LCHMO_ENTFA
ID LCHMO_ENTFA Reviewed; 194 AA.
AC Q838S1;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Lytic chitin monooxygenase {ECO:0000305|PubMed:22210154};
DE EC=1.14.99.53 {ECO:0000269|PubMed:22210154};
DE AltName: Full=EfCBM33A {ECO:0000303|PubMed:22210154};
DE AltName: Full=Lytic polysaccharide monooxygenase {ECO:0000303|PubMed:24828494};
DE Short=LPMO {ECO:0000303|PubMed:24828494};
DE Flags: Precursor;
GN OrderedLocusNames=EF_0362 {ECO:0000312|EMBL:AAO80225.1};
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2] {ECO:0007744|PDB:4A02}
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF 29-194, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=22210154; DOI=10.1016/j.jmb.2011.12.033;
RA Vaaje-Kolstad G., Bohle L.A., Gaseidnes S., Dalhus B., Bjoras M.,
RA Mathiesen G., Eijsink V.G.;
RT "Characterization of the chitinolytic machinery of Enterococcus faecalis
RT V583 and high-resolution structure of its oxidative CBM33 enzyme.";
RL J. Mol. Biol. 416:239-254(2012).
RN [3] {ECO:0007744|PDB:4ALC, ECO:0007744|PDB:4ALE, ECO:0007744|PDB:4ALQ}
RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 29-194 IN COMPLEX WITH COPPER,
RP AND COFACTOR.
RC STRAIN=ATCC 700802 / V583;
RX PubMed=24828494; DOI=10.1074/jbc.m114.563494;
RA Gudmundsson M., Kim S., Wu M., Ishida T., Momeni M.H., Vaaje-Kolstad G.,
RA Lundberg D., Royant A., Stahlberg J., Eijsink V.G., Beckham G.T.,
RA Sandgren M.;
RT "Structural and electronic snapshots during the transition from a Cu(II) to
RT Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray
RT photoreduction.";
RL J. Biol. Chem. 289:18782-18792(2014).
CC -!- FUNCTION: Involved in chitin degradation. Catalyzes the oxidative
CC cleavage of glycosidic bonds in both alpha- and beta-chitin via a
CC copper-dependent mechanism, leading to oxidized chitooligosaccharides
CC with a dominance of even-numbered products. Acts synergistically with
CC the chitinase EfChi18A, and combining the two enzymes leads to rapid
CC and complete depolymerization of crystalline chitin, especially with
CC beta-chitin as a substrate. Is likely involved in a chitin degradation
CC pathway that allows E.faecalis V583 to grow on chitin as a carbon
CC source. {ECO:0000269|PubMed:22210154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl]n+m + reduced acceptor +
CC O2 = [(1->4)-N-acetyl-beta-D-glucosaminyl]m-1-(1->4)-2-(acetylamino)-
CC 2-deoxy-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-
CC glucosaminyl]n + acceptor + H2O.; EC=1.14.99.53;
CC Evidence={ECO:0000269|PubMed:22210154};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:22210154, ECO:0000269|PubMed:24828494};
CC Note=The copper metal center seems to be reduced from a Cu(II) to Cu(I)
CC oxidation state prior to binding of dioxygen for catalysis.
CC {ECO:0000269|PubMed:24828494};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:22210154}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22210154}.
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DR EMBL; AE016830; AAO80225.1; -; Genomic_DNA.
DR RefSeq; NP_814154.1; NC_004668.1.
DR RefSeq; WP_002355225.1; NZ_KE136524.1.
DR PDB; 4A02; X-ray; 0.95 A; A=29-194.
DR PDB; 4ALC; X-ray; 1.49 A; A=29-194.
DR PDB; 4ALE; X-ray; 1.48 A; A=29-194.
DR PDB; 4ALQ; X-ray; 1.48 A; A=29-194.
DR PDB; 4ALR; X-ray; 1.49 A; A=29-194.
DR PDB; 4ALS; X-ray; 1.47 A; A=29-194.
DR PDB; 4ALT; X-ray; 1.49 A; A=29-194.
DR PDBsum; 4A02; -.
DR PDBsum; 4ALC; -.
DR PDBsum; 4ALE; -.
DR PDBsum; 4ALQ; -.
DR PDBsum; 4ALR; -.
DR PDBsum; 4ALS; -.
DR PDBsum; 4ALT; -.
DR AlphaFoldDB; Q838S1; -.
DR SMR; Q838S1; -.
DR STRING; 226185.EF_0362; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR EnsemblBacteria; AAO80225; AAO80225; EF_0362.
DR GeneID; 60892816; -.
DR KEGG; efa:EF0362; -.
DR PATRIC; fig|226185.45.peg.2967; -.
DR eggNOG; COG3397; Bacteria.
DR HOGENOM; CLU_047929_2_0_9; -.
DR OMA; STWDYYI; -.
DR BRENDA; 1.14.99.53; 2095.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR004302; Cellulose/chitin-bd_N.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF03067; LPMO_10; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW Copper; Metal-binding; Oxidoreductase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..194
FT /note="Lytic chitin monooxygenase"
FT /id="PRO_5004299127"
FT DOMAIN 29..191
FT /note="Chitin-binding type-4"
FT /evidence="ECO:0000255"
FT BINDING 29
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:24828494,
FT ECO:0007744|PDB:4ALE, ECO:0007744|PDB:4ALR,
FT ECO:0007744|PDB:4ALS, ECO:0007744|PDB:4ALT"
FT BINDING 114
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:24828494,
FT ECO:0007744|PDB:4ALE, ECO:0007744|PDB:4ALR,
FT ECO:0007744|PDB:4ALS, ECO:0007744|PDB:4ALT"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4A02"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:4A02"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4A02"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:4A02"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:4ALE"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4A02"
FT TURN 75..79
FT /evidence="ECO:0007829|PDB:4A02"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:4A02"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:4ALS"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:4A02"
FT STRAND 101..112
FT /evidence="ECO:0007829|PDB:4A02"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:4A02"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:4A02"
FT STRAND 139..150
FT /evidence="ECO:0007829|PDB:4A02"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:4A02"
FT STRAND 168..193
FT /evidence="ECO:0007829|PDB:4A02"
SQ SEQUENCE 194 AA; 21138 MW; 2E67D54AFF3F3C40 CRC64;
MKKSLLTIVL AFSFVLGGAA LAPTVSEAHG YVASPGSRAF FGSSAGGNLN TNVGRAQWEP
QSIEAPKNTF ITGKLASAGV SGFEPLDEQT ATRWHKTNIT TGPLDITWNL TAQHRTASWD
YYITKNGWNP NQPLDIKNFD KIASIDGKQE VPNKVVKQTI NIPTDRKGYH VIYAVWGIGD
TVNAFYQAID VNIQ
