ID Q7WWP8_LACAI Unreviewed; 480 AA.
AC Q7WWP8; F1SVF2; Q5FJ62;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 118.
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 Name=gtfA2 {ECO:0000313|EMBL:AAO21868.1};
OS Lactobacillus acidophilus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1579 {ECO:0000313|EMBL:AAO21868.1};
RN [1] {ECO:0000313|EMBL:AAO21868.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12847288; DOI=10.1073/pnas.1332765100;
RA Barrangou R., Altermann E., Hutkins R., Cano R., Klaenhammer T.R.;
RT "Functional and comparative genomic analyses of an operon involved in
RT fructooligosaccharide utilization by Lactobacillus acidophilus.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8957-8962(2003).
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|ARBA:ARBA00008452,
CC ECO:0000256|PIRNR:PIRNR003059}.
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DR EMBL; AY172020; AAO21868.1; -; Genomic_DNA.
DR RefSeq; WP_011254462.1; NZ_WPCN01000003.1.
DR AlphaFoldDB; Q7WWP8; -.
DR SMR; Q7WWP8; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 56943017; -.
DR KEGG; laf:SD55_1419; -.
DR OMA; ISWWSAM; -.
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 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR003059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003059}.
FT DOMAIN 6..423
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-1"
FT ACT_SITE 234
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-1"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 191..193
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 291..292
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 335..338
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ SEQUENCE 480 AA; 55808 MW; A3D0F58AA0DDCF61 CRC64;
MPIENKVMLI TYPDSLGKNL KELDEILSED LKGAVGGIHL LPFFPSTGDR GFAPTGYTEV
DPKFGDWSDI EKIGKKYYLM FDFMINHISR QSKFYKDFKQ KKDKSKYADL FLSWDKFWPE
GRPTRKDIDL IYKRKDRAPY QEITFTDGSK EKLWNTFGEE QIDMDVRKEV TQKFIKDTLR
ALIDHGADII RLDAFAYAVK KLDTNDFFVE PEIWDLLKQV QDDISDKGAM ILPEIHEHYS
MPFKISKHGY YIYDFALPMV TLYSLYSGKS NRLADWLKKC PMKQFTTLDT HDGIGVVDAR
DILSPDEIKY TSNELYKVGA NVKKKYSSAE YHNLDIYQIN TTYYSALGND DKKYFIARLI
QMFAPGIPQV YYVGMLAGKN DIELLEKTKE GRNINRHYYG REEVAEETKR PLVAALLKLF
NFRNNEAAFD LDGSIEITTP NENVIQITRM NKDKTRKARA VINLKNLTYQ VTVNNEVINF
//
