ID   MANB_PIRSP              Reviewed;         571 AA.
AC   P55297;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase B;
DE            EC=3.2.1.78;
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase B;
DE   AltName: Full=Beta-mannanase B;
DE   Flags: Precursor;
GN   Name=MANB;
OS   Piromyces sp.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; Piromyces; unclassified Piromyces.
OX   NCBI_TaxID=45796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8768520; DOI=10.1111/j.1574-6968.1996.tb08382.x;
RA   Millward-Sadler S.J., Hall J., Black G.W., Hazlewood G.P., Gilbert H.J.;
RT   "Evidence that the Piromyces gene family encoding endo-1,4-mannanases arose
RT   through gene duplication.";
RL   FEMS Microbiol. Lett. 141:183-188(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC         mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR   EMBL; X97408; CAA66061.1; -; mRNA.
DR   AlphaFoldDB; P55297; -.
DR   SMR; P55297; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   CLAE; MAN26B_PIRSP; -.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1220.10; -; 2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR005084; CMB_fam6.
DR   InterPro; IPR009034; Dockerin_dom_fun_sf.
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; PF02013; CBM_10; 2.
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   SUPFAM; SSF64571; SSF64571; 2.
DR   PROSITE; PS51763; CBM10; 2.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Repeat; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..571
FT                   /note="Mannan endo-1,4-beta-mannosidase B"
FT                   /id="PRO_0000012175"
FT   DOMAIN          22..141
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          165..459
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   DOMAIN          491..527
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          534..571
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   ACT_SITE        319
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        407
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ   SEQUENCE   571 AA;  64397 MW;  B13E44581FAA9DAA CRC64;
     MNSLSLLLFC IFFVFSTFAK KVYYEAENGK LDGVTVYKSD LTGFSGTGYV GRFENPGNSV
     TVTVEVPQTG MYDLTIVYCA NMGQKINSLT VNGQSAGDIT FTENTKFEDL NVGAIYLNKG
     KNTIGLVSSW GWMWVDAFVI NDAPNAAKDV TSKLNPTLIN PKAIPAAKKL YDFLKTNYGK
     RILSGQVGAA GQAGDEGQEI QRIQKATGKL PAVWNMDFIF ESNDCTWRPQ NPDITEMAIN
     WWKKYQGKGI MSAQWHWNIA GKTGDFAFYK KDTTFSIDNA VTEGTWEYEK IIKDIDRVAG
     HIKKLQAVNM PLIWRPLHEN DGDWFWWGNN PKSCAKLWKI LYERMVNYHG LNNLIWLWNG
     KNDANTPVDY IDIIGVDIYA NDHGPQTTAY NTHFDFYGGK KMVVLSENGR IPDIQQCVDQ
     NAWWGYFQTW NSEFILQDSY HTDAQLKEYF THKTVMNMDE LPSFNVNSYE YQSGNNNNNS
     SNNNNNNNSS ECFSIPLGYP CCKGNTVVYT DNDGDWGVEN NEWCGIGNSS SAVVCWSEAL
     GYPCCVSSSD VYYTDNDGEW GVENGDWCGI I