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Database: UniProt
Entry: A0A0M3AQ85_9SPHN
LinkDB: A0A0M3AQ85_9SPHN
Original site: A0A0M3AQ85_9SPHN 
ID   A0A0M3AQ85_9SPHN        Unreviewed;       322 AA.
AC   A0A0M3AQ85;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=YP76_10590 {ECO:0000313|EMBL:KKW92357.1};
OS   Sphingobium chungbukense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW92357.1, ECO:0000313|Proteomes:UP000033874};
RN   [1] {ECO:0000313|EMBL:KKW92357.1, ECO:0000313|Proteomes:UP000033874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ77 {ECO:0000313|EMBL:KKW92357.1,
RC   ECO:0000313|Proteomes:UP000033874};
RA   Kim Y.-C., Chae J.-C.;
RT   "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT   chungbukense DJ77.";
RL   Submitted (APR-2015) 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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKW92357.1}.
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DR   EMBL; LBIC01000004; KKW92357.1; -; Genomic_DNA.
DR   RefSeq; WP_046763564.1; NZ_LBIC01000004.1.
DR   AlphaFoldDB; A0A0M3AQ85; -.
DR   STRING; 56193.YP76_10590; -.
DR   PATRIC; fig|56193.3.peg.2195; -.
DR   Proteomes; UP000033874; Unassembled WGS sequence.
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; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
FT   DOMAIN          152..306
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   322 AA;  34720 MW;  68A736117242C62C CRC64;
     MKWGWTAMVH ALHKRFMFQS LALASMILSG APLSAILRDG DRTDMRFDQP AHMAPRPARR
     LHSITVPIPP VARGLSLPPV EGPRDASRPL VVIDAGHGGH DPGAVNRENG EREKDVTLAI
     AQAVRDQLVK SGRVRVALTR NDDHFLILQE RYGIARKLNA DLFISIHADS ADDAIARGAT
     VYTLSETASD REAARLAARE NKADVLNGVN LGGQSSDVSS ILIDLTQRES MNISVSFARL
     LQREAAPYVP FRNTAHRFAS LMVLKAPDTP SVLFETGYIS NTADAAFLAS KEGQANIARG
     VARAIEVHFA RRLAAGGDGA GG
//
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