LCEMO_STRA7
ID LCEMO_STRA7 Reviewed; 364 AA.
AC A3KKC4;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Lytic cellulose monooxygenase {ECO:0000305|PubMed:28366436};
DE EC=1.14.99.54 {ECO:0000269|PubMed:28366436};
DE AltName: Full=Lytic polysaccharide monooxygenase {ECO:0000303|PubMed:28366436};
DE Short=LPMO {ECO:0000303|PubMed:28366436};
DE AltName: Full=SamLPMO10C {ECO:0000303|PubMed:28366436};
DE Flags: Precursor;
GN ORFNames=SAM23877_1271 {ECO:0000312|EMBL:AKZ54320.1},
GN SAML1174 {ECO:0000312|EMBL:CAJ90160.1};
OS Streptomyces ambofaciens (strain ATCC 23877 / 3486 / DSM 40053 / JCM 4204 /
OS NBRC 12836 / NRRL B-2516).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=278992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516;
RX PubMed=16956972; DOI=10.1093/molbev/msl108;
RA Choulet F., Aigle B., Gallois A., Mangenot S., Gerbaud C., Truong C.,
RA Francou F.-X., Fourrier C., Guerineau M., Decaris B., Barbe V.,
RA Pernodet J.-L., Leblond P.;
RT "Evolution of the terminal regions of the Streptomyces linear chromosome.";
RL Mol. Biol. Evol. 23:2361-2369(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516;
RX PubMed=26410452; DOI=10.1016/j.jbiotec.2015.09.020;
RA Thibessard A., Haas D., Gerbaud C., Aigle B., Lautru S., Pernodet J.L.,
RA Leblond P.;
RT "Complete genome sequence of Streptomyces ambofaciens ATCC 23877, the
RT spiramycin producer.";
RL J. Biotechnol. 214:117-118(2015).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, PATHWAY, AND
RP BIOTECHNOLOGY.
RX PubMed=28366436; DOI=10.1016/j.carres.2017.02.004;
RA Valenzuela S.V., Ferreres G., Margalef G., Pastor F.I.J.;
RT "Fast purification method of functional LPMOs from Streptomyces ambofaciens
RT by affinity adsorption.";
RL Carbohydr. Res. 448:205-211(2017).
CC -!- FUNCTION: Involved in the degradation of lignocellulosic biomass.
CC Catalyzes the oxidative cleavage of glycosidic bonds in cellulosic
CC substrates via a copper-dependent mechanism. Degrades phosphoric acid
CC swollen cellulose (PASC) to oxidized cellooligosaccharides with degrees
CC of polymerization of 4-8. Also shows activity on agricultural fiber
CC paper pulps such as flax pulp. Is not active on chitin.
CC {ECO:0000269|PubMed:28366436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-beta-D-glucosyl]n+m + reduced acceptor + O2 = [(1->4)-
CC beta-D-glucosyl]m-1-(1->4)-D-glucono-1,5-lactone + [(1->4)-beta-D-
CC glucosyl]n + acceptor + H2O.; EC=1.14.99.54;
CC Evidence={ECO:0000269|PubMed:28366436};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000305|PubMed:28366436};
CC -!- PATHWAY: Glycan metabolism; cellulose degradation.
CC {ECO:0000269|PubMed:28366436}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28366436}.
CC -!- BIOTECHNOLOGY: The purification method developed for LPMOs can be a
CC cheap, simple and fast solution for the purification of these enzymes
CC for industrial applications. In addition, the activity of SamLPMO10C
CC shows the potential of LPMOs in lignocellulosic biomass valorization.
CC {ECO:0000305|PubMed:28366436}.
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DR EMBL; AM238663; CAJ90160.1; -; Genomic_DNA.
DR EMBL; CP012382; AKZ54320.1; -; Genomic_DNA.
DR RefSeq; WP_053127554.1; NZ_CP012382.1.
DR AlphaFoldDB; A3KKC4; -.
DR SMR; A3KKC4; -.
DR STRING; 1889.SAM40697_1112; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR EnsemblBacteria; AKZ54320; AKZ54320; SAM23877_1271.
DR KEGG; samb:SAM23877_1271; -.
DR OMA; DWPRTHL; -.
DR OrthoDB; 1005693at2; -.
DR UniPathway; UPA00696; -.
DR Proteomes; UP000061018; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030248; F:cellulose binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.290; -; 1.
DR InterPro; IPR001919; CBD2.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00553; CBM_2; 1.
DR Pfam; PF03067; LPMO_10; 1.
DR SMART; SM00637; CBD_II; 1.
DR SUPFAM; SSF49384; SSF49384; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51173; CBM2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Copper; Metal-binding;
KW Monooxygenase; Oxidoreductase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..364
FT /note="Lytic cellulose monooxygenase"
FT /id="PRO_5011202515"
FT DOMAIN 35..225
FT /note="Chitin-binding type-4"
FT /evidence="ECO:0000255"
FT DOMAIN 258..364
FT /note="CBM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01135"
FT REGION 234..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 35
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q838S1"
FT BINDING 144
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q838S1"
SQ SEQUENCE 364 AA; 38266 MW; 89031575F35239C4 CRC64;
MARRSRYISL AAVMATLLSA LGVTFLLGQG RAEAHGVAMM PGSRTYLCQL DAKTGTGALD
PTNPACRSAL DTSGATALYN WFAVLDSNAG GRGAGYVPDG TLCSAGNRSP YDFRGYNAAR
SDWPRTHLTS GSTIQVNYSN WAAHPGDFRV YLTKPGWSPT SELGWDDLEL IETVTDPPQR
GSAGADGGHY YWDLALPSGR SGDALIFMQW VRSDSQENFF SCSDVVFDGG NGEVTGIRGS
GGTPTPTPTP TTPPTTPPPT HSGSCMAVYN VENSWSGGFQ GSVEVMNHGT EPLNGWAVQW
KPGNGTTLGG VWNGSPTRGT DGTVKVRNVD HNRVVPPDGS VTFGFTATST GNDFPVGTIG
CVAP
