucrose"
FT                   /ligand_id="ChEBI:CHEBI:17992"
FT                   /evidence="ECO:0000250|UniProtKB:A0ZZH6"
SQ   SEQUENCE   488 AA;  53899 MW;  2F5DF772AE53ACBF CRC64;
     MKNSVQLITY VDRLSGGGFP ELRALLDGRL QGLFGGVHAL PFFNPIDGAD AGFDPTDHTI
     VDPRLGSWDD VRALAGSVEI MADLIVNHVS AQSSWFQDFI AKGSDSEFAD MFMTFGKAFP
     RGASEQDLLN IYRPRLGCRF QRPRLQIGSQ RMLWTTFTPQ QIDIDVHSAH GALYLETILD
     RFAEANVTAI RLDAAGYAIK KAGTSCFMID ETYAFLAKLA EKARDRGMEV LVEIHSYYRD
     QIEIASKVDR VYDFALPPLI LHSLFTGDAT ALARWLEISP HNAITVLDTH DGIGVIDVGA
     HSDGRPGLLE PQAIDHLVEE IHRRSEGQSR LATGAAASNL DLYQVNCTYY DALGRNDDDY
     LIARAIQFFA PGIPQVYYVG LLGGINDMEL LGKTGVGRDI NRHFYEDREI DLALESPLVK
     RLSDLIRFRN THPAFNGSFE VATDDTGSLV LSWNLNTEFA QLVVSFSQGK ATITASGCYD
     FTFSGAIA