ID   MAN5_CELJU              Reviewed;         430 AA.
AC   B3PF24;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000303|PubMed:19441796};
DE            EC=3.2.1.78 {ECO:0000269|PubMed:19441796};
DE   AltName: Full=Mannanase 5A {ECO:0000303|PubMed:19441796};
DE            Short=Man5A {ECO:0000303|PubMed:19441796};
DE   AltName: Full=Mannanase A {ECO:0000303|PubMed:19441796};
DE            Short=ManA {ECO:0000303|PubMed:19441796};
GN   Name=man5A {ECO:0000303|PubMed:19441796}; OrderedLocusNames=CJA_3338;
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107;
RX   PubMed=18556790; DOI=10.1128/jb.01701-07;
RA   DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP   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: Catalyzes the endo hydrolysis of beta-1,4-linked mannan,
CC       galactomannan and glucomannan. It is able to hydrolyze mannosidic
CC       linkages that are flanked by mannose or glucose.
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=6.2 mg/ml for glucomannan {ECO:0000269|PubMed:19441796};
CC         KM=8.5 mg/ml for galactomannan {ECO:0000269|PubMed:19441796};
CC         Note=kcat is 140000 min(-1) for mannanase activity with galactomannan
CC         as substrate. kcat is 62000 min(-1) for mannanase activity with
CC         glucomannan as substrate. {ECO:0000269|PubMed:19441796};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; CP000934; ACE84673.1; -; Genomic_DNA.
DR   RefSeq; WP_012488914.1; NC_010995.1.
DR   AlphaFoldDB; B3PF24; -.
DR   SMR; B3PF24; -.
DR   STRING; 498211.CJA_3338; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EnsemblBacteria; ACE84673; ACE84673; CJA_3338.
DR   KEGG; cja:CJA_3338; -.
DR   eggNOG; COG2730; Bacteria.
DR   HOGENOM; CLU_018488_1_1_6; -.
DR   OMA; GTAPNGY; -.
DR   OrthoDB; 1395441at2; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.30.32.30; -; 2.
DR   InterPro; IPR002883; CBM10/Dockerin_dom.
DR   InterPro; IPR036601; CBM10_sf.
DR   InterPro; IPR009031; CBM_fam10.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF02013; CBM_10; 2.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01064; CBM_10; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57615; SSF57615; 1.
DR   PROSITE; PS51763; CBM10; 2.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Reference proteome; Repeat.
FT   CHAIN           1..430
FT                   /note="Mannan endo-1,4-beta-mannosidase"
FT                   /id="PRO_0000433975"
FT   DOMAIN          357..390
FT                   /note="CBM10 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   DOMAIN          395..424
FT                   /note="CBM10 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
FT   ACT_SITE        173
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P22533"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P22533"
SQ   SEQUENCE   430 AA;  46325 MW;  AEA56FEB0A9B073F CRC64;
     MSLFTPLSET NVRSHTNTSS VFCRRIKTLV AGLTALGLML AAVSASAGFY VSGKQLREGN
     GNNFIMRGVN LPHAWFPDRT NQALADISAT GANSVRVVLS NGRLWSRTPE SQVASIISQA
     KARQLITVLE VHDTTGYGEQ TAATLSEAVD YWIAIRNALI GQEDYVIINI GNEPFGNGQS
     ASTWLNLHRD AINRLRNAGF THTLMVDAAN WGQDWENIMR NNASSLFNSD PRRNVIFSVH
     MYEVYPNDTA VNNYMSAFNS MNLPLVVGEF AANHFGSYVD AGSIMARAQQ YGFGYLGWSW
     SGNSSNLSAL DVVTNFNAGS LTTWGNLLIN NTNGIRNTSR KATIFGGSGS SSSSAGSCGT
     APNGYPYCCN ASSATGNGWG WENNRSCVVA TTSTSCNWYG TSYPICVNTS SGWGWENNRS
     CIAASTCAAQ