ID   MA26A_MYCTT             Reviewed;         482 AA.
AC   G2Q4H7;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000305};
DE            EC=3.2.1.- {ECO:0000269|PubMed:27193267};
DE   AltName: Full=Endo-(1,4)-beta-mannanase {ECO:0000305};
DE   AltName: Full=GH26 family endo-beta-mannanase {ECO:0000303|PubMed:27193267};
DE   Flags: Precursor;
GN   Name=Man26A {ECO:0000303|PubMed:27193267}; ORFNames=MYCTH_99077;
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=27193267; DOI=10.1007/s00253-016-7609-2;
RA   Katsimpouras C., Dimarogona M., Petropoulos P., Christakopoulos P.,
RA   Topakas E.;
RT   "A thermostable GH26 endo-beta-mannanase from Myceliophthora thermophila
RT   capable of enhancing lignocellulose degradation.";
RL   Appl. Microbiol. Biotechnol. 100:8385-8397(2016).
CC   -!- FUNCTION: Mannan endo-1,4-beta-mannosidase that exhibits high activity
CC       against konjac glucomannan and carob galactomannan, as well as a lower
CC       activity toward beta-mannan (PubMed:27193267). Shows no activity
CC       against barley beta-glucan, birchwood xylan, and low viscosity
CC       carboxymethyl cellulose (CMC) (PubMed:27193267). Has the ability to
CC       hydrolyze manno-oligosaccharides such as M4 which is degraded slightly
CC       to M3 and M1, M5 which is mainly degraded to M4 and M1, and M6 which is
CC       mostly hydrolyzed to M4 and M2 (PubMed:27193267). Shows no activity
CC       toward M2 and M3 manno-oligosaccharides (PubMed:27193267).
CC       {ECO:0000269|PubMed:27193267}.
CC   -!- ACTIVITY REGULATION: The activity is completely impaired by Ag(+),
CC       partially inhibited by Zn(2+), and enhanced by Co(2+), Ni(2+) and
CC       Cu(2+) by 22.6, 14.5 and 20.8 %, respectively (PubMed:27193267).
CC       Ca(2+), Na(+), Mg(2+), Mn(2+), urea and EDTA do not significantly
CC       affect the mannanase activity (PubMed:27193267).
CC       {ECO:0000269|PubMed:27193267}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.22 mg/ml for carob galactomannan {ECO:0000269|PubMed:27193267};
CC         KM=3.22 mg/ml for konjac glucomannan {ECO:0000269|PubMed:27193267};
CC         Vmax=296.8 umol/min/mg enzyme toward carob galactomannan
CC         {ECO:0000269|PubMed:27193267};
CC         Vmax=475.2 umol/min/mg enzyme toward konjac glucomannan
CC         {ECO:0000269|PubMed:27193267};
CC       pH dependence:
CC         Optimum pH is 6.0. {ECO:0000269|PubMed:27193267};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:27193267};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:27193267}.
CC   -!- BIOTECHNOLOGY: The addition of Man26A as a supplement to the commercial
CC       enzyme mixture Celluclast(R) 1.5 L and Novozyme(R) 188 results in
CC       enhanced enzymatic hydrolysis of pretreated beechwood sawdust,
CC       improving the release of total reducing sugars and glucose by 13 and 12
CC       %, respectively. {ECO:0000269|PubMed:27193267}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family. {ECO:0000305}.
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DR   EMBL; CP003002; AEO53670.1; -; Genomic_DNA.
DR   RefSeq; XP_003658915.1; XM_003658867.1.
DR   AlphaFoldDB; G2Q4H7; -.
DR   SMR; G2Q4H7; -.
DR   STRING; 78579.XP_003658915.1; -.
DR   EnsemblFungi; AEO53670; AEO53670; MYCTH_99077.
DR   GeneID; 11508627; -.
DR   KEGG; mtm:MYCTH_99077; -.
DR   VEuPathDB; FungiDB:MYCTH_99077; -.
DR   eggNOG; ENOG502QT55; Eukaryota.
DR   HOGENOM; CLU_016930_1_1_1; -.
DR   InParanoid; G2Q4H7; -.
DR   OrthoDB; 792920at2759; -.
DR   BRENDA; 3.2.1.78; 13804.
DR   Proteomes; UP000007322; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:InterPro.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR40079; PTHR40079; 1.
DR   Pfam; PF16990; CBM_35; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..482
FT                   /note="Mannan endo-1,4-beta-mannosidase"
FT                   /id="PRO_5003436064"
FT   DOMAIN          42..160
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          181..474
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        332
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        422
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        300
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   482 AA;  52766 MW;  1C22E017638773E0 CRC64;
     MARTLRYLLC GILALAAGSN AVPAARGSTR AAPAAEPSTS ATTYEAEDAI LSGTTVDTAQ
     EGYTGSGYVT GFDEASDKIT FEVESEATKL YDLSIRIAAI YGDKHTTVVL NGGASSDVSF
     PAGDTWVDVP AGQVLLNEGA NTIEIVSNWG WYLVDSITLT PSAPRPEHQI NRSLNNPSAD
     ASARALYDYL RSIYGKKILA GQQDLTWADY VTQQTGKTPA LVSVDLMDYS PSRVERGTKG
     TSVEEAITHA ERGGIVSALW HWNAPAGLYD TDEHPWWSGF YTDATDFDVA AALSSTDNAN
     YTLLLRDIDA IAVQLKRLRD ARVPVLWRPL HEAEGGWFWW GAKGPDPAKQ LYALLYDRLV
     NHHGINNLIW VWNSLSPDWY PGDDTVDILS ADVYAQGNGP MSTQYNQLID LGKDKKMIAA
     AEVGAAPLPD LLQAYEAHWL WFAVWGDTFI NNAEWNSPEV LKTVYTSDYV LTLDEIQGWQ
     DS