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Database: UniProt
Entry: A0A0X1T5P1_PSEAA
LinkDB: A0A0X1T5P1_PSEAA
Original site: A0A0X1T5P1_PSEAA 
ID   A0A0X1T5P1_PSEAA        Unreviewed;       476 AA.
AC   A0A0X1T5P1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=AWM79_19640 {ECO:0000313|EMBL:AMB87388.1};
OS   Pseudomonas agarici.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB87388.1, ECO:0000313|Proteomes:UP000063229};
RN   [1] {ECO:0000313|EMBL:AMB87388.1, ECO:0000313|Proteomes:UP000063229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB87388.1,
RC   ECO:0000313|Proteomes:UP000063229};
RA   McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA   SanMiguel P., Csonka L.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP014135; AMB87388.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X1T5P1; -.
DR   STRING; 46677.AWM79_19640; -.
DR   OMA; KRYFAAN; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000063229; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd00118; LysM; 1.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000063229}.
SQ   SEQUENCE   476 AA;  50287 MW;  983E472E9A86512E CRC64;
     MMGFGMRIRA LVAVVGLVLT ALAVDAVAAT QVKSVRLWRA PDNTRLVFDL SGTVQHSVFT
     LTAPDRLVID INGATLASPL NVPTANTPIT SIRTAQRTPT DLRVVIDLKK VVTPKSFTLA
     PNAQYGNRLV VDLFDNPADA APPPAPTAAV ATVPAVPVRA TEPAIKLPPA PSGQRDIIVV
     IDAGHGGEDP GASGSRGQHE KDVVLSIARE LQRQVNGQKG YRAELTRTGD YFIPLRGRTE
     IARKKGADLF VSIHADAAPS AAAFGASVFA LSDRGATSET ARWLADSENR SDLIGGAGNV
     SLDDKDKMLA GVLLDLSMTA SLTSSLNVGQ KVLSNIGRVT PLHKPRVEQA GFMVLKSPDI
     PSILVETGFI SNSNEAAKLA SSNHQQALAR SISAGIRQFF QQNPPPGTYI AWLRDSGKIA
     QGPRDHRVAP GETLAMLAVR YQVSAATLRS ANNLSSDELK VGQNLTIPGT ELAAKQ
//
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