SUCP_BIFAA
ID SUCP_BIFAA Reviewed; 504 AA.
AC A0ZZH6; Q84HQ2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Sucrose phosphorylase {ECO:0000303|PubMed:14740189, ECO:0000303|PubMed:14756551, ECO:0000303|PubMed:20691225};
DE Short=SP {ECO:0000303|PubMed:14756551};
DE Short=SPase {ECO:0000303|PubMed:20691225};
DE EC=2.4.1.7 {ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225};
GN Name=sucP {ECO:0000303|PubMed:14740189};
GN Synonyms=spl {ECO:0000312|EMBL:BAF38859.1};
GN OrderedLocusNames=BAD_0078 {ECO:0000312|EMBL:BAF38859.1};
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RX PubMed=14740189; DOI=10.1007/s00253-003-1534-x;
RA van den Broek L.A., van Boxtel E.L., Kievit R.P., Verhoef R., Beldman G.,
RA Voragen A.G.;
RT "Physico-chemical and transglucosylation properties of recombinant sucrose
RT phosphorylase from Bifidobacterium adolescentis DSM20083.";
RL Appl. Microbiol. Biotechnol. 65:219-227(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20691225; DOI=10.1016/j.jbiotec.2010.07.029;
RA Cerdobbel A., Desmet T., De Winter K., Maertens J., Soetaert W.;
RT "Increasing the thermostability of sucrose phosphorylase by multipoint
RT covalent immobilization.";
RL J. Biotechnol. 150:125-130(2010).
RN [4] {ECO:0007744|PDB:1R7A}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS), SUBUNIT, REACTION MECHANISM, AND
RP ACTIVE SITE.
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RX PubMed=14756551; DOI=10.1021/bi0356395;
RA Sprogoe D., van den Broek L.A., Mirza O., Kastrup J.S., Voragen A.G.,
RA Gajhede M., Skov L.K.;
RT "Crystal structure of sucrose phosphorylase from Bifidobacterium
RT adolescentis.";
RL Biochemistry 43:1156-1162(2004).
RN [5] {ECO:0007744|PDB:2GDU, ECO:0007744|PDB:2GDV}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF WILD-TYPE IN COVALENT COMPLEX
RP WITH BETA-D-GLUCOSE AND MUTANT GLN-232 IN COMPLEX WITH SUCROSE, MUTAGENESIS
RP OF GLU-232, REACTION MECHANISM, AND ACTIVE SITE.
RX PubMed=16990265; DOI=10.1074/jbc.m605611200;
RA Mirza O., Skov L.K., Sprogoe D., van den Broek L.A., Beldman G.,
RA Kastrup J.S., Gajhede M.;
RT "Structural rearrangements of sucrose phosphorylase from Bifidobacterium
RT adolescentis during sucrose conversion.";
RL J. Biol. Chem. 281:35576-35584(2006).
RN [6] {ECO:0007744|PDB:5C8B}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF MUTANT PHE-345 IN COMPLEX WITH
RP BETA-D-GLUCOSE, AND MUTAGENESIS OF GLN-345.
RX PubMed=26527586; DOI=10.1002/cbic.201500514;
RA Kraus M., Grimm C., Seibel J.;
RT "Redesign of the active site of sucrose phosphorylase through a clash-
RT induced cascade of loop shifts.";
RL ChemBioChem 17:33-36(2016).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of sucrose into
CC alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189,
CC PubMed:20691225). Is involved in sucrose degradation. Also displays
CC transglucosylation activity in vitro, by transferring the glucosyl
CC moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-
CC arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).
CC {ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225}.
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:14740189, ECO:0000269|PubMed:20691225};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.8 mM for sucrose (at 58 degrees Celsius and pH 6.5)
CC {ECO:0000269|PubMed:20691225};
CC Note=kcat is 207 sec(-1) for the phosphorolysis of sucrose (at 58
CC degrees Celsius and pH 6.5). {ECO:0000269|PubMed:20691225};
CC pH dependence:
CC Optimum pH is 6.0-6.5 for the phosphorolysis of sucrose.
CC {ECO:0000269|PubMed:14740189, ECO:0000269|PubMed:20691225};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius for the phosphorolysis of
CC sucrose (PubMed:14740189). The His-tagged enzyme shows an optimum
CC temperature of 58 degrees Celsius (PubMed:20691225). The
CC immobilization of the enzyme on Sepabeads EC-HFA increases
CC thermostability, and optimum temperature is shifted to 65 degrees
CC Celsius (PubMed:20691225). {ECO:0000269|PubMed:14740189,
CC ECO:0000269|PubMed:20691225};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14740189,
CC ECO:0000269|PubMed:14756551}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC phosphorylase subfamily. {ECO:0000305}.
