MANB_BACSU
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 03-AUG-2022, entry version 119.
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}; OrderedLocusNames=BSU05880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; 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; O05512; -.
DR PRIDE; O05512; -.
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 OMA; HYISGQQ; -.
DR BioCyc; BSUB:BSU05880-MON; -.
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 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 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
