LCHMO_STRA7
ID LCHMO_STRA7 Reviewed; 172 AA.
AC A3KIM2;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Lytic chitin monooxygenase {ECO:0000305|PubMed:28366436};
DE EC=1.14.99.53 {ECO:0000269|PubMed:28366436};
DE AltName: Full=Lytic polysaccharide monooxygenase {ECO:0000303|PubMed:28366436};
DE Short=LPMO {ECO:0000303|PubMed:28366436};
DE AltName: Full=SamLPMO10B {ECO:0000303|PubMed:28366436};
DE Flags: Precursor;
GN ORFNames=SAM23877_0645 {ECO:0000312|EMBL:AKZ53694.1},
GN SAML0570 {ECO:0000312|EMBL:CAJ89556.1};
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 [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, AND PATHWAY.
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 chitin degradation. Catalyzes the oxidative
CC cleavage of glycosidic bonds in chitin via a copper-dependent
CC mechanism, leading to oxidized chitooligomers with degrees of
CC polymerization of 4-6. Is not active on cellulose.
CC {ECO:0000269|PubMed:28366436}.
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:28366436};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000305|PubMed:28366436};
CC -!- PATHWAY: Glycan degradation; chitin degradation.
CC {ECO:0000269|PubMed:28366436}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:28366436}.
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DR EMBL; CP012382; AKZ53694.1; -; Genomic_DNA.
DR EMBL; AM238663; CAJ89556.1; -; Genomic_DNA.
DR RefSeq; WP_053126548.1; NZ_CP012382.1.
DR AlphaFoldDB; A3KIM2; -.
DR SMR; A3KIM2; -.
DR STRING; 1889.SAM40697_0535; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR EnsemblBacteria; AKZ53694; AKZ53694; SAM23877_0645.
DR KEGG; samb:SAM23877_0645; -.
DR OMA; STWDYYI; -.
DR OrthoDB; 1005693at2; -.
DR UniPathway; UPA00349; -.
DR Proteomes; UP000061018; 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; ISS: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 Carbohydrate metabolism; Chitin degradation; Chitin-binding; Copper;
KW Metal-binding; Oxidoreductase; Polysaccharide degradation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..172
FT /note="Lytic chitin monooxygenase"
FT /id="PRO_5011202451"
FT DOMAIN 31..168
FT /note="Chitin-binding type-4"
FT /evidence="ECO:0000255"
FT BINDING 31
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q838S1"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:Q838S1"
SQ SEQUENCE 172 AA; 17827 MW; 8148AA24C5BC9D6C CRC64;
MHAGRKTAVL IGAALAPVIA VSLPAASASA HGYISNPPSR QAQCAAGTVS CGDITYEPQS
VEGPKGLTSC SGGNSRFAEL DDDSKGWAVT PVPRNATFSW KLTAQHSTST WEYYVGGQRI
ALFDDGGAKP GAVVDHQVDF GGLDGRQKVL AVWNVADTDN AFYACIDVNV GG