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DR EMBL; AF543301; AAO33821.1; -; Genomic_DNA.
DR EMBL; AP009256; BAF38859.1; -; Genomic_DNA.
DR RefSeq; WP_011742626.1; NC_008618.1.
DR PDB; 1R7A; X-ray; 1.77 A; A/B=1-504.
DR PDB; 2GDU; X-ray; 2.10 A; A/B=1-504.
DR PDB; 2GDV; X-ray; 2.00 A; A/B=1-504.
DR PDB; 5C8B; X-ray; 2.70 A; B=1-504.
DR PDB; 5M9X; X-ray; 2.35 A; B=1-504.
DR PDB; 5MAN; X-ray; 2.04 A; B=1-504.
DR PDB; 5MB2; X-ray; 1.75 A; B=1-504.
DR PDB; 6FME; X-ray; 1.51 A; A/B=1-504.
DR PDBsum; 1R7A; -.
DR PDBsum; 2GDU; -.
DR PDBsum; 2GDV; -.
DR PDBsum; 5C8B; -.
DR PDBsum; 5M9X; -.
DR PDBsum; 5MAN; -.
DR PDBsum; 5MB2; -.
DR PDBsum; 6FME; -.
DR AlphaFoldDB; A0ZZH6; -.
DR SMR; A0ZZH6; -.
DR STRING; 1680.BADO_0067; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; BAF38859; BAF38859; BAD_0078.
DR KEGG; bad:BAD_0078; -.
DR HOGENOM; CLU_021358_1_0_11; -.
DR OMA; PNATQFT; -.
DR BRENDA; 2.4.1.7; 842.
DR Proteomes; UP000008702; Chromosome.
DR GO; GO:0009018; F:sucrose phosphorylase activity; IEA:UniProtKB-EC.
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; IPR015325; Suc_Porlyase_C.
DR InterPro; IPR016377; Sucrose_GGa_phosphorylase-rel.
DR InterPro; IPR022527; Sucrose_phospho.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09244; DUF1964; 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 3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..504
FT /note="Sucrose phosphorylase"
FT /id="PRO_0000442435"
FT ACT_SITE 192
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0000305|PubMed:14756551"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:14756551,
FT ECO:0000305|PubMed:16990265"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT BINDING 88
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT BINDING 190..192
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT BINDING 232
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT BINDING 289..290
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT BINDING 342..345
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT BINDING 399
FT /ligand="sucrose"
FT /ligand_id="ChEBI:CHEBI:17992"
FT /evidence="ECO:0000269|PubMed:16990265,
FT ECO:0007744|PDB:2GDU"
FT MUTAGEN 232
FT /note="E->Q: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:16990265"
FT MUTAGEN 345
FT /note="Q->F: Decreases affinity for sucrose. Highly
FT improves in vitro activity towards aromatic acceptors,
FT allowing efficient glucosylation of resveratrol, (+)-
FT catechin and (-)-epicatechin."
FT /evidence="ECO:0000269|PubMed:16990265"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 148..153
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 168..183
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 209..224
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 255..265
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5MAN"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 371..378
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 389..395
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 418..432
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 434..437
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 460..465
FT /evidence="ECO:0007829|PDB:6FME"
FT HELIX 467..470
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:6FME"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:6FME"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:6FME"
SQ SEQUENCE 504 AA; 56190 MW; 10705FE3182E5754 CRC64;
MKNKVQLITY ADRLGDGTIK SMTDILRTRF DGVYDGVHIL PFFTPFDGAD AGFDPIDHTK
VDERLGSWDD VAELSKTHNI MVDAIVNHMS WESKQFQDVL AKGEESEYYP MFLTMSSVFP
NGATEEDLAG IYRPRPGLPF THYKFAGKTR LVWVSFTPQQ VDIDTDSDKG WEYLMSIFDQ
MAASHVSYIR LDAVGYGAKE AGTSCFMTPK TFKLISRLRE EGVKRGLEIL IEVHSYYKKQ
VEIASKVDRV YDFALPPLLL HALSTGHVEP VAHWTDIRPN NAVTVLDTHD GIGVIDIGSD
QLDRSLKGLV PDEDVDNLVN TIHANTHGES QAATGAAASN LDLYQVNSTY YSALGCNDQH
YIAARAVQFF LPGVPQVYYV GALAGKNDME LLRKTNNGRD INRHYYSTAE IDENLKRPVV
KALNALAKFR NELDAFDGTF SYTTDDDTSI SFTWRGETSQ ATLTFEPKRG LGVDNTTPVA
MLEWEDSAGD HRSDDLIANP PVVA
