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Mannan endo-1,4-beta-mannosidase (EC 3.2.1.78)

 D0UZJ9_BACIU            Unreviewed;       362 AA.
D0UZJ9;
15-DEC-2009, integrated into UniProtKB/TrEMBL.
15-DEC-2009, sequence version 1.
31-JAN-2018, entry version 32.
RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000256|PIRNR:PIRNR018168};
EC=3.2.1.78 {ECO:0000256|PIRNR:PIRNR018168};
Bacillus subtilis.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=1423 {ECO:0000313|EMBL:ACY00389.1};
[1] {ECO:0000313|EMBL:ACY00389.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BME0437 {ECO:0000313|EMBL:ACY00389.1};
Liu P.F., Chen S.L., Liu Z.D.;
"A novel bioassay for detection of N-acyl homoserine lactone (AHL) and
screening of AHL-degrading microorganisms.";
Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:ACY00389.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BME0437 {ECO:0000313|EMBL:ACY00389.1};
PubMed=22528649; DOI=10.1007/s12010-012-9653-4;
Liu P., Gao Y., Huang W., Shao Z., Shi J., Liu Z.;
"A novel bioassay for high-throughput screening microorganisms with N-
acyl homoserine lactone degrading activity.";
Appl. Biochem. Biotechnol. 167:73-80(2012).
-!- CATALYTIC ACTIVITY: Random hydrolysis of (1->4)-beta-D-mannosidic
linkages in mannans, galactomannans and glucomannans.
{ECO:0000256|PIRNR:PIRNR018168}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR018168}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
{ECO:0000256|PIRNR:PIRNR018168, ECO:0000256|PROSITE-
ProRule:PRU01100}.
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EMBL; GQ988368; ACY00389.1; -; Genomic_DNA.
ProteinModelPortal; D0UZJ9; -.
CAZy; GH26; Glycoside Hydrolase Family 26.
eggNOG; ENOG4105D3P; Bacteria.
eggNOG; COG4124; LUCA.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-UniRule.
GO; GO:0006080; P:substituted mannan metabolic process; IEA:UniProtKB-UniRule.
InterPro; IPR022790; GH26_dom.
InterPro; IPR000805; Glyco_hydro_26.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR016714; Mannan-1_4-b-mannosidase.
PANTHER; PTHR40079; PTHR40079; 1.
Pfam; PF02156; Glyco_hydro_26; 1.
PIRSF; PIRSF018168; Mannan-1_4-beta-mannosidase; 1.
PRINTS; PR00739; GLHYDRLASE26.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS51764; GH26; 1.
3: Inferred from homology;
Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR018168};
Glycosidase {ECO:0000256|PIRNR:PIRNR018168, ECO:0000256|PROSITE-
ProRule:PRU01100, ECO:0000313|EMBL:ACY00389.1};
Hydrolase {ECO:0000256|PIRNR:PIRNR018168, ECO:0000256|PROSITE-
ProRule:PRU01100, ECO:0000313|EMBL:ACY00389.1};
Secreted {ECO:0000256|PIRNR:PIRNR018168};
Signal {ECO:0000256|PIRNR:PIRNR018168}.
SIGNAL 1 26 {ECO:0000256|PIRNR:PIRNR018168}.
CHAIN 27 362 Mannan endo-1,4-beta-mannosidase.
{ECO:0000256|PIRNR:PIRNR018168}.
/FTId=PRO_5010756496.
DOMAIN 38 349 GH26. {ECO:0000259|PROSITE:PS51764}.
ACT_SITE 193 193 Proton donor. {ECO:0000256|PROSITE-
ProRule:PRU01100}.
ACT_SITE 292 292 Nucleophile. {ECO:0000256|PROSITE-
ProRule:PRU01100}.
SEQUENCE 362 AA; 40749 MW; 9A0EF01F5325F652 CRC64;
MLKKHTISLL IIFLLASAVL AKPIEAHTVA PVNPNAQQTT KAVMNWLAHL PNRTENRVLS
GAFGGYSHDT FSMAEADRIR SATGQSPAIY GCDYARGWLE TAKIEDSIDV SCNGDLISYW
KNGGIPQISL HLANPAFQSG HFKTPITNDQ YKKILDSSTA EGKRLNAMLS KIADGLQELE
NQGVPVLFRP LHEMNGEWFW WGLTSYNQKD NERISLYKQL YKKIYHYMTD ARGLDHLIWV
YSPDANRDFK TDFYPGASYV DIVGLDAYFQ DAYSINGYDQ LTALNKPFAF TEVGPQTANG
SFDYSLFINA IKQKYPKTIY FLAWNDEWSP AVNKGASALY HDSWTLNKGE IWSGDSLTPI
VE


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