GGP_BACIE
ID GGP_BACIE Reviewed; 761 AA.
AC D6XZ22;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=1,2-alpha-glucosylglycerol phosphorylase {ECO:0000305};
DE EC=2.4.1.332 {ECO:0000269|PubMed:24466148, ECO:0000269|PubMed:24828502};
DE AltName: Full=2-O-alpha-glucosylglycerol phosphorylase {ECO:0000303|PubMed:24466148};
DE Short=GGP {ECO:0000303|PubMed:24466148};
GN OrderedLocusNames=Bsel_2816 {ECO:0000312|EMBL:ADI00307.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10 {ECO:0000312|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF GLU-475.
RX PubMed=24466148; DOI=10.1371/journal.pone.0086548;
RA Nihira T., Saito Y., Ohtsubo K., Nakai H., Kitaoka M.;
RT "2-O-alpha-D-glucosylglycerol phosphorylase from Bacillus selenitireducens
RT MLS10 possessing hydrolytic activity on beta-D-glucose 1-phosphate.";
RL PLoS ONE 9:E86548-E86548(2014).
RN [3] {ECO:0007744|PDB:4KTP, ECO:0007744|PDB:4KTR}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH BETA-D-GLUCOSE AND
RP GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND
RP MUTAGENESIS OF TYR-327; TRP-381; TYR-572 AND LYS-587.
RX PubMed=24828502; DOI=10.1074/jbc.m114.573212;
RA Touhara K.K., Nihira T., Kitaoka M., Nakai H., Fushinobu S.;
RT "Structural basis for reversible phosphorolysis and hydrolysis reactions of
RT 2-O-alpha-glucosylglycerol phosphorylase.";
RL J. Biol. Chem. 289:18067-18075(2014).
CC -!- FUNCTION: Catalyzes both the (1) reversible phosphorolysis of 2-O-
CC alpha-D-glucopyranosyl-sn-glycerol (GG) from beta-D-glucose 1-phosphate
CC (betaGlc1P) and glycerol and (2) the hydrolysis of betaGlc1P. the
CC betaGlc1P hydrolysis is a glucosyl-transfer reaction to an acceptor
CC water molecule that produces an anomer-inverted alpha-glucose, not a
CC phosphatase-type reaction. In the absence of glycerol produces alpha-D-
CC glucopyranose and phosphate from beta-D-glucopyranose 1-phosphate.
CC {ECO:0000269|PubMed:24466148, ECO:0000269|PubMed:24828502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-O-(alpha-D-glucopyranosyl)glycerol + phosphate = beta-D-
CC glucose 1-phosphate + glycerol; Xref=Rhea:RHEA:43060,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:43474, ChEBI:CHEBI:57684,
CC ChEBI:CHEBI:82766; EC=2.4.1.332;
CC Evidence={ECO:0000269|PubMed:24466148, ECO:0000269|PubMed:24828502};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for 2-O-alpha-D-glucopyranosyl-sn-glycerol
CC {ECO:0000269|PubMed:24466148};
CC KM=0.57 mM for phosphate {ECO:0000269|PubMed:24466148};
CC Note=kcat is 95 sec(-1) with 2-O-alpha-D-glucopyranosyl-sn-glycerol.
CC {ECO:0000269|PubMed:24466148};
CC pH dependence:
CC Optimum pH is 6.0-8.0. {ECO:0000269|PubMed:24466148};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:24466148,
CC ECO:0000269|PubMed:24828502}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; CP001791; ADI00307.1; -; Genomic_DNA.
DR RefSeq; WP_013173720.1; NC_014219.1.
DR PDB; 4KTP; X-ray; 1.90 A; A/B=1-761.
DR PDB; 4KTR; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-761.
DR PDBsum; 4KTP; -.
DR PDBsum; 4KTR; -.
DR AlphaFoldDB; D6XZ22; -.
DR SMR; D6XZ22; -.
DR STRING; 439292.Bsel_2816; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR EnsemblBacteria; ADI00307; ADI00307; Bsel_2816.
DR KEGG; bse:Bsel_2816; -.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_2_1_9; -.
DR OMA; ECAKFYY; -.
DR BRENDA; 2.4.1.332; 13105.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR005194; Glyco_hydro_65_C.
DR InterPro; IPR005195; Glyco_hydro_65_M.
