ID   MANB_BACIU              Reviewed;         360 AA.
AC   P55278;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000303|PubMed:7727534};
DE            EC=3.2.1.78 {ECO:0000250|UniProtKB:O05512};
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase {ECO:0000303|PubMed:7727534};
DE   AltName: Full=Beta-mannanase {ECO:0000303|PubMed:7727534};
DE   Flags: Precursor;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NM-39;
RX   PubMed=7727534; DOI=10.1016/0304-4165(95)00011-y;
RA   Mendoza N.S., Arai M., Sugimoto K., Ueda M., Kawaguchi T., Joson L.M.;
RT   "Cloning and sequencing of beta-mannanase gene from Bacillus subtilis NM-
RT   39.";
RL   Biochim. Biophys. Acta 1243:552-554(1995).
CC   -!- FUNCTION: Involved in the degradation of glucomannan. Catalyzes the
CC       endo hydrolysis of beta-1,4-linked mannan, galactomannan and
CC       glucomannan. {ECO:0000250|UniProtKB:O05512}.
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         Evidence={ECO:0000250|UniProtKB:O05512};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O05512}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O05512}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR   EMBL; D37964; BAA07178.1; -; Genomic_DNA.
DR   PIR; S60268; S60268.
DR   AlphaFoldDB; P55278; -.
DR   SMR; P55278; -.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR   InterPro; IPR022790; GH26_dom.
DR   InterPro; IPR000805; Glyco_hydro_26.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR016714; MANB/E.
DR   PANTHER; PTHR40079; PTHR40079; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PIRSF; PIRSF018168; Mannan-1_4-beta-mannosidase; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..360
FT                   /note="Mannan endo-1,4-beta-mannosidase"
FT                   /id="PRO_0000012171"
FT   DOMAIN          36..347
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        191
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   ACT_SITE        290
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   SITE            190
FT                   /note="Plays an important role in maintaining the position
FT                   of the catalytic nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
SQ   SEQUENCE   360 AA;  40295 MW;  070B0EBCC0382383 CRC64;
     MLKKLAVCLS IVLLLLGAAS PISAHTVYPV NPNAQQTTKD IMNWLAHLPN RSENRVMSGA
     FGGYSDVTFS MTEENRLKNA TGQSPAIYGC DYGRGWLETA DITDTIDYCC NSSLISYWKS
     GGLPQVSLHL ANPAFPSGNY KTAISNSQYK NILDPSTVEG KRLEALLSKI ADGLTQLKNQ
     GVTVLFRPLH EMNGEWFWWG LTGYNQKDNE RISLYKELYK KIYRYMTETR GLDNLLWVYS
     PDANRDFKTD FYPGSSYVDI TGLDAYFTDP YAISGYDEML SLKKPFAFAE TGPSGNIGSF
     DYAAFINAIR QKYPQTTYFL TWDEQLSPAA NQGAQSLYQN SWTLNKGEIW NGGSLTPIAE