ID Q9ZF13_THEFU PRELIMINARY; PRT; 279 AA. AC Q9ZF13; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Beta-mannanase (EC 3.2.1.78) (Fragment). GN Name=man; OS Thermomonospora fusca. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Streptosporangineae; Nocardiopsaceae; Thermobifida. OX NCBI_TaxID=2021; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KW3; RA Hilge M., Gloor S., Winterhalter K., Piontek K.; RT "Crystallization and preliminary crystallographic analysis of two RT beta-mannanase isoforms from Thermomonospora fusca KW3."; RL Acta Crystallogr. 52:1224-1225(1996). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=KW3; RX MEDLINE=99036862; 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 RT glycosyl hydrolase - substrate specificity in glycosyl hydrolase RT family 5."; RL Structure 6:1433-1444(1998). DR EMBL; AJ006227; CAA06924.1; -. DR PDB; 1BQC; X-ray; A=1-279. DR PDB; 2MAN; X-ray; A=1-279. DR PDB; 3MAN; X-ray; A=1-279. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl ...; IEA. DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA. DR GO; GO:0005975; P:carbohydrate metabolism; IEA. DR InterPro; IPR001547; Glyco_hydro_5. DR Pfam; PF00150; Cellulase; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; UNKNOWN_1. KW Glycosidase; Hydrolase. FT NON_TER 1 1 FT NON_TER 279 279 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 //