LAM55_STREK
ID LAM55_STREK Reviewed; 605 AA.
AC G2NFJ9;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Exo-beta-1,3-glucanase {ECO:0000303|PubMed:25752603};
DE EC=3.2.1.58 {ECO:0000269|PubMed:25752603};
DE AltName: Full=Glucan 1,3-beta-glucosidase {ECO:0000305|PubMed:25752603};
DE AltName: Full=Laminarinase {ECO:0000303|PubMed:25752603};
DE AltName: Full=SacteLam55A {ECO:0000303|PubMed:25752603};
DE Flags: Precursor;
GN ORFNames=SACTE_4363 {ECO:0000312|EMBL:AEN12197.1};
OS Streptomyces sp. (strain SirexAA-E / ActE).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=862751;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SirexAA-E / ActE;
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA Adams S., Book A., Currie C., Woyke T.;
RT "Complete sequence of Streptomyces sp. SirexAA-E.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SirexAA-E / ActE;
RX PubMed=23301151; DOI=10.1038/srep01030;
RA Takasuka T.E., Book A.J., Lewin G.R., Currie C.R., Fox B.G.;
RT "Aerobic deconstruction of cellulosic biomass by an insect-associated
RT Streptomyces.";
RL Sci. Rep. 3:1030-1030(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 46-605 OF WILD-TYPE AND MUTANT
RP ALA-502 IN COMPLEXES WITH PRODUCT AND SUBSTRATES, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, MUTAGENESIS OF
RP GLN-174; SER-198; ASP-449; GLU-480; GLU-502 AND TYR-505, AND REACTION
RP MECHANISM.
RC STRAIN=SirexAA-E / ActE;
RX PubMed=25752603; DOI=10.1074/jbc.m114.623579;
RA Bianchetti C.M., Takasuka T.E., Deutsch S., Udell H.S., Yik E.J.,
RA Bergeman L.F., Fox B.G.;
RT "Active site and laminarin binding in glycoside hydrolase family 55.";
RL J. Biol. Chem. 290:11819-11832(2015).
CC -!- FUNCTION: Exo-beta-1,3-glucanase that specifically hydrolyzes laminarin
CC and laminarioligosaccharides, producing glucose and laminaribiose as
CC end products. {ECO:0000269|PubMed:25752603}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58; Evidence={ECO:0000269|PubMed:25752603};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.93 mg/ml for L.digitata soluble laminarin (at pH 6 and 40
CC degrees Celsius) {ECO:0000269|PubMed:25752603};
CC Vmax=128 umol/min/mg enzyme with L.digitata soluble laminarin as
CC substrate (at pH 6 and 40 degrees Celsius)
CC {ECO:0000269|PubMed:25752603};
CC Note=kcat is 138 sec(-1) with L.digitata soluble laminarin as
CC substrate (at pH 6 and 40 degrees Celsius).
CC {ECO:0000269|PubMed:25752603};
CC pH dependence:
CC Optimum pH is 6. Maintains 70% or more of the maximal activity from
CC pH 6.0 to 9.0. {ECO:0000269|PubMed:25752603};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Maintains 70% or more of
CC the maximal activity from 35 to 65 degrees Celsius.
CC {ECO:0000269|PubMed:25752603};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23301151}.
CC -!- INDUCTION: Is up-regulated during growth on biomass, i.e. when the
CC bacterium is grown on cellobiose, xylan, and various pretreated
CC switchgrass samples. {ECO:0000269|PubMed:23301151}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 55 family. {ECO:0000305}.
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DR EMBL; CP002993; AEN12197.1; -; Genomic_DNA.
DR RefSeq; WP_014048156.1; NC_015953.1.
DR PDB; 4PEW; X-ray; 1.51 A; A/B=46-605.
DR PDB; 4PEX; X-ray; 1.75 A; A/B=46-605.
DR PDB; 4PEY; X-ray; 1.50 A; A=46-605.
DR PDB; 4PEZ; X-ray; 1.90 A; A=46-605.
DR PDB; 4PF0; X-ray; 1.75 A; A/B=46-605.
DR PDB; 4TYV; X-ray; 1.75 A; A/B=55-605.
DR PDB; 4TZ1; X-ray; 1.50 A; A=57-605.
