ID   MANB_BACSU              Reviewed;         362 AA.
AC   O05512; Q797D6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000303|PubMed:18177310};
DE            EC=3.2.1.78 {ECO:0000269|PubMed:19441796};
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase {ECO:0000303|PubMed:18177310};
DE   AltName: Full=Beta-mannanase {ECO:0000303|PubMed:18177310};
DE   AltName: Full=Glucomannan utilization protein G {ECO:0000303|PubMed:18177310};
DE   Flags: Precursor;
GN   Name=gmuG {ECO:0000303|PubMed:9202461};
GN   Synonyms=ydhT {ECO:0000303|PubMed:9202461};
GN   OrderedLocusNames=BSU05880;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA   Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA   Ogasawara N.;
RT   "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT   Bacillus subtilis chromosome.";
RL   Microbiology 143:1861-1866(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 153; 158 AND 160.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 27-37.
RC   STRAIN=168;
RX   PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA   Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT   "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT   dimensional protein electrophoretic study.";
RL   Microbiology 146:65-75(2000).
RN   [5]
RP   FUNCTION IN GLUCOMANNAN UTILIZATION, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA   Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT   "Glucomannan utilization operon of Bacillus subtilis.";
RL   FEMS Microbiol. Lett. 279:103-109(2008).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) OF 21-362, AND SUBUNIT.
RA   Bonanno J.B., Rutter M., Bain K.T., Iizuka M., Romero R., Smith D.,
RA   Wasserman S., Sauder J.M., Burley S.K., Almo S.C.;
RT   "Crystal structure of the YdhT protein from Bacillus subtilis.";
RL   Submitted (FEB-2008) to the PDB data bank.
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 27-362, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE SPECIFICITY.
RX   PubMed=19441796; DOI=10.1021/bi900515d;
RA   Tailford L.E., Ducros V.M., Flint J.E., Roberts S.M., Morland C.,
RA   Zechel D.L., Smith N., Bjornvad M.E., Borchert T.V., Wilson K.S.,
RA   Davies G.J., Gilbert H.J.;
RT   "Understanding how diverse beta-mannanases recognize heterogeneous
RT   substrates.";
RL   Biochemistry 48:7009-7018(2009).
CC   -!- FUNCTION: Involved in the degradation of glucomannan. Catalyzes the
CC       endo hydrolysis of beta-1,4-linked mannan, galactomannan and
CC       glucomannan. {ECO:0000269|PubMed:18177310,
CC       ECO:0000269|PubMed:19441796}.
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:0000269|PubMed:19441796};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.7 mg/ml for glucomannan {ECO:0000269|PubMed:19441796};
CC         KM=4.5 mg/ml for galactomannan {ECO:0000269|PubMed:19441796};
CC         Note=kcat is 330 min(-1) for mannanase activity with galactomannan as
CC         substrate. kcat is 350 min(-1) for mannanase activity with
CC         glucomannan as substrate. {ECO:0000269|PubMed:19441796};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.6}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10658653}.
CC   -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose and
CC       mannobiose, the possible degradation products of glucomannan. Repressed
CC       by glucose via the carbon catabolite repression system. Also repressed
CC       by GmuR. {ECO:0000269|PubMed:18177310}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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DR   EMBL; D88802; BAA19712.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12407.2; -; Genomic_DNA.
DR   PIR; H69785; H69785.
DR   RefSeq; NP_388469.2; NC_000964.3.
DR   RefSeq; WP_003244107.1; NZ_JNCM01000031.1.
DR   PDB; 2WHK; X-ray; 1.70 A; A=27-362.
DR   PDB; 3CBW; X-ray; 1.27 A; A/B=21-362.
DR   PDBsum; 2WHK; -.
DR   PDBsum; 3CBW; -.
DR   AlphaFoldDB; O05512; -.
DR   SMR; O05512; -.
DR   STRING; 224308.BSU05880; -.
DR   CAZy; GH26; Glycoside Hydrolase Family 26.
DR   PaxDb; 224308-BSU05880; -.
DR   DNASU; 938034; -.
DR   EnsemblBacteria; CAB12407; CAB12407; BSU_05880.
DR   GeneID; 938034; -.
DR   KEGG; bsu:BSU05880; -.
DR   PATRIC; fig|224308.179.peg.632; -.
DR   eggNOG; COG4124; Bacteria.
DR   InParanoid; O05512; -.
DR   OrthoDB; 185675at2; -.
DR   BioCyc; BSUB:BSU05880-MONOMER; -.
DR   BRENDA; 3.2.1.78; 658.
DR   EvolutionaryTrace; O05512; -.
DR   Proteomes; UP000001570; Chromosome.
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   Gene3D; 3.20.20.80; Glycosidases; 1.
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:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR   Pfam; PF02156; Glyco_hydro_26; 1.
DR   PIRSF; PIRSF018168; Mannan-1_4-beta-mannosidase; 1.
DR   PRINTS; PR00739; GLHYDRLASE26.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51764; GH26; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Carbohydrate metabolism; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:10658653"
FT   CHAIN           27..362
FT                   /note="Mannan endo-1,4-beta-mannosidase"
FT                   /id="PRO_0000360866"
FT   DOMAIN          38..349
FT                   /note="GH26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT   ACT_SITE        193
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   ACT_SITE        292
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         131
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   BINDING         324..325
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   SITE            192
FT                   /note="Plays an important role in maintaining the position
FT                   of the catalytic nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P49424"
FT   CONFLICT        153
FT                   /note="K -> N (in Ref. 1; BAA19712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158..160
FT                   /note="STV -> ATA (in Ref. 1; BAA19712)"
FT                   /evidence="ECO:0000305"
FT   HELIX           38..49
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           50..52
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          61..66
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           74..83
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          88..96
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           104..107
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           113..121
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          125..131
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          137..139
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           148..155
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           160..180
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          186..189
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           211..229
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          236..241
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   TURN            250..253
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   TURN            257..259
FT                   /evidence="ECO:0007829|PDB:2WHK"
FT   STRAND          261..270
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           272..274
FT                   /evidence="ECO:0007829|PDB:2WHK"
FT   HELIX           278..282
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          288..297
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           304..314
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          318..323
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           326..328
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           330..332
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   HELIX           336..341
FT                   /evidence="ECO:0007829|PDB:3CBW"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:3CBW"
SQ   SEQUENCE   362 AA;  40892 MW;  C7E1D527AA001B14 CRC64;
     MFKKHTISLL IIFLLASAVL AKPIEAHTVS PVNPNAQQTT KTVMNWLAHL PNRTENRVLS
     GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE TANIEDSIDV SCNGDLMSYW
     KNGGIPQISL HLANPAFQSG HFKTPITNDQ YKKILDSSTV EGKRLNAMLS KIADGLQELE
     NQGVPVLFRP LHEMNGEWFW WGLTSYNQKD NERISLYKQL YKKIYHYMTD TRGLDHLIWV
     YSPDANRDFK TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG
     SFDYSLFINA IKQKYPKTIY FLAWNDEWSA AVNKGASALY HDSWTLNKGE IWNGDSLTPI
     VE
//