ID   MANA_STRLI              Reviewed;         383 AA.
AC   P51529;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   28-JUN-2023, entry version 90.
DE   RecName: Full=Mannan endo-1,4-beta-mannosidase;
DE            EC=3.2.1.78;
DE   AltName: Full=1,4-beta-D-mannan mannanohydrolase;
DE   AltName: Full=Beta-mannanase;
DE   Flags: Precursor;
GN   Name=manA;
OS   Streptomyces lividans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 36-42.
RC   STRAIN=66 / 1326;
RX   PubMed=8457214; DOI=10.1042/bj2900857;
RA   Arcand N., Kluepfel D., Paradis F.W., Morosoli R., Shareck F.;
RT   "Beta-mannanase of Streptomyces lividans 66: cloning and DNA sequence of
RT   the manA gene and characterization of the enzyme.";
RL   Biochem. J. 290:857-863(1993).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Shareck F.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.8.;
CC       Temperature dependence:
CC         Optimum temperature is 58 degrees Celsius.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000305}.
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DR   EMBL; M92297; AAA26710.2; -; Genomic_DNA.
DR   PIR; S30386; S30386.
DR   AlphaFoldDB; P51529; -.
DR   SMR; P51529; -.
DR   CAZy; CBM10; Carbohydrate-Binding Module Family 10.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
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; 1.
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; PTHR42754:SF1; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42754; ENDOGLUCANASE; 1.
DR   Pfam; PF02013; CBM_10; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SMART; SM01064; CBM_10; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51763; CBM10; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:8457214"
FT   CHAIN           36..383
FT                   /note="Mannan endo-1,4-beta-mannosidase"
FT                   /id="PRO_0000007900"
FT   DOMAIN          339..377
FT                   /note="CBM10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01099"
SQ   SEQUENCE   383 AA;  39682 MW;  5DB4B407C64E94C3 CRC64;
     MRNARSTLIT TAGMAFAVLG LLFALAGPSA GRAEAAAGGI HVSNGRVVEG NGSAFVMRGV
     NHAYTWYPDR TGSIADIAAK GANTVRVVLS SGGRWTKTSA SEVSALIGQC KANKVICVLE
     VHDTTGYGKD GATSLDQAGD YWVGVKSAAW RAQEDYVVVN IGNEPFGNTN YAAWTDATKS
     AIGKLRGAGL GHALMVDAPN WGQDWSGTMR SNAASVFASD PDRNTVFSIH MYGVYDTAAE
     VRDYLNAFVG NGLPIVVGEF GDQHSDGNPD EDAIMATAQS LGVGYLGWSW SGNGGGVEYL
     DMVNGFDPNS LTSWGNRILY GSNGIAATSR TATVYGGGGG STGGTAPNGY PYCVNGGASD
     PDGDGWGWEN SRSCVVRGSA ADH
//