GELL_GEOSE
ID GELL_GEOSE Reviewed; 204 AA.
AC P85513;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Gellan lyase;
DE EC=4.2.2.25;
DE Flags: Fragments;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND FUNCTION.
RC STRAIN=98 {ECO:0000269|Ref.1};
RA Atanassova M., Rodriguez-Alonso P., Garabal J.I., Derekova A.,
RA Terziiska A., Mandeva R., Kambourova M.;
RT "Primary structure analysis of a purified thermostable gellan lyase
RT produced by Bulgarian geothermal spring inhabitant Geobacillus
RT stearothermophilus 98.";
RL Eur. J. Biochem. 0:0-0(2008).
RN [2] {ECO:0000305}
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16482399; DOI=10.1007/s00792-005-0503-y;
RA Derekova A., Sjoholm C., Mandeva R., Michailova L., Kambourova M.;
RT "Biosynthesis of a thermostable gellan lyase by newly isolated and
RT characterized strain of Geobacillus stearothermophilus 98.";
RL Extremophiles 10:321-326(2006).
RN [3]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=98;
RX PubMed=20469643; DOI=10.1515/znc-2010-3-411;
RA Derekova A., Atanassova M., Christova P., Tchorbanov B., Shosheva A.,
RA Mandeva R., Rodriguez-Alonso P., Garabal J.I., Kambourova M.;
RT "Physicochemical characteristics of a thermostable gellan lyase from
RT Geobacillus stearothermophilus 98.";
RL Z. Naturforsch. C Biosci. 65:231-238(2010).
CC -!- FUNCTION: Cleaves the glycosidic bonds of gellan backbone and releases
CC tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with
CC unsaturated glucuronic acid at the non-reducing terminal. The enzyme is
CC highly specific to the heteropolysaccharide gellan.
CC {ECO:0000269|PubMed:16482399, ECO:0000269|PubMed:20469643,
CC ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-
CC glucopyranosyluronate bonds of gellan backbone releasing
CC tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-
CC glucopyranosyluronic acid at the non-reducing end. The
CC tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-
CC Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-
CC Glcp.; EC=4.2.2.25;
CC -!- ACTIVITY REGULATION: Activity is stimulated by zinc, potassium,
CC lithium, cobalt, sodium, calcium, iron, manganase, magnesium and
CC mercury ions at a concentration of 1 mM, but inhibited by copper ions
CC at a concentration of 1 mM. Activity is inhibited by potassium, sodium
CC and magnesium ions at a concentration of 1 M. Activity is inhibited by
CC urea, EDTA, dithiothreitol, p-CMB, PSF, natrium lauryl sulfate and N-
CC bromosuccinimide. {ECO:0000269|PubMed:16482399}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.21 uM for gellan {ECO:0000269|PubMed:16482399,
CC ECO:0000269|PubMed:20469643};
CC pH dependence:
CC Most active from pH 5.0 to 8.0. {ECO:0000269|PubMed:16482399,
CC ECO:0000269|PubMed:20469643};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Active from 50 to 80
CC degrees Celsius, at 55 degrees Celsius it has 50% of its full
CC activity. Thermostable, retains full activity after heating at 60
CC degrees Celsius for 24 hours. In the absence of substrate, its half
CC life at 70 degrees Celsius is 50 minutes. In the presence of
CC substrate full activity is retained after incubation at 70 degrees
CC Celsius for 2.5 hours. {ECO:0000269|PubMed:16482399,
CC ECO:0000269|PubMed:20469643};
CC -!- SUBUNIT: Multimer. {ECO:0000269|PubMed:16482399}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16482399}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the exponential growth phase.
CC {ECO:0000269|PubMed:16482399}.
CC -!- INDUCTION: By gellan. {ECO:0000269|PubMed:16482399}.
CC -!- CAUTION: The order of the peptides shown is unknown.
CC {ECO:0000269|PubMed:16482399}.
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DR AlphaFoldDB; P85513; -.
DR BRENDA; 4.2.2.25; 623.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052762; F:gellan lyase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lyase; Secreted.
FT CHAIN <1..>204
FT /note="Gellan lyase"
FT /id="PRO_0000367894"
FT NON_CONS 9..10
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 21..22
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 35..36
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 51..52
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 64..65
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 82..83
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 97..98
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 117..118
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 127..128
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 151..152
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 164..165
FT /evidence="ECO:0000303|Ref.1"
FT NON_CONS 190..191
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 1
FT /evidence="ECO:0000303|Ref.1"
FT NON_TER 204
FT /evidence="ECO:0000303|Ref.1"
SQ SEQUENCE 204 AA; 20542 MW; BF0BF2BE836460D7 CRC64;
LVSESNPGRA IPAGGKGATI RAARPGLATT LNGPKAGNGT TGATKLTTPA RPLSEGANMM
CDHRAGGNAA ISGSSVGEGT ARAGDSKVMS RMLSPKGSII AGTVNMMPAD IAAGSVRTPS
SLPPDGRSAT PMSVSEVASD ISHKDGSVNV TKDPVTAAGL TAMRKNANKG SPPASPLPLK
ADNKGVHINK HWVDLKNDND FNTR
