ID   D9J0D7_9THEO            Unreviewed;       330 AA.
AC   D9J0D7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Man5B {ECO:0000313|EMBL:AGA35556.1};
GN   Name=man5B {ECO:0000313|EMBL:AGA35556.1};
OS   Caldanaerobius polysaccharolyticus.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobius.
OX   NCBI_TaxID=44256 {ECO:0000313|EMBL:AGA35556.1};
RN   [1] {ECO:0000313|EMBL:AGA35556.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KMTHCJ {ECO:0000313|EMBL:AGA35556.1};
RX   PubMed=20562312; DOI=10.1128/JB.00257-10;
RA   Han Y., Dodd D., Hespen C.W., Ohene-Adjei S., Schroeder C.M., Mackie R.I.,
RA   Cann I.K.;
RT   "Comparative analyses of two thermophilic enzymes exhibiting both beta-1,4
RT   mannosidic and beta-1,4 glucosidic cleavage activities from Caldanaerobius
RT   polysaccharolyticus.";
RL   J. Bacteriol. 192:4111-4121(2010).
RN   [2] {ECO:0007829|PDB:3W0K}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RA   Oyama T., Schmitz G.E., Dodd D., Han Y., Burnett A., Nagasawa N.,
RA   Mackie R.I., Nakamura H., Morikawa K., Cann I.K.O.;
RT   "Crystal structure of a glycoside hydrolase.";
RL   Submitted (OCT-2012) to the PDB data bank.
RN   [3] {ECO:0000313|EMBL:AGA35556.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KMTHCJ {ECO:0000313|EMBL:AGA35556.1};
RX   PubMed=24278284;
RA   Oyama T., Schmitz G.E., Dodd D., Han Y., Burnett A., Nagasawa N.,
RA   Mackie R.I., Nakamura H., Morikawa K., Cann I.;
RT   "Mutational and Structural Analyses of Caldanaerobius polysaccharolyticus
RT   Man5B Reveal Novel Active Site Residues for Family 5 Glycoside
RT   Hydrolases.";
RL   PLoS ONE 8:E80448-E80448(2013).
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; KC180757; AGA35556.1; -; Genomic_DNA.
DR   PDB; 3W0K; X-ray; 1.60 A; A/B=1-330.
DR   PDBsum; 3W0K; -.
DR   AlphaFoldDB; D9J0D7; -.
DR   SMR; D9J0D7; -.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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; PTHR31297:SF41; ENDOGLUCANASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G01830)-RELATED; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3W0K};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153}.
FT   DOMAIN          4..293
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
SQ   SEQUENCE   330 AA;  39187 MW;  B9B21D9868C52B9D CRC64;
     MKKYGFNFQW MYVWEEGREP EPPDKKALDF LAETGFNFVR IPVDYRFWTR NFDYFNPDKK
     VFEYIDLYLR ECSARNIHMC LNLHRAPGYC INRNDIERDN LWLDKRAQDG FVYQWELFAK
     RYKGVSSKFL SFDLVNEPPN IGQYGLTREN HASLIIRTVE AIRKIDPDRE IVIDGLGGGN
     IAMPELAHLG VVHSGRGYQP MALTHYQASW WDGHKGLPEP YYPDLLWQGK VWNKDTLREY
     YKPWRDLQQK GVNVHIGEFG CFNKTSNDVA IRWFEDVLSL YKEFEWGYSL WNFKGPFGIV
     EHGRPGAKYE YYRGFKVDRE LLDLLVENRV
//