KOJP_ECOLI
ID KOJP_ECOLI Reviewed; 755 AA.
AC P77154;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Kojibiose phosphorylase {ECO:0000303|PubMed:29684280};
DE EC=2.4.1.230 {ECO:0000269|PubMed:29684280};
GN Name=ycjT; OrderedLocusNames=b1316, JW1309;
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, 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: In vitro catalyzes the phosphorolysis of D-kojibiose into
CC beta-D-glucose 1-phosphate and D-glucose. No other disaccharides tested
CC substitute for D-kojibiose. In the reverse direction disaccharides can
CC be formed from beta-D-glucose 1-phosphate plus D-glucose, L-sorbose, D-
CC sorbitol, L-iditol or 1,5-anhydro-D-glucitol, but with low efficiency.
CC The beta-D-glucose 1-phosphate product is the substrate for YcjU (AC
CC P77366), the next apparent enzyme in the putative biochemical pathway
CC encoded in this locus (yjcM to ycjW). {ECO:0000269|PubMed:29684280}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=kojibiose + phosphate = beta-D-glucose 1-phosphate + D-
CC glucose; Xref=Rhea:RHEA:11176, ChEBI:CHEBI:4167, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57684, ChEBI:CHEBI:142460; EC=2.4.1.230;
CC Evidence={ECO:0000269|PubMed:29684280};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.05 mM for kojibiose (at pH 7.5, 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC KM=3.0 mM for phosphate (at pH 7.5, 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC KM=1.7 mM for D-glucose (at pH 7.5, 30 degrees Celsius)
CC {ECO:0000269|PubMed:29684280};
CC Note=kcat is 1.0 sec(-1) for phosphorolysis of kojibiose, and kcat is
CC 0.8 sec(-1) for the reverse reaction. {ECO:0000269|PubMed:29684280};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown on glucose.
CC {ECO:0000269|PubMed:29684280}.
CC -!- MISCELLANEOUS: Kojibiose does not support bacterial growth of K12 /
CC BW25113 nor of BL-21(DE3), perhaps because it is not transported into
CC E.coli. {ECO:0000269|PubMed:29684280}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 65 family. {ECO:0000305}.
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DR EMBL; U00096; AAC74398.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14891.1; -; Genomic_DNA.
DR PIR; G64880; G64880.
DR RefSeq; NP_415832.1; NC_000913.3.
DR RefSeq; WP_000198036.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P77154; -.
DR SMR; P77154; -.
DR BioGRID; 4263194; 19.
DR IntAct; P77154; 1.
DR STRING; 511145.b1316; -.
DR CAZy; GH65; Glycoside Hydrolase Family 65.
DR PaxDb; P77154; -.
DR PRIDE; P77154; -.
DR EnsemblBacteria; AAC74398; AAC74398; b1316.
DR EnsemblBacteria; BAA14891; BAA14891; BAA14891.
DR GeneID; 945895; -.
DR KEGG; ecj:JW1309; -.
DR KEGG; eco:b1316; -.
DR PATRIC; fig|1411691.4.peg.963; -.
DR EchoBASE; EB3676; -.
DR eggNOG; COG1554; Bacteria.
DR HOGENOM; CLU_006285_2_1_6; -.
DR InParanoid; P77154; -.
DR OMA; EAYCIPF; -.
DR PhylomeDB; P77154; -.
DR BioCyc; EcoCyc:G6654-MON; -.
DR BioCyc; MetaCyc:G6654-MON; -.
DR BRENDA; 2.4.1.230; 2026.
DR PRO; PR:P77154; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central.
DR GO; GO:0033831; F:kojibiose phosphorylase activity; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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 Glycosidase; Hydrolase; Reference proteome; Transferase.
FT CHAIN 1..755
FT /note="Kojibiose phosphorylase"
FT /id="PRO_0000108017"
FT ACT_SITE 473
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 333..334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
FT BINDING 573..574
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:D6XZ22"
SQ SEQUENCE 755 AA; 84867 MW; 89A645A7A5AB599D CRC64;
MTRPVTLSEP HFSQHTLNKY ASLMAQGNGY LGLRASHEED YTRQTRGMYL AGLYHRAGKG
EINELVNLPD VVGMEIAING EVFSLSHEAW QRELDFASGE LRRNVVWRTS NGSGYTIASR
RFVSADQLPL IALEITITPL DADASVLIST GIDATQTNHG RQHLDETQVR VFGQHLMQGS
YTTQDGRSDV AISCCCKVSG DVQQCYTAKE RRLLQHTSAQ LHAGETMTLQ KLVWIDWRDD
RQAALDEWGS ASLRQLEMCA QQSYDQLLAA STENWRQWWQ KRRITVNGGE AHDQQALDYA
LYHLRIMTPA HDERSSIAAK GLTGEGYKGH VFWDTEVFLL PFHLFSDPTV ARSLLRYRWH
NLPGAQEKAR RNGWQGALFP WESARSGEEE TPEFAAINIR TGLRQKVASA QAEHHLVADI
AWAVIQYWQT TGDESFIAHE GMALLLETAK FWISRAVRVN DRLEIHDVIG PDEYTEHVNN
NAYTSYMARY NVQQALNIAR QFGCSDDAFI HRAEMFLKEL WMPEIQPDGV LPQDDSFMAK
PAINLAKYKA AAGKQTILLD YSRAEVNEMQ ILKQADVVML NYMLPEQFSA ASCLANLQFY
EPRTIHDSSL SKAIHGIVAA RCGLLTQSYQ FWREGTEIDL GADPHSCDDG IHAAATGAIW
LGAIQGFAGV SVRDGELHLN PALPEQWQQL SFPLFWQGCE LQVTLDAQRI AIRTSAPVSL
RLNGQLITVA EESVFCLGDF ILPFNGTATK HQEDE
