ID   D4LDC6_RUMC1            Unreviewed;       716 AA.
AC   D4LDC6;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   02-SEP-2026, entry version 70.
DE   SubName: Full=Beta-mannanase {ECO:0000313|EMBL:CBL17621.1};
GN   OrderedLocusNames=RUM_15270 {ECO:0000313|EMBL:CBL17621.1};
OS   Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS   18P13).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales;
OC   Oscillospiraceae; Ruminococcus.
OX   NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL17621.1, ECO:0000313|Proteomes:UP000007054};
RN   [1] {ECO:0000313|EMBL:CBL17621.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Type strain: 18P13 {ECO:0000313|EMBL:CBL17621.1};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Ruminococcus sp. 18P13.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL17621.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Type strain: 18P13 {ECO:0000313|EMBL:CBL17621.1};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
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DR   EMBL; FP929052; CBL17621.1; -; Genomic_DNA.
DR   RefSeq; WP_015558527.1; NZ_BAAIFP010000004.1.
DR   AlphaFoldDB; D4LDC6; -.
DR   STRING; 213810.RUM_15270; -.
DR   CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   GeneID; 83156246; -.
DR   KEGG; rch:RUM_15270; -.
DR   PATRIC; fig|213810.4.peg.1425; -.
DR   HOGENOM; CLU_016930_1_0_9; -.
DR   BioCyc; RCHA213810:RUM_RS07435-MONOMER; -.
DR   Proteomes; UP000007054; Chromosome.
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:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   CDD; cd04086; CBM35_mannanase-like; 1.
DR   CDD; cd14256; Dockerin_I; 1.
DR   Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR005084; CBM6.
DR   InterPro; IPR002105; Dockerin_1_rpt.
DR   InterPro; IPR016134; Dockerin_dom.
DR   InterPro; IPR036439; Dockerin_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   PANTHER; PTHR40079:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR   Pfam; PF16990; CBM_35; 2.
DR   Pfam; PF00404; Dockerin_1; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF63446; Type I dockerin domain; 1.
DR   PROSITE; PS51175; CBM6; 2.
DR   PROSITE; PS51766; DOCKERIN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PROSITE-ProRule:PRU10142};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW   ProRule:PRU01100};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01100}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU10142};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007054};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..716
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003060860"
FT   DOMAIN          40..168
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          188..508
FT                   /note="GH26"
FT                   /evidence="ECO:0000259|PROSITE:PS51764"
FT   DOMAIN          529..650
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          654..716
FT                   /note="Dockerin"
FT                   /evidence="ECO:0000259|PROSITE:PS51766"
FT   ACT_SITE        349
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        456
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ   SEQUENCE   716 AA;  79544 MW;  054F48F7F6A776B2 CRC64;
     MNSFVKRLGS ALTASAMMLT AGIFVPVQAA DTGADAAPLF TAEAEDCTLL TGASVTTNVY
     GTEYPGYSGD GFVWAGNAGG MTFEVDVPEN AMYELTTRCW MYLGDPGTTR MQTLAIDGDV
     KSSIYIANNE KWEDSSFGFF YLEKGKHTIE VGATGSWGFI LYDTVTFDFA DMPELNIAPD
     PCDKNATAET KALMKYMTGQ YGNHIISGQQ EIYGGGNNGD TELEFRYIYE TTGKYPVIRG
     FDFMNYNPLY GWEDGTTGRV INWVANCGGI ATASWHINVP QDFDSYTLGD QLDWQKCTYK
     PTSSFNTANC LDPTTKEYKY LMLAIEDLAE QLLILQDANV PIIFRPFHEA EGNNNTNGSG
     AWFWWGSSGA EVYKELWKLL YTTLTEEYGI HNCIWEVNLY DYANSAQWYP GNDYVDMVAY
     DKYEGSPYTW NTSAATSVFL TLVNDTNDTK MVALAENDVI PDITNMVNEG AWWSYFCPWY
     GDFITNGTTN TKEMLDKIYN SDYVVTLDEV PNDLYGYARG NGGNWNVEGA YECEDGNIQT
     NKGTTTVAYD YCSGGKYVYL QGEGDYIEQT VTVEKAGKYA IRYGYQQNFE KNGKTQNLYV
     NGTAVGEAFF PYSILFGESD AIVVELKAGK NTIKVESGEG WTYFDYLTVS YVGDDILTGD
     INLDGKLSVS DVVLLQKYLI KSGKLTADQA KRADLNGDGV LNAYDLALLK HTMLGK
//