ID A0A1L9T6P2_9EURO Unreviewed; 345 AA.
AC A0A1L9T6P2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ASPSYDRAFT_92988 {ECO:0000313|EMBL:OJJ54953.1};
OS Aspergillus sydowii CBS 593.65.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=1036612 {ECO:0000313|EMBL:OJJ54953.1, ECO:0000313|Proteomes:UP000184356};
RN [1] {ECO:0000313|Proteomes:UP000184356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 593.65 {ECO:0000313|Proteomes:UP000184356};
RX PubMed=28196534; DOI=10.1186/s13059-017-1151-0;
RA de Vries R.P., Riley R., Wiebenga A., Aguilar-Osorio G., Amillis S.,
RA Uchima C.A., Anderluh G., Asadollahi M., Askin M., Barry K., Battaglia E.,
RA Bayram O., Benocci T., Braus-Stromeyer S.A., Caldana C., Canovas D.,
RA Cerqueira G.C., Chen F., Chen W., Choi C., Clum A., Dos Santos R.A.,
RA Damasio A.R., Diallinas G., Emri T., Fekete E., Flipphi M., Freyberg S.,
RA Gallo A., Gournas C., Habgood R., Hainaut M., Harispe M.L., Henrissat B.,
RA Hilden K.S., Hope R., Hossain A., Karabika E., Karaffa L., Karanyi Z.,
RA Krasevec N., Kuo A., Kusch H., LaButti K., Lagendijk E.L., Lapidus A.,
RA Levasseur A., Lindquist E., Lipzen A., Logrieco A.F., MacCabe A.,
RA Maekelae M.R., Malavazi I., Melin P., Meyer V., Mielnichuk N., Miskei M.,
RA Molnar A.P., Mule G., Ngan C.Y., Orejas M., Orosz E., Ouedraogo J.P.,
RA Overkamp K.M., Park H.-S., Perrone G., Piumi F., Punt P.J., Ram A.F.,
RA Ramon A., Rauscher S., Record E., Riano-Pachon D.M., Robert V., Roehrig J.,
RA Ruller R., Salamov A., Salih N.S., Samson R.A., Sandor E., Sanguinetti M.,
RA Schuetze T., Sepcic K., Shelest E., Sherlock G., Sophianopoulou V.,
RA Squina F.M., Sun H., Susca A., Todd R.B., Tsang A., Unkles S.E.,
RA van de Wiele N., van Rossen-Uffink D., Oliveira J.V., Vesth T.C.,
RA Visser J., Yu J.-H., Zhou M., Andersen M.R., Archer D.B., Baker S.E.,
RA Benoit I., Brakhage A.A., Braus G.H., Fischer R., Frisvad J.C.,
RA Goldman G.H., Houbraken J., Oakley B., Pocsi I., Scazzocchio C.,
RA Seiboth B., vanKuyk P.A., Wortman J., Dyer P.S., Grigoriev I.V.;
RT "Comparative genomics reveals high biological diversity and specific
RT adaptations in the industrially and medically important fungal genus
RT Aspergillus.";
RL Genome Biol. 18:RESEARCH28.1-RESEARCH28.45(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; KV878593; OJJ54953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9T6P2; -.
DR STRING; 1036612.A0A1L9T6P2; -.
DR VEuPathDB; FungiDB:ASPSYDRAFT_92988; -.
DR OrthoDB; 2282228at2759; -.
DR Proteomes; UP000184356; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR047763; PG_bind_dom_phiBT1-type.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR NCBIfam; NF038080; PG_bind_siph; 1.
DR PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000184356};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..345
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013313188"
FT DOMAIN 192..236
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 345 AA; 37380 MW; 14746475BD0FE80B CRC64;
MPPFHSIALL SLLPLVSPMF LVPRTSWNAT PPTEPYKPMP QPNLGTKIHY VGPVYTTRPH
AHCSAYMKSI QEDHLANPEQ GWMDIAYNLA VCEHGYVFDG RGAGHMSGAN GNSTLNENHY
AVLAFLGKVG LMEPTGEQVE GVKDAVAYLR RAGAGREIRG HRDGWNTECP GENLYKLVTG
GGLEPGKLWD GGEHVVKHGE TVECIAEEYN VPARYIVAVN GLKGVEDVKA GDVLEIPARG
VPIDPSLFPP EEGDGDGDGG ELNYEEFPGA DFFKSEPNSP IIKSMGERLV EIGCGKYSDG
PSTQWTDEDL ASYACWQEAL GYTGADADGW PGKVSWDQLQ VPAVE
//
