ID A0A0J1DIB3_9FIRM Unreviewed; 575 AA.
AC A0A0J1DIB3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Sucrose 6(F)-phosphate phosphorylase {ECO:0000256|PIRNR:PIRNR003059};
DE EC=2.4.1.329 {ECO:0000256|PIRNR:PIRNR003059};
GN ORFNames=AA931_12775 {ECO:0000313|EMBL:KLU38802.1};
OS Peptococcaceae bacterium 1109.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1655638 {ECO:0000313|EMBL:KLU38802.1, ECO:0000313|Proteomes:UP000036486};
RN [1] {ECO:0000313|EMBL:KLU38802.1, ECO:0000313|Proteomes:UP000036486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1109 {ECO:0000313|EMBL:KLU38802.1};
RA Town J.R., Dumonceaux T.J.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + sucrose 6(F)-phosphate = alpha-D-glucose 1-
CC phosphate + beta-D-fructose 6-phosphate; Xref=Rhea:RHEA:38863,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:57723,
CC ChEBI:CHEBI:58601; EC=2.4.1.329;
CC Evidence={ECO:0000256|PIRNR:PIRNR003059};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC phosphorylase subfamily. {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:KLU38802.1}.
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DR EMBL; LDJB01000009; KLU38802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1DIB3; -.
DR STRING; 1655638.AA931_12775; -.
DR PATRIC; fig|1655638.3.peg.2588; -.
DR Proteomes; UP000036486; Unassembled WGS sequence.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11356; AmyAc_Sucrose_phosphorylase-like_1; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR033746; GGa_phosphorylase.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR InterPro; IPR016377; Sucrose_GGa_phosphorylase-rel.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF214; GLUCOSYLGLYCERATE 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.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR003059};
KW Transferase {ECO:0000256|PIRNR:PIRNR003059}.
FT DOMAIN 28..456
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 229..231
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 339..340
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 445
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ SEQUENCE 575 AA; 64573 MW; EA79D5DFECD8542F CRC64;
MTRDALLDSI RSLAAPLYGA DEADRIVELV SDLVEESNPR DVNDSSLTQA DSILITYGDL
LRREGTPPLR VLHGFLKEHL KGTVSAVHIL PFYPYSSDDG FSVIDYWQVN KELGSWEDIS
RIGQDFDLMV DAVVNHISSK SKWFQAYLNG DPEYLDFFIE ADPDLDYSTV VRPRALPLLT
EFETRMGRRH LWTTFSADQI DLNFASPEVL KEWIKLFFFY IQQGARFIRL DAVGYLWKEI
GTSCIHLDET HRVVQLLRAV AELANPAAKI VTETNVPHND NISYFGNGSN EAHMVYQFPL
PPLVLHTFIQ EDCRALSQWA HSLEDPPGDA TFFNFLASHD GVGLMPAVDL LSAEELELMI
ETVKRRGGFV SYKHNADGTE SPYELNINYL SALFEPGEPQ ETAVRRFLTA HSILLSLMGV
PGIYIHSLLG SLNYEEGVQS SGIKRRINRE KLDYAAVLAE LNDPSSLRNQ VFSGIKHMLT
VRQDQPAFHP KSPQEILFLD PSVCAIKRGT PEQEVVISLN NVSGTTQRVS LAKEILGAAV
QAVDLLTGTT YRVENKGLEL ALPPYQACWL KLSYI
//
