XY30A_MYCTT
ID XY30A_MYCTT Reviewed; 477 AA.
AC G2Q1N4;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=GH30 family xylanase {ECO:0000303|PubMed:31110561};
DE EC=3.2.1.- {ECO:0000269|PubMed:31110561};
DE Flags: Precursor;
GN Name=Xyn30A {ECO:0000303|PubMed:31110561}; ORFNames=MYCTH_38558;
OS Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799)
OS (Sporotrichum thermophile).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX NCBI_TaxID=573729;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42464 / BCRC 31852 / DSM 1799;
RX PubMed=21964414; DOI=10.1038/nbt.1976;
RA Berka R.M., Grigoriev I.V., Otillar R., Salamov A., Grimwood J., Reid I.,
RA Ishmael N., John T., Darmond C., Moisan M.-C., Henrissat B., Coutinho P.M.,
RA Lombard V., Natvig D.O., Lindquist E., Schmutz J., Lucas S., Harris P.,
RA Powlowski J., Bellemare A., Taylor D., Butler G., de Vries R.P.,
RA Allijn I.E., van den Brink J., Ushinsky S., Storms R., Powell A.J.,
RA Paulsen I.T., Elbourne L.D.H., Baker S.E., Magnuson J., LaBoissiere S.,
RA Clutterbuck A.J., Martinez D., Wogulis M., de Leon A.L., Rey M.W.,
RA Tsang A.;
RT "Comparative genomic analysis of the thermophilic biomass-degrading fungi
RT Myceliophthora thermophila and Thielavia terrestris.";
RL Nat. Biotechnol. 29:922-927(2011).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOTECHNOLOGY.
RX PubMed=31110561; DOI=10.1186/s13068-019-1455-2;
RA Katsimpouras C., Dedes G., Thomaidis N.S., Topakas E.;
RT "A novel fungal GH30 xylanase with xylobiohydrolase auxiliary activity.";
RL Biotechnol. Biofuels 12:120-120(2019).
CC -!- FUNCTION: Xylanase exhibiting endo- and exo-xylanase activity
CC (PubMed:31110561). Shows the highest activity toward beechwood
CC glucuronoxylan, which consists of a beta-1,4-linked xylose backbone
CC decorated with the methylated form of D-glucuronic acid (MeGlcA)
CC attached directly to the main chain at xylose C2 (PubMed:31110561).
CC Acts also against wheat arabinoxylan, a xylan without MeGlcA
CC substituents along the main chain, but the xylanase activity is about
CC two orders of magnitude lower than that achieved in the case of
CC beechwood xylan (PubMed:31110561). Shows no activity against carob
CC galactomannan, konjac glucomannan, or barley beta-glucan
CC (PubMed:31110561). The recombinant xylanase also exhibits an exo-
CC activity by releasing processively disaccharide units from the non-
CC reducing end of linear and decorated xylooligosaccharides (XOS)
CC (PubMed:31110561). {ECO:0000269|PubMed:31110561}.
CC -!- ACTIVITY REGULATION: Activity is enhanced by 10 mM Co(2+), Cu 2(2+) and
CC Mn(2+) to levels as high as 44% (PubMed:31110561). Partial inhibition
CC of activity from 5 to 15% is observed in the presence of the following
CC compouinds at a centration of 10 mM (from higher inhibition to lower):
CC EDTA > Mg(2+) > urea, Zn(2+) > Fe(3+) (PubMed:31110561).
CC {ECO:0000269|PubMed:31110561}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.7 mg/ml for beechwood xylan {ECO:0000269|PubMed:31110561};
CC Vmax=7.1 umol/min/mg enzyme toward beechwood xylan
CC {ECO:0000269|PubMed:31110561};
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:31110561};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:31110561};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:31110561}.
CC -!- BIOTECHNOLOGY: The recombinant xylanase could be used for the
CC production of disaccharide units and uronic xylooligosaccharides from
CC glucuronoxylan, which in turn would be utilized as prebiotics carrying
CC manifold health benefits. {ECO:0000269|PubMed:31110561}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {ECO:0000305}.
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DR EMBL; CP003002; AEO55025.1; -; Genomic_DNA.
DR RefSeq; XP_003660270.1; XM_003660222.1.
DR AlphaFoldDB; G2Q1N4; -.
DR SMR; G2Q1N4; -.
DR STRING; 78579.XP_003660270.1; -.
DR EnsemblFungi; AEO55025; AEO55025; MYCTH_38558.
DR GeneID; 11508437; -.
DR KEGG; mtm:MYCTH_38558; -.
DR VEuPathDB; FungiDB:MYCTH_38558; -.
DR eggNOG; KOG2566; Eukaryota.
DR HOGENOM; CLU_031530_1_0_1; -.
DR InParanoid; G2Q1N4; -.
DR OrthoDB; 644299at2759; -.
DR Proteomes; UP000007322; Chromosome 1.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004348; F:glucosylceramidase activity; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:InterPro.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR039514; 6GAL-like.
DR InterPro; IPR033452; GH30_C.
DR InterPro; IPR001139; Glyco_hydro_30.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11069; PTHR11069; 1.
DR Pfam; PF14587; Glyco_hydr_30_2; 1.
DR Pfam; PF17189; Glyco_hydro_30C; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..477
FT /note="GH30 family xylanase"
FT /id="PRO_5003435145"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 477 AA; 50883 MW; 4E490DB0637B0EB7 CRC64;
MYSLLIALLC AGTAVDAQAL QQRQAGTTLT VDLSTTYQRI DGFGTSEAFQ RAVQMSRLPE
EGQRRALDVL FSTTNGAGLS ILRNGIGSSP DMSSDHMVSI APKSPGSPNN PLIYSWDGSD
NKQLWVSQEA VHTYGVKTIY ADAWSAPGYM KTNGNDANGG TLCGLSGAQC ASGDWRQAYA
DYLTKYVEFY QESNVTVTHL GFINEPELTT SYASMRFSAS QAAEFIRILY PTIQKSNLTY
KPTIACCDAE GWNSQAGMLG ALSSVNSMFG LVTAHAYTSQ PGFSMNTPHP VWMTEAADLQ
GAWTSAWYSY GGAGEGWTWA NNVYNAIVNG NASAYLYWIG AQTGNTNSHM VHIDANAGTV
EPSKRLWALG QWSRFVRPGA RRVAVSGASG SLRTAAFRNE DGSVAVVVIN SGGDAAVNVR
LASSSSADQQ PASAKAWATD NSRAIEEIQA SFADGVATVN VPSRSMTTVV LYPAADA