DR PDB; 4TZ3; X-ray; 1.90 A; A=57-605.
DR PDB; 4TZ5; X-ray; 1.75 A; A/B=57-605.
DR PDBsum; 4PEW; -.
DR PDBsum; 4PEX; -.
DR PDBsum; 4PEY; -.
DR PDBsum; 4PEZ; -.
DR PDBsum; 4PF0; -.
DR PDBsum; 4TYV; -.
DR PDBsum; 4TZ1; -.
DR PDBsum; 4TZ3; -.
DR PDBsum; 4TZ5; -.
DR AlphaFoldDB; G2NFJ9; -.
DR SMR; G2NFJ9; -.
DR STRING; 862751.SACTE_4363; -.
DR EnsemblBacteria; AEN12197; AEN12197; SACTE_4363.
DR KEGG; ssx:SACTE_4363; -.
DR PATRIC; fig|862751.12.peg.4534; -.
DR eggNOG; ENOG502Z7WW; Bacteria.
DR HOGENOM; CLU_013797_1_0_11; -.
DR OMA; VQHHGFA; -.
DR OrthoDB; 352760at2; -.
DR Proteomes; UP000001397; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IDA:UniProtKB.
DR GO; GO:0009251; P:glucan catabolic process; IDA:UniProtKB.
DR Gene3D; 2.160.20.10; -; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..605
FT /note="Exo-beta-1,3-glucanase"
FT /id="PRO_0000433464"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 502
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:25752603"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25752603"
FT BINDING 194..196
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25752603"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25752603"
FT BINDING 446..449
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25752603"
FT BINDING 480..481
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25752603"
FT BINDING 505
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 174
FT /note="Q->A: 1300-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 174
FT /note="Q->N: 280-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 198
FT /note="S->A: 13-fold decrease in catalytic efficiency while
FT nearly no effect on substrate affinity."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 449
FT /note="D->A: 1200-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 449
FT /note="D->N: 330-fold decrease in catalytic efficiency
FT while only 2-fold decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 480
FT /note="E->A,Q: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 502
FT /note="E->A,Q: Loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:25752603"
FT MUTAGEN 505
FT /note="Y->A: 150-fold decrease in catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:25752603"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4TYV"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 216..229
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:4TZ1"
FT STRAND 254..264
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 377..384
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 390..397
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 411..423
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 427..433
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:4PEY"
FT TURN 456..459
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 463..467
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 491..502
FT /evidence="ECO:0007829|PDB:4PEY"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 533..542
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 564..574
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 577..581
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:4PEY"
FT STRAND 599..604
FT /evidence="ECO:0007829|PDB:4PEY"
SQ SEQUENCE 605 AA; 64661 MW; C9800602EBFDEE26 CRC64;
MHVPPTDPAR SAPPASPHRR RRPKALGLTA LAAAMLMAVP TTQAAFGSDV RPAAAQEVVG
GGDLGPNVLV FDPSTPDIQG KVDEVFRKQE SNQFGTDRYA LMFKPGTYND INAQIGFYTS
IAGLGLNPDD TTFNGDVTVD AGWFDGNATQ NFWRSAENLA LNPVNGTNRW AVSQAAPFRR
MHVKGGLNLA PDGYGWASGG YIADSKIDGE VGPYSQQQWY TRDSSVGGWG NGVWNMTFSG
VEGAPAQSFP EPPYTTLETT PVSREKPFLY LDGDDYKVFV PAKRTNARGT SWGNGTPEGE
SLPLDQFYVV KPGATAETIN AAVDQGLHLL FTPGVYHVDQ PIEIDRANTV ALGLGLATII
PDNGVTALKV GDVDGVKVAG LLVDAGPVNS ETLVEVGSDG ASGDHAANPT SLQDVFVRIG
GAGPGKATTS IVVNSNDTII DHTWVWRADH GEGVGWETNR ADYGVHVKGD NVLATGLFVE
HFNKYDVQWS GENGKTIFYQ NEKAYDAPDQ AAIQNGDIKG YAAYKVDDSV TTHEGWGMGS
YCYFNVNPDI RQQHGFQAPV KPGVKFHDLL VVSLGGKGQY EHVINDIGDP TSGDTTIPSQ
VVSFP
