ID U2IRD5_9STRE Unreviewed; 481 AA.
AC U2IRD5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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 ORFNames=HMPREF1557_00958 {ECO:0000313|EMBL:ERJ76481.1};
OS Streptococcus sobrinus W1703.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ76481.1, ECO:0000313|Proteomes:UP000016617};
RN [1] {ECO:0000313|EMBL:ERJ76481.1, ECO:0000313|Proteomes:UP000016617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ76481.1,
RC ECO:0000313|Proteomes:UP000016617};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERJ76481.1}.
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DR EMBL; AWVA01000057; ERJ76481.1; -; Genomic_DNA.
DR RefSeq; WP_021673300.1; NZ_KI259660.1.
DR AlphaFoldDB; U2IRD5; -.
DR PATRIC; fig|1227275.3.peg.850; -.
DR HOGENOM; CLU_021358_1_0_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000016617; Unassembled WGS sequence.
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..396
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 481 AA; 55345 MW; FCC09D591D513979 CRC64;
MTLTNKTMLI TYLDSLGKNL KELDENISKY FGDAIGGVHL LPFFPSTGDR GFAPVDYDQV
DPAFGDWDDV KRLGDKYYLM FDFMINHISR QSKYYKDFQE KKDASAYADL FLRWEKFWPE
NRPTQADIDL IYKRKDKAPM QEIIFADGSK EHLWNTFGEE QIDLDVTKEV TMDFIKKTIE
NLAANGCDLI RLDAFAYAVK KLDSNDFFVE PEIWDLLTKV QAIAKEAGAD ILPEIHEHYS
IQFKIADHDY FVYDFALPMV TLYSLYSGQA QRLADWLAKS PMKQFTTLDT HDGIGVVDVK
DILTDEEIDY TSNQLYKVGA NVNRKYSTAE YNNLDIYQIN STYYSALGDD DKKYFLARLI
QAFAPGIPQV YYVGLLAGKN DLELLEKTKE GRNINRHYYS SQEIAQEVQR PVVKALLNLF
SYRNQSSAFD LDGSIETTVK DENTIIIKRG NRDNSVLAQA EINLNDLTYQ VTENGQTITF
E
//
