ID R7FEG5_9FIRM Unreviewed; 470 AA.
AC R7FEG5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Sucrose 6(F)-phosphate phosphorylase {ECO:0000256|PIRNR:PIRNR003059};
DE EC=2.4.1.329 {ECO:0000256|PIRNR:PIRNR003059};
GN ORFNames=BN611_00774 {ECO:0000313|EMBL:CDE13689.1};
OS Ruminococcus sp. CAG:330.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1262954 {ECO:0000313|EMBL:CDE13689.1, ECO:0000313|Proteomes:UP000018377};
RN [1] {ECO:0000313|EMBL:CDE13689.1, ECO:0000313|Proteomes:UP000018377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:330 {ECO:0000313|Proteomes:UP000018377};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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|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:CDE13689.1}.
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DR EMBL; CBIH010000211; CDE13689.1; -; Genomic_DNA.
DR AlphaFoldDB; R7FEG5; -.
DR STRING; 1262954.BN611_00774; -.
DR Proteomes; UP000018377; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000018377};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR003059}.
FT DOMAIN 7..424
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 194
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-1"
FT ACT_SITE 235
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-1"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 192..194
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 235
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 292..293
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 336..339
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR003059-2"
SQ SEQUENCE 470 AA; 54316 MW; D88DF73B142D364A CRC64;
MKKLNNQIML ITYADSMGKN LKELHTVLNR YYHNAIGGVH ILPFFPSSAD RGFAPVTYEK
VDEAFGTFDD VEALGEDYYL MFDFMVNHIS AHSEYFQDFL QHKDESPYRD FFIRYSSFWE
NGEPTPEQLD LIYKRKPRAP YIEAEFADGT TEKIWCTFCE EQIDLDVEKP AVKEFIRRTL
KSMCRHGAAV IRLDAFAYAI KKKDTNCFFV EPEIWDLLHE IEGIVQEEQA EILPEIHEHY
TIPMKIADKG FWIYDFALPV LTLHALFNHT GVYLKKWLEQ CPMKQFTTLD THDGIGIVDV
KDLLPDAEIE TVKEQMYQQG ANVKKIYSSE AYNNLDIYQV NTTYYSALGN RDDAYLLARA
IQFFAPGIPQ VYYVGMLAGS NDIALMERTK NGRDINRHYY TSEEVAKEQE RSVVQDLKRL
MELRNTHPAF GLDGAIAVTA EGDQLTITRT CGDAQLTLHA DLTNYRFTID
//
