ID C8P5Y5_9LACO Unreviewed; 485 AA.
AC C8P5Y5;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=gtfA {ECO:0000313|EMBL:EEW54071.1};
GN ORFNames=HMPREF0494_0729 {ECO:0000313|EMBL:EEW54071.1};
OS Limosilactobacillus antri DSM 16041.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=525309 {ECO:0000313|EMBL:EEW54071.1, ECO:0000313|Proteomes:UP000003675};
RN [1] {ECO:0000313|EMBL:EEW54071.1, ECO:0000313|Proteomes:UP000003675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16041 {ECO:0000313|EMBL:EEW54071.1,
RC ECO:0000313|Proteomes:UP000003675};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (SEP-2009) 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:EEW54071.1}.
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DR EMBL; ACLL01000018; EEW54071.1; -; Genomic_DNA.
DR RefSeq; WP_007124032.1; NZ_GG700733.1.
DR AlphaFoldDB; C8P5Y5; -.
DR STRING; 525309.HMPREF0494_0729; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PATRIC; fig|525309.8.peg.1922; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_021358_1_0_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000003675; 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 10..426
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 196
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-1"
FT ACT_SITE 237
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 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 294..295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 338..341
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 395
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ SEQUENCE 485 AA; 55856 MW; 6AE66BBA2D3A0707 CRC64;
MPIQNKAMLI TYSDSMAKNI KETHEVLKEY IGDAIGGVHL LPFFPSTGDR GFAPYRYDVV
DSAFGNWDDV EALGEDYYLM FDFMINHISR KSEMYQDFKQ KHDDSKYNDF FIRWEKFWEA
AGKGRPTQAD IDLIYKRKDK APEQEIEFAD GSKEHLWNTF GEEQIDINVK SKVAQEFFKQ
TLIDMVKHGA DLIRLDAFAY AVKKVDTNDF FVEPEIWDLL NEVREILAPY QAEILPEIHE
HYTIPEKISK HGYFTYDFAL PMTTLYTLYS GKTNRLANWL KMSPMKQFTT LDTHDGIGVV
DAKDILSDDE IEYSSNELYK VGANVKRKYS SAEYHNLDIY QINSTYYSAL GDDDKAYLLA
RAFQVFAPGI PMIYYVGLLA GSNDLELLEK TKEGRNINRH YYTKDEVAKE VQRPVVKNLL
DLLSWRNQFA AFDLDGSIDV ETPSETTIKI TRKDKDGANV AVLEADAANK TFTITANGEQ
VMEQK
//
