MANB_CALSA
ID MANB_CALSA Reviewed; 1331 AA.
AC P22533;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-mannanase/endoglucanase A;
DE Includes:
DE RecName: Full=Mannan endo-1,4-beta-mannosidase A;
DE EC=3.2.1.78;
DE AltName: Full=Beta-mannanase;
DE AltName: Full=Endo-1,4-mannanase;
DE Includes:
DE RecName: Full=Endo-1,4-beta-glucanase;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase;
DE Flags: Precursor;
GN Name=manA;
OS Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX NCBI_TaxID=44001;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1476429; DOI=10.1128/aem.58.12.3864-3867.1992;
RA Gibbs M.D., Saul D.J., Luthi E., Bergquist P.L.;
RT "The beta-mannanase from 'Caldocellum saccharolyticum' is part of a
RT multidomain enzyme.";
RL Appl. Environ. Microbiol. 58:3864-3867(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.
RX PubMed=2039230; DOI=10.1128/aem.57.3.694-700.1991;
RA Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L.;
RT "Cloning, sequence analysis, and expression in Escherichia coli of a gene
RT coding for a beta-mannanase from the extremely thermophilic bacterium
RT 'Caldocellum saccharolyticum'.";
RL Appl. Environ. Microbiol. 57:694-700(1991).
CC -!- FUNCTION: Degradation of hemicelluloses, the second most abundant
CC polysaccharides in nature. Contains two catalytic domains with
CC mannanase and endoglucanase activities.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.;
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.;
CC -!- SIMILARITY: In the N-terminal section; belongs to the glycosyl
CC hydrolase 5 (cellulase A) family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 44 (cellulase J) family. {ECO:0000305}.
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DR EMBL; L01257; AAA71887.1; -; Unassigned_DNA.
DR EMBL; M36063; AAA72861.1; -; Genomic_DNA.
DR PIR; A48954; A48954.
DR AlphaFoldDB; P22533; -.
DR SMR; P22533; -.
DR CAZy; CBM3; Carbohydrate-Binding Module Family 3.
DR CAZy; GH44; Glycoside Hydrolase Family 44.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR BRENDA; 3.2.1.78; 1055.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
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:1901136; P:carbohydrate derivative catabolic process; IEA:UniProt.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProt.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 2.60.40.710; -; 2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR024745; Glyco_hydro_44.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR018087; Glyco_hydro_5_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00942; CBM_3; 2.
DR Pfam; PF00150; Cellulase; 1.
DR Pfam; PF12891; Glyco_hydro_44; 1.
DR SMART; SM01067; CBM_3; 2.
DR SUPFAM; SSF49384; SSF49384; 2.
DR SUPFAM; SSF51445; SSF51445; 2.
DR PROSITE; PS51172; CBM3; 2.
DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW Multifunctional enzyme; Polysaccharide degradation; Repeat; Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..1331
FT /note="Beta-mannanase/endoglucanase A"
FT /id="PRO_0000007899"
FT DOMAIN 363..516
FT /note="CBM3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT DOMAIN 566..719
FT /note="CBM3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00513"
FT REGION 42..325
FT /note="Catalytic (mannanase)"
FT REGION 319..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..1331
FT /note="Catalytic (endoglucanase)"
FT COMPBIAS 332..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 162
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 257
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 338
FT /note="T -> P (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 340..346
FT /note="TPTPTPT -> RQHQHRQ (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1331 AA; 146893 MW; FFBCA51BB8D8F0E0 CRC64;
MRLKTKIRKK WLSVLCTVVF LLNILFIANV TILPKVGAAT SNDGVVKIDT STLIGTNHAH
CWYRDRLDTA LRGIRSWGMN SVRVVLSNGY RWTKIPASEV ANIISLSRSL GFKAIILEVH
DTTGYGEDGA ACSLAQAVEY WKEIKSVLDG NEDFVIINIG NEPYGNNNYQ NWVNDTKNAI
KALRDAGFKH TIMVDAPNWG QDWSNTMRDN AQSIMEADPL RNLVFSIHMY GVYNTASKVE
EYIKSFVDKG LPLVIGEFGH QHTDGDPDEE AIVRYAKQYK IGLFSWSWCG NSSYVGYLDM
VNNWDPNNPT PWGQWYKTNA IGTSSTPTPT STVTPTPTPT PTPTPTVTAT PTPTPTPVST
PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV DGERAQSAIS
DWAQIGASNV TFKFVKLSSS VSGADYYLEI GFKSGAGQLQ PGKDTGEIQM RFNKDDWSNY
NQGNDWSWIQ SMTSYGENEK VTAYIDGVLV WGQEPSGATP APAPTATPTP TPTVTPTPTV
TPTPTVTATP TPTPTPTPTP VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI
DLSRVTIRYW YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG
QLQPGKDTGE IQIRFNKSDW SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG VLVWGQEPSG
TTPSPTSTPT VTVTPTPTPT PTPTPTPTVT PTPTVTPTPT VTATPTPTPT PIPTVTPLPT
ISPSPSVVEI TINTNAGRTQ ISPYIYGANQ DIEGVVHSAR RLGGNRLTGY NWENNFSNAG
NDWYHSSDDY LCWSMGISGE DAKVPAAVVS KFHEYSLKNN AYSAVTLQMA GYVSKDNYGT
VSENETAPSN RWAEVKFKKD APLSLNPDLN DNFVYMDEFI NYLINKYGMA SSPTGIKGYI
LDNEPDLWAS THPRIHPNKV TCKELIEKSV ELAKVIKTLD PSAEVFGYAS YGFMGYYSLQ
DAPDWNQVKG EHRWFISWYL EQMKKASDSF GKRLLDVLDL HWYPEARGGN IRVCFDGEND
TSKEVVIARM QAPRTLWDPT YKTSVKGQIT AGENSWINQW FSDYLPIIPN VKADIEKYYP
GTKLAISEFD YGGRNHISGG IALADVLGIF GKYGVNFAAR WGDSGSYAAA AYNIYLNYDG
KGSKYGNTNV SANTSDVENM PVYASINGQD DSELHIILIN RNYDQKLQVK INITSTPKYT
KAEIYGFDSN SPEYKKMGNI DNIESNVFTL EVPKFNGVSH SITLDFNVSI KIIQNEVIKF
IRNLVFMRAL V
