GGAP_ECOLI
ID GGAP_ECOLI Reviewed; 559 AA.
AC P76041; P78149; P78151;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glucosylglycerate phosphorylase {ECO:0000303|PubMed:28754708};
DE Short=GGa phosphorylase {ECO:0000303|PubMed:28754708};
DE Short=GGaP {ECO:0000303|PubMed:28754708};
DE EC=2.4.1.352 {ECO:0000269|PubMed:28754708, ECO:0000269|PubMed:29684280};
GN Name=ycjM; Synonyms=ggaP; OrderedLocusNames=b1309, JW1302;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=28754708; DOI=10.1128/aem.01434-17;
RA Franceus J., Pinel D., Desmet T.;
RT "Glucosylglycerate phosphorylase, an enzyme with novel specificity involved
RT in compatible solute metabolism.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=29684280; DOI=10.1021/acs.biochem.8b00392;
RA Mukherjee K., Narindoshvili T., Raushel F.M.;
RT "Discovery of a kojibiose phosphorylase in Escherichia coli K-12.";
RL Biochemistry 57:2857-2867(2018).
CC -!- FUNCTION: Catalyzes the reversible phosphorolysis of glucosylglycerate
CC into alpha-D-glucose 1-phosphate (Glc1P) and D-glycerate (also called
CC (R)-glycerate) (PubMed:28754708, PubMed:29684280). May be a regulator
CC of intracellular levels of glucosylglycerate, a compatible solute that
CC primarily protects organisms facing salt stress and very specific
CC nutritional constraints (PubMed:28754708). Cannot catalyze the
CC phosphorolysis of sucrose (PubMed:28754708). Does not act on other
CC sugars such as alpha-D-galactose 1-phosphate, alpha-D-mannose 1-
CC phosphate or beta-D-glucose 1-phosphate; in vitro D-erythronate can
CC substitute for D-glycerate with a much lower efficiency
CC (PubMed:29684280). {ECO:0000269|PubMed:28754708,
CC ECO:0000269|PubMed:29684280}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-glucopyranosyl)-glycerate + phosphate = (R)-
CC glycerate + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:55268,
CC ChEBI:CHEBI:16659, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601,
CC ChEBI:CHEBI:62510; EC=2.4.1.352;
CC Evidence={ECO:0000269|PubMed:28754708, ECO:0000269|PubMed:29684280};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for D-glycerate (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:28754708};
CC KM=69 uM for 2-O-(alpha-D-glucopyranosyl)-D-glycerate (at pH 6.5 and
CC 30 degrees Celsius) {ECO:0000269|PubMed:29684280};
CC KM=2.2 mM for phosphate (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC KM=9.4 mM for alpha-D-glucose 1-phosphate (at pH 6.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:29684280};
CC KM=4.4 mM for D-glycerate (at pH 6.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC Note=kcat is 2.2 sec(-1) for phosphorolysis of 2-O-(alpha-D-
CC glucopyranosyl)-D-glycerate, kcat is 325 sec(-1) for glyceration of
CC alpha-D-glucose 1-phosphate. {ECO:0000269|PubMed:29684280};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown on glucose.
CC {ECO:0000269|PubMed:29684280}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC Glucosylglycerate phosphorylase subfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74391.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14886.1; -; Genomic_DNA.
DR PIR; H64879; H64879.
DR RefSeq; NP_415825.4; NC_000913.3.
DR RefSeq; WP_000810499.1; NZ_LN832404.1.
DR AlphaFoldDB; P76041; -.
DR SMR; P76041; -.
DR BioGRID; 4263230; 11.
DR IntAct; P76041; 2.
DR STRING; 511145.b1309; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; P76041; -.
DR PRIDE; P76041; -.
DR EnsemblBacteria; AAC74391; AAC74391; b1309.
DR EnsemblBacteria; BAA14886; BAA14886; BAA14886.
DR GeneID; 945659; -.
DR KEGG; ecj:JW1302; -.
DR KEGG; eco:b1309; -.
DR PATRIC; fig|1411691.4.peg.970; -.
DR EchoBASE; EB3669; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_021358_0_0_6; -.
DR InParanoid; P76041; -.
DR OMA; PNATQFT; -.
DR PhylomeDB; P76041; -.
DR BioCyc; EcoCyc:G6647-MON; -.
DR BioCyc; MetaCyc:G6647-MON; -.
DR BRENDA; 2.4.1.352; 2026.
DR PRO; PR:P76041; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0110068; F:glucosylglycerate phosphorylase activity; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11356; AmyAc_Sucrose_phosphorylase-like_1; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR033746; GGa_phosphorylase.
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 Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF003059; Sucrose_phosphorylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..559
FT /note="Glucosylglycerate phosphorylase"
FT /id="PRO_0000072299"
FT ACT_SITE 229
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:A0ZZH6"
SQ SEQUENCE 559 AA; 64186 MW; C05B71B0E0E369C2 CRC64;
MKQKITDYLD EIYGGTFTAT HLQKLVTRLE SAKRLITQRR KKHWDESDVV LITYADQFHS
NDLKPLPTFN QFYHQWLQSI FSHVHLLPFY PWSSDDGFSV IDYHQVASEA GEWQDIQQLG
ECSHLMFDFV CNHMSAKSEW FKNYLQQHPG FEDFFIAVDP QTDLSAVTRP RALPLLTPFQ
MRDHSTRHLW TTFSDDQIDL NYRSPEVLLA MVDVLLCYLA KGAEYVRLDA VGFMWKEPGT
SCIHLEKTHL IIKLLRSIID NVAPGTVIIT ETNVPHKDNI AYFGAGDDEA HMVYQFSLPP
LVLHAVQKQN VEALCAWAQN LTLPSSNTTW FNFLASHDGI GLNPLRGLLP ESEILELVEA
LQQEGALVNW KNNPDGTRSP YEINVTYMDA LSRRESSDEE RCARFILAHA ILLSFPGVPA
IYIQSILGSR NDYAGVEKLG YNRAINRKKY HSKEITRELN DEATLRHAVY HELSRLITLR
RSHNEFHPDN NFTIDTINSS VMRIPRSNAD GNCLTGLFNV SKNIQHVNIT NLHGRDLISE
VDILGNEITL RPWQVMWIK
