SUCPP_ILUCY
ID SUCPP_ILUCY Reviewed; 523 AA.
AC A0A6C7EEG6;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Sucrose 6(F)-phosphate phosphorylase {ECO:0000303|PubMed:31405215};
DE Short=SPP {ECO:0000303|PubMed:31405215};
DE EC=2.4.1.329 {ECO:0000269|PubMed:31405215};
DE AltName: Full=Sucrose 6'-phosphate phosphorylase;
GN ORFNames=YM304_32550 {ECO:0000312|EMBL:BAN03569.1};
OS Ilumatobacter coccineus (strain NBRC 103263 / KCTC 29153 / YM16-304).
OC Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales;
OC Ilumatobacteraceae; Ilumatobacter.
OX NCBI_TaxID=1313172;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103263 / KCTC 29153 / YM16-304;
RX PubMed=23524358; DOI=10.1099/ijs.0.047316-0;
RA Matsumoto A., Kasai H., Matsuo Y., Shizuri Y., Ichikawa N., Fujita N.,
RA Omura S., Takahashi Y.;
RT "Ilumatobacter nonamiense sp. nov. and Ilumatobacter coccineum sp. nov.,
RT isolated from seashore sand.";
RL Int. J. Syst. Evol. Microbiol. 63:3404-3408(2013).
RN [2] {ECO:0007744|PDB:6S9U}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE,
RP AND MUTAGENESIS OF ARG-152; LYS-364; TYR-377 AND LYS-434.
RC STRAIN=NBRC 103263 / KCTC 29153 / YM16-304;
RX PubMed=31405215; DOI=10.3390/ijms20163906;
RA Franceus J., Capra N., Desmet T., Thunnissen A.W.H.;
RT "Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6F-
RT Phosphate Phosphorylase.";
RL Int. J. Mol. Sci. 20:0-0(2019).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of sucrose 6(F)-
CC phosphate into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose 6-
CC phosphate (PubMed:31405215). May be involved in a new pathway for the
CC degradation of sucrose, which could become phosphorylated on its
CC fructose moiety during uptake via a PTS system (By similarity). Shows
CC strict specificity since it does not catalyze reactions with
CC alternative substrates (PubMed:31405215).
CC {ECO:0000250|UniProtKB:D9TT09, ECO:0000269|PubMed:31405215}.
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:0000269|PubMed:31405215};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38864;
CC Evidence={ECO:0000305|PubMed:31405215};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.8 mM for phosphate (at 35 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:31405215};
CC KM=11.3 mM for sucrose 6(F)-phosphate (at 35 degrees Celsius and pH
CC 7) {ECO:0000305|PubMed:31405215};
CC KM=2.0 mM for D-fructose 6-phosphate (at 35 degrees Celsius and pH
CC 6.5) {ECO:0000305|PubMed:31405215};
CC KM=18.8 mM for alpha-D-glucose 1-phosphate (at 35 degrees Celsius and
CC pH 6.5) {ECO:0000305|PubMed:31405215};
CC Note=kcat is 126 sec(-1) for the phosphorolysis of sucrose 6(F)-
CC phosphate (at 35 degrees Celsius and pH 7). kcat is 45 sec(-1) for
CC the synthetic direction with alpha-D-glucose 1-phosphate and D-
CC fructose 6-phosphate as substrates (at 35 degrees Celsius and pH
CC 6.5). {ECO:0000305|PubMed:31405215};
CC pH dependence:
CC Optimum pH is 6.5 in the synthesis direction, and more than 50% of
CC the maximum activity is retained within the pH range of 5.5 to 8. In
CC the phosphorolytic direction, the optimum is reached at pH 6.
CC {ECO:0000269|PubMed:31405215};
CC Temperature dependence:
CC Optimum temperature is 35 degrees Celsius.
CC {ECO:0000269|PubMed:31405215};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:31405215}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. Sucrose
CC phosphorylase subfamily. {ECO:0000305}.
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DR EMBL; AP012057; BAN03569.1; -; Genomic_DNA.
DR PDB; 6S9U; X-ray; 2.05 A; A=1-523.
DR PDBsum; 6S9U; -.
DR AlphaFoldDB; A0A6C7EEG6; -.
DR SMR; A0A6C7EEG6; -.
DR KEGG; aym:YM304_32550; -.
DR BRENDA; 2.4.1.329; 17579.
