SUCP_STRMU
ID SUCP_STRMU Reviewed; 481 AA.
AC P10249; Q99064;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sucrose phosphorylase {ECO:0000303|PubMed:2971020};
DE EC=2.4.1.7 {ECO:0000269|PubMed:2971020};
DE AltName: Full=Glucosyltransferase-A {ECO:0000303|PubMed:2967248};
DE Short=GTF-A {ECO:0000303|PubMed:2971020};
DE AltName: Full=Sucrose glucosyltransferase;
GN Name=gtfA {ECO:0000303|PubMed:2967248, ECO:0000303|PubMed:3194228};
GN OrderedLocusNames=SMU_881;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=3194228; DOI=10.1093/nar/16.21.10398;
RA James L.C., Hughes T.A., Curtiss R. III;
RT "Nucleotide sequence of the gtfA gene from S. mutans GS-5.";
RL Nucleic Acids Res. 16:10398-10398(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, AND
RP MUTAGENESIS OF 462-ILE--GLU-481.
RC STRAIN=Ingbritt;
RX PubMed=2967248; DOI=10.1128/iai.56.6.1585-1588.1988;
RA Ferretti J.J., Huang T.-T., Russell R.R.B.;
RT "Sequence analysis of the glucosyltransferase A gene (gtfA) from
RT Streptococcus mutans Ingbritt.";
RL Infect. Immun. 56:1585-1588(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PROBABLE SUBCELLULAR LOCATION.
RC STRAIN=Ingbritt;
RX PubMed=2971020; DOI=10.1128/iai.56.10.2763-2765.1988;
RA Russell R.R.B., Mukasa H., Shimamura A., Ferretti J.J.;
RT "Streptococcus mutans gtfA gene specifies sucrose phosphorylase.";
RL Infect. Immun. 56:2763-2765(1988).
CC -!- FUNCTION: Intracellular catabolism of sucrose (PubMed:2971020). Being
CC intracellular, probably not involved in synthesis of extracellular
CC polysaccharides (Probable). {ECO:0000269|PubMed:2971020,
CC ECO:0000305|PubMed:2967248}.
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:0000269|PubMed:2971020};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24049;
CC Evidence={ECO:0000269|PubMed:2971020};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24050;
CC Evidence={ECO:0000269|PubMed:2971020};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2971020}.
CC -!- MISCELLANEOUS: Some earlier publications concluded that the product of
CC the reaction of GtfA with sucrose was a glucan, because of its
CC insolubility in ethanol.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC phosphorylase subfamily. {ECO:0000305}.
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DR EMBL; X08057; CAA30846.1; -; Genomic_DNA.
DR EMBL; M77351; AAA26937.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN58596.1; -; Genomic_DNA.
DR PIR; A27626; A27626.
DR PIR; S01972; BWSOGM.
DR RefSeq; NP_721290.1; NC_004350.2.
DR RefSeq; WP_002262875.1; NC_004350.2.
DR AlphaFoldDB; P10249; -.
DR SMR; P10249; -.
DR STRING; 210007.SMU_881; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P10249; -.
DR EnsemblBacteria; AAN58596; AAN58596; SMU_881.
DR KEGG; smu:SMU_881; -.
DR PATRIC; fig|210007.7.peg.787; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_021358_1_0_9; -.
DR OMA; PNATQFT; -.
DR PhylomeDB; P10249; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009018; F:sucrose phosphorylase activity; IDA:CACAO.
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 1: Evidence at protein level;
KW Cytoplasm; Dental caries; Direct protein sequencing; Glycosyltransferase;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2967248"
FT CHAIN 2..481
FT /note="Sucrose phosphorylase"
FT /id="PRO_0000072301"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT ACT_SITE 234
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 191..193
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 234
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 291..292
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 335..338
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 392
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT MUTAGEN 462..481
FT /note="Missing: Loss of glucan synthesis."
FT /evidence="ECO:0000269|PubMed:2967248"
FT CONFLICT 4..5
FT /note="IN -> TI (in Ref. 1; CAA30846 and 2; AAA26937)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="G -> A (in Ref. 1; CAA30846)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="C -> R (in Ref. 1; CAA30846 and 2; AAA26937)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="D -> N (in Ref. 2; AAA26937)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="S -> G (in Ref. 1; CAA30846 and 2; AAA26937)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> V (in Ref. 1; CAA30846)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="N -> I (in Ref. 1; CAA30846)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="N -> I (in Ref. 1; CAA30846)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..444
FT /note="AT -> EN (in Ref. 1; CAA30846)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="K -> T (in Ref. 1; CAA30846 and 2; AAA26937)"
FT /evidence="ECO:0000305"
FT CONFLICT 480..481
FT /note="FE -> LSMISCQT (in Ref. 1; CAA30846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 55687 MW; 1B403FD6D95FFC8C CRC64;
MPIINKTMLI TYADSLGKNL KELNENIENY FGDAVGGVHL LPFFPSTGDR GFAPIDYHEV
DSAFGDWDDV KCLGEKYYLM FDFMINHISR QSKYYKDYQE KHEASAYKDL FLNWDKFWPK
NRPTQEDVDL IYKRKDRAPK QEIQFADGSV EHLWNTFGEE QIDLDVTKEV TMDFIRSTIE
NLAANGCDLI RLDAFAYAVK KLDTNDFFVE PEIWTLLDKV RDIAAVSGAE ILPEIHEHYT
IQFKIADHDY YVYDFALPMV TLYSLYSSKV DRLAKWLKMS PMKQFTTLDT HDGIGVVDVK
DILTDEEITY TSNELYKVGA NVNRKYSTAE YNNLDIYQIN STYYSALGDD DQKYFLARLI
QAFAPGIPQV YYVGFLAGKN DLELLESTKE GRNINRHYYS SEEIAKEVKR PVVKALLNLF
TYRNQSAAFD LDGRIEVETP NEATIVIERQ NKDGSHIAKA EINLQDMTYR VTENDQTISF
E
