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Database: UniProt
Entry: A0A0Q4C1H8_9SPHN
LinkDB: A0A0Q4C1H8_9SPHN
Original site: A0A0Q4C1H8_9SPHN 
ID   A0A0Q4C1H8_9SPHN        Unreviewed;       288 AA.
AC   A0A0Q4C1H8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=ASE49_03510 {ECO:0000313|EMBL:KQM19325.1};
OS   Novosphingobium sp. Leaf2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM19325.1, ECO:0000313|Proteomes:UP000050893};
RN   [1] {ECO:0000313|EMBL:KQM19325.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19325.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM19325.1, ECO:0000313|Proteomes:UP000050893}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf2 {ECO:0000313|EMBL:KQM19325.1,
RC   ECO:0000313|Proteomes:UP000050893};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQM19325.1}.
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DR   EMBL; LMJY01000012; KQM19325.1; -; Genomic_DNA.
DR   RefSeq; WP_056769781.1; NZ_LMJY01000012.1.
DR   AlphaFoldDB; A0A0Q4C1H8; -.
DR   STRING; 1735670.ASE49_03510; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000050893; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050893}.
FT   DOMAIN          124..279
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   288 AA;  29954 MW;  AC8876C410C8249F CRC64;
     MPRTRLILVL AVPLGLLLVA LVASMAMASR AGAYDYVIRF DLPSATAPVD LPRIDGPADA
     SRPLVVIDAG HGGFDPGAGQ GALKEKTVAL EIALAIRQRL LDAGGIRVAL TRDTDRFIAL
     PDRPDMARRL NADLFVSIHA DSADGDSARG ASVYVLSEKG SSEAAERFAA RENGAGKVNG
     VALSQANANV GAILLDLSQR GAQGRSAQAA SLLLRELGDA HIGMHRDQPQ TAALAVLKAP
     DIPSILFETG YINNPADVQV LGSRAGQQQL ADAAAKAIRA FFARNAGA
//
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