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 27-MAR-2024, entry version 73.
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; Pseudomonadota; 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 KEGG; cja:CJA_3338; -.
DR eggNOG; COG2730; Bacteria.
DR HOGENOM; CLU_018488_1_1_6; -.
DR OrthoDB; 220114at2; -.
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; CBM10; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
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 PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR Pfam; PF02013; CBM_10; 2.
DR Pfam; PF00150; Cellulase; 1.
DR SMART; SM01064; CBM_10; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57615; Type X cellulose binding domain, CBDX; 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
//