DR Proteomes; UP000011863; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..523
FT /note="Sucrose 6(F)-phosphate phosphorylase"
FT /id="PRO_0000450866"
FT ACT_SITE 223
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:31405215"
FT ACT_SITE 264
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:31405215"
FT BINDING 58
FT /ligand="sucrose 6(F)-phosphate"
FT /ligand_id="ChEBI:CHEBI:57723"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 96
FT /ligand="sucrose 6(F)-phosphate"
FT /ligand_id="ChEBI:CHEBI:57723"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 221..223
FT /ligand="sucrose 6(F)-phosphate"
FT /ligand_id="ChEBI:CHEBI:57723"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 264
FT /ligand="sucrose 6(F)-phosphate"
FT /ligand_id="ChEBI:CHEBI:57723"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 326..327
FT /ligand="sucrose 6(F)-phosphate"
FT /ligand_id="ChEBI:CHEBI:57723"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT BINDING 434
FT /ligand="sucrose 6(F)-phosphate"
FT /ligand_id="ChEBI:CHEBI:57723"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
FT SITE 327
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305|PubMed:31405215"
FT MUTAGEN 152
FT /note="R->A: 28-fold decrease in catalytic activity in the
FT synthesis direction, but only slight decrease in affinity
FT for beta-D-fructose 6-phosphate. Gains some activity on
FT fructose, glycerol, and D-glycerate."
FT /evidence="ECO:0000269|PubMed:31405215"
FT MUTAGEN 364
FT /note="K->S: 65-fold decrease in catalytic activity in the
FT synthesis direction, and 3-fold decrease in affinity for
FT beta-D-fructose 6-phosphate. Gains some activity on
FT fructose, glycerol, and D-glycerate."
FT /evidence="ECO:0000269|PubMed:31405215"
FT MUTAGEN 377
FT /note="Y->H: 50-fold decrease in catalytic activity in the
FT synthesis direction, but only slight decrease in affinity
FT for beta-D-fructose 6-phosphate."
FT /evidence="ECO:0000269|PubMed:31405215"
FT MUTAGEN 434
FT /note="K->A: 400-fold decrease in catalytic activity in the
FT synthesis direction, and 17-fold decrease in affinity for
FT beta-D-fructose 6-phosphate. Gains some activity on
FT fructose and glycerol."
FT /evidence="ECO:0000269|PubMed:31405215"
FT MUTAGEN 434
FT /note="K->R: 6-fold decrease in catalytic activity in the
FT synthesis direction, and 5-fold decrease in affinity for
FT beta-D-fructose 6-phosphate. Gains some activity on
FT fructose and D-glycerate."
FT /evidence="ECO:0000269|PubMed:31405215"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:6S9U"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 27..34
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6S9U"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6S9U"
FT TURN 115..119
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:6S9U"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 242..256
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 273..279
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 289..299
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:6S9U"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 383..386
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 391..403
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 404..411
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 412..415
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 443..449
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 453..467
FT /evidence="ECO:0007829|PDB:6S9U"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 484..491
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 494..501
FT /evidence="ECO:0007829|PDB:6S9U"
FT TURN 502..505
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:6S9U"
FT STRAND 516..522
FT /evidence="ECO:0007829|PDB:6S9U"
SQ SEQUENCE 523 AA; 58833 MW; 5289594830DF9A58 CRC64;
MTHAGMKASL PNRVMLNAYP DSIDGDLAGT VRMLQRPEFT DAFGLFYVLP SIFNSDLDRG
FSIIDYDLNS DLASAEDLAA LDELGIMLKF DMVLNHLSVG SPQFQDLLKH GDDSAFRDFF
IDWNEFWEGE GELHADGHVV PSPEHLDRLF MRKPGLPILQ VRFPDGSDRF YWNTFYQRVE
TIDGERSYLG QMDLNAESPR VWTFYRETFE KLARYGAKIV RLDAFAYLHK AVGDTNFFNT
PGTWDHLDRL RTISEENGLV LLPEIHGEYG TKIHEELSDR DYPVYDFFFP GLVIDAIDSA
SNTHLLRWID EIIERDIATV NMLGCHDGIP VIDLKGGPTG QGLLPDATIE AMISRLLERG
GRVKNLYGAD GTKVSYYQVN ATFFSALGES DARLRLARAI QLFVPGTPQV WYLDLFAGAN
DVEAADRAGA DGHKEINRTN LSAADVEAGL ARPIVLDQLE MIRLRNASPA FDGRFEVVPT
DDTRLQLRWQ NGSTVALLDA DLATERFTIT HEHDGHTEIL GYD
