ID   MANC_PIRSP              Reviewed;         569 AA.
AC   P55298;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   22-FEB-2023, entry version 102.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase C;
DE            EC=3.2.1.78;
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase C;
DE   AltName: Full=Beta-mannanase C;
DE   Flags: Precursor;
GN   Name=MANC;
OS   Piromyces sp.
OC   Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC   Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC   Neocallimastigaceae; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X97520; CAA66134.1; -; mRNA.
DR   AlphaFoldDB; P55298; -.
DR   SMR; P55298; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   CLAE; MAN26C_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   CDD; cd04086; CBM35_mannanase-like; 1.
DR   Gene3D; 3.90.1220.10; Cellulose docking domain, dockering; 2.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 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; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF64571; Cellulose docking domain, dockering; 2.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..569
FT                   /note="Mannan endo-1,4-beta-mannosidase C"
FT                   /id="PRO_0000012176"
FT   DOMAIN          21..139
FT                   /note="CBM6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00523"
FT   DOMAIN          163..457
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   DOMAIN          489..525
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          532..569
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   ACT_SITE        317
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        405
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
FT   BINDING         377
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B4XC07"
SQ   SEQUENCE   569 AA;  64115 MW;  19277764E18328B5 CRC64;
     MLTLTLLLYL SFITTVFSKK VIYEAENGKL DGVSKYNELQ GYSGTGYVGR FESAGNSVTV
     TVEVSQTGMY DMSIIYCGNM GQKINSLKIN GKNSGDITFP ENSSFEELNI GAVYLNSGEN
     TVSLVASWGW IWIDALVVND TPNVAKDVSP HINPTLVNPK AIPAAKKLYD FLRSNYGKRI
     LSGQVGGAGQ AGDEGQEIQR IQKATGKLPA VWNMDFIFES NDCTWRPENP DITEMAINWW
     KKYQGKGIMA AQWHWNIAGK TGDFAFYKKD TTFSIDNAVT EGTWEYEKII KDIDRVAGHI
     KKLQAVNMPL IWRPLHENDG DWFWWGNNPK SCAKLWKILY ERMVNYHGLN NLIWLWNGKN
     DANTPVDYID IIGVDIYAND HGPQTTAYNT HFDFYGGKKM VVLSENGRIP DIQQCVDQNA
     WWGYFQTWNS EFILQDSYHT DAQLKEYFTH KTVMNMDELP SFNVNSYEYQ SGNNNNNSSN
     NNNNNNSSEC FSIPLGYPCC KGNTVVYTDN DGDWGVENNE WCGIGNSSSA VVCWSEALGY
     PCCVSSSDVY YTDNDGEWGV ENGDWCGII
//