ID   MANB_CALM0              Reviewed;         513 AA.
AC   P16699;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase A and B {ECO:0000303|PubMed:2694961};
DE            EC=3.2.1.78 {ECO:0000250|UniProtKB:O05512};
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase {ECO:0000303|PubMed:2694961};
DE   AltName: Full=Beta-mannanase {ECO:0000303|PubMed:2694961};
DE   AltName: Full=Endo-1,4-mannanase {ECO:0000303|PubMed:2694961};
DE   Contains:
DE     RecName: Full=Mannan endo-1,4-beta-mannosidase A;
DE   Contains:
DE     RecName: Full=Mannan endo-1,4-beta-mannosidase B;
DE   Flags: Precursor;
OS   Caldalkalibacillus mannanilyticus (strain DSM 16130 / CIP 109019 / JCM
OS   10596 / AM-001) (Bacillus mannanilyticus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX   NCBI_TaxID=1236954;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2694961; DOI=10.1128/aem.55.12.3178-3183.1989;
RA   Akino T., Kato C., Horikoshi K.;
RT   "Two Bacillus beta-mannanases having different COOH termini are produced in
RT   Escherichia coli carrying pMAH5.";
RL   Appl. Environ. Microbiol. 55:3178-3183(1989).
CC   -!- FUNCTION: Could be involved in the degradation of glucomannan and
CC       catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan
CC       and 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:2694961}.
CC   -!- MISCELLANEOUS: The production of the two beta-mannanases seems not to
CC       be caused by proteolytic cleavage. {ECO:0000305|PubMed:2694961}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR   EMBL; M31797; AAA22586.1; -; Genomic_DNA.
DR   PIR; A37219; A37219.
DR   AlphaFoldDB; P16699; -.
DR   SMR; P16699; -.
DR   CAZy; CBM59; Carbohydrate-Binding Module Family 59.
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; 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; PF02156; Glyco_hydro_26; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:2694961"
FT   CHAIN           27..513
FT                   /note="Mannan endo-1,4-beta-mannosidase A"
FT                   /id="PRO_0000012169"
FT   CHAIN           27..365
FT                   /note="Mannan endo-1,4-beta-mannosidase B"
FT                   /id="PRO_0000012170"
FT   DOMAIN          41..353
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        195
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   ACT_SITE        295
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         429..430
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   SITE            194
FT                   /note="Plays an important role in maintaining the position
FT                   of the catalytic nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
SQ   SEQUENCE   513 AA;  58430 MW;  88D105F622CDB5A8 CRC64;
     MKVYKKVAFV MAFIMFFSVL PTISMSSEAN GAALSNPNAN QTTKNVYSWL ANLPNKSNKR
     VVSGHFGGYS DSTLAWIKQC ARELTGKMPG ILSCDYKNWQ TRLYVADQIS YGCNQELINF
     WNQGGLVTIS VHMPNPGFHS GENYKTILPT SQFQNLTNHR TTEGRRWKDM LDKMADGLDE
     LQNNGVTVLF RPLHEMNGEW FWWGAEGYNQ FDQTRANAYI SAWRDMYQYF THERKLNNLI
     WVYSPDVYRD HVTSYYPGAN YVDIVALDSY HPDPHSLTDQ YNRMIALDKP FAFAEIGPPE
     SMAGSFDYSN YIQAIKQKYP RTVYFLAWND KWSPHNNRGA WDLFNDSWVV NRGEIDYGQS
     NPATVLYDFE NNTLSWSGCE FTDGGPWTSN EWSANGTQSL KADVVLGNNS YHLQKTVNRN
     LSSFKNLEIK VSHSSWGNVG SGMTARVFVK TGSAWRWNAG EFCQFAGKRT TALSIDLTKV
     SNLHDVREIG VEYKAPANSN GKTAIYLDHV TVR