DR InterPro; IPR005196; Glyco_hydro_65_N.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR017045; Malt_Pase/Glycosyl_Hdrlase.
DR Pfam; PF03633; Glyco_hydro_65C; 1.
DR Pfam; PF03632; Glyco_hydro_65m; 1.
DR Pfam; PF03636; Glyco_hydro_65N; 1.
DR PIRSF; PIRSF036289; Glycosyl_hydrolase_malt_phosph; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..761
FT /note="1,2-alpha-glucosylglycerol phosphorylase"
FT /id="PRO_0000432712"
FT ACT_SITE 475
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:24828502"
FT BINDING 327..328
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000269|PubMed:24828502,
FT ECO:0007744|PDB:4KTR"
FT BINDING 333..334
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24828502,
FT ECO:0007744|PDB:4KTP"
FT BINDING 587..588
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:24828502,
FT ECO:0007744|PDB:4KTP"
FT MUTAGEN 327
FT /note="Y->F: Abolishes both phosphorylase and hydrolase
FT activities."
FT /evidence="ECO:0000269|PubMed:24828502"
FT MUTAGEN 381
FT /note="W->F: Impaired phosphorylase activity without
FT affecting the hydrolase activity."
FT /evidence="ECO:0000269|PubMed:24828502"
FT MUTAGEN 475
FT /note="E->A,Q: Loss of function."
FT /evidence="ECO:0000269|PubMed:24466148"
FT MUTAGEN 572
FT /note="Y->F: Impairs both phosphorylase and hydrolase
FT activities."
FT /evidence="ECO:0000269|PubMed:24828502"
FT MUTAGEN 587
FT /note="K->A: Abolishes both phosphorylase and hydrolase
FT activities."
FT /evidence="ECO:0000269|PubMed:24828502"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 140..151
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 197..208
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 266..284
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 292..308
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 362..371
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 416..431
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 441..455
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 484..503
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 506..516
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 520..532
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 559..565
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 575..577
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 591..597
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 604..614
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 615..617
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 625..635
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 639..650
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 651..656
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:4KTP"
FT HELIX 672..683
FT /evidence="ECO:0007829|PDB:4KTP"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 707..715
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 718..733
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 748..752
FT /evidence="ECO:0007829|PDB:4KTP"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:4KTP"
SQ SEQUENCE 761 AA; 86261 MW; 83C736FB42D580D8 CRC64;
MHEIGEHLTT NTGWDIIKNR YEAAQAITEG SNFMIGNGFM GYRGTFAEDG KDAYAACIVT
DTWDKADGKW EELSTVPNAL LTLLHVDGEP FIMSEEAASF ERTLDLSQGV TSRKVSQRMK
NGATITIHEE KFASYRKKHA VLMKYTVESD QDTDAVLDTG IDYDVWSING DHLQGHHYFS
HPTGDGVTAK TVSYEDTVTV VETCSLDADA SEEDYQNPDG SGRTFSLSLE AGKPVTLEKA
MIIYSSNDVD NPQDEALLEA KHMQSYEEEK AANRLEWDNL WSHYDVTIQN NIIDQVALRF
NIYHAIIATP VHKSLPIGAR GLSCQAYQGA AFWDQEIYNM PMYLYSNPEI ARNILKYRHR
TLDGARRKAK RLGYEGAYYA WISGKTGDEL CPDFFFKDVL SGRDIRNHFN DWQIHISPDI
AYAVKKYHQV TGDDAFIRDY GAEMIFEIAR FLASHAVYKP MRGRYEFMRV QGPDEYHENV
DNNAFTNHQA MFTLQAADEL LQTLDEKTLS AVKEKIGLSD DEISLWRDML ANTYVPKPDK
HGIIEQFDGY YDLETIIPAK KVTERLIKED EYYGYPNGVT VRTQCIKQAD VIQLFVLHPH
LYDRKTVELN YEFYEPRTLH FSSLSPSSYA IVAAQIDKVE EAYRNFRKSV MIDLLNTNEA
VSGGTFIGGI HTAANGASWQ MVVNGFGGLS VHGDDIHLSP RLPDAWDGYT FKAIVKGQTL
EVDVTKEQIT ITNKSEDRKP LTLHIFGEKS VLDSERITKS R
