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   27-MAR-2024, entry version 124.
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; Bacillota; Clostridia; Caldicellulosiruptorales;
OC   Caldicellulosiruptoraceae; 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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.710; Endoglucanase-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 2.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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   PANTHER; PTHR34142:SF1; CELLULASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
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; SSF51445; (Trans)glycosidases; 2.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 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
//