ID   Q9ZF13_THEFU            Unreviewed;       279 AA.
AC   Q9ZF13;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   28-JUN-2023, entry version 87.
DE   SubName: Full=Beta-mannanase {ECO:0000313|EMBL:CAA06924.1};
DE            EC=3.2.1.78 {ECO:0000313|EMBL:CAA06924.1};
DE   Flags: Fragment;
GN   Name=man {ECO:0000313|EMBL:CAA06924.1};
OS   Thermobifida fusca (Thermomonospora fusca).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=2021 {ECO:0000313|EMBL:CAA06924.1};
RN   [1] {ECO:0000313|EMBL:CAA06924.1, ECO:0007829|PDB:1BQC}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KW3 {ECO:0000313|EMBL:CAA06924.1};
RX   PubMed=9817845; DOI=10.1016/S0969-2126(98)00142-7;
RA   Hilge M., Gloor S.M., Rypniewski W., Sauer O., Heightman T.D.,
RA   Zimmermann W., Winterhalter K., Piontek K.;
RT   "High-resolution native and complex structures of thermostable beta-
RT   mannanase from Thermomonospora fusca - substrate specificity in glycosyl
RT   hydrolase family 5.";
RL   Structure 6:1433-1444(1998).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|RuleBase:RU361153}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ006227; CAA06924.1; -; Genomic_DNA.
DR   PDB; 1BQC; X-ray; 1.50 A; A=1-279.
DR   PDB; 2MAN; X-ray; 1.90 A; A=1-279.
DR   PDB; 3MAN; X-ray; 1.60 A; A=1-279.
DR   PDBsum; 1BQC; -.
DR   PDBsum; 2MAN; -.
DR   PDBsum; 3MAN; -.
DR   AlphaFoldDB; Q9ZF13; -.
DR   SMR; Q9ZF13; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   EvolutionaryTrace; Q9ZF13; -.
DR   GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR42754:SF1; BULB-TYPE LECTIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR42754; ENDOGLUCANASE; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1BQC, ECO:0007829|PDB:2MAN};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:CAA06924.1}.
FT   DOMAIN          11..257
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   ACT_SITE        126
FT                   /note="EMO_00062 proton shuttle (general acid/base)"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   ACT_SITE        223
FT                   /note="EMO_00050 covalent catalysis"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   SITE            48
FT                   /note="EMO_00158 modifies pKa"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   SITE            125
FT                   /note="EMO_00033 electrostatic stabiliser"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   SITE            194
FT                   /note="EMO_00158 modifies pKa"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   SITE            196
FT                   /note="EMO_00158 modifies pKa"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   SITE            252
FT                   /note="EMO_00038 activator,EMO_00033 electrostatic
FT                   stabiliser"
FT                   /evidence="ECO:0007829|PDB:1BQC"
FT   DISULFID        72..79
FT                   /evidence="ECO:0007829|PDB:1BQC, ECO:0007829|PDB:2MAN"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAA06924.1"
FT   NON_TER         279
FT                   /evidence="ECO:0000313|EMBL:CAA06924.1"
SQ   SEQUENCE   279 AA;  30657 MW;  98A2850FAE013DB0 CRC64;
     GLHVKNGRLY EANGQEFIIR GVSHPHNWYP QHTQAFADIK SHGANTVRVV LSNGVRWSKN
     GPSDVANVIS LCKQNRLICM LEVHDTTGYG EQSGASTLDQ AVDYWIELKS VLQGEEDYVL
     INIGNEPYGN DSATVAAGAW DTSAAIQRLR AAGFEHTLVV DAPNWGQDWT NTMRNNADQV
     YASDPTGNTV FSIHMYGVYS QASTITSYLE HFVNAGLPLI IGEFGHDHSD GNPDEDTIMA
     EAERLKLGYI GWSWSGNGGG VEYLDMVYNF DGDNLSPWG
//