ID A0A0J8H0N4_9ALTE Unreviewed; 179 AA.
AC A0A0J8H0N4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD {ECO:0000256|ARBA:ARBA00039257};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE AltName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00042615};
GN ORFNames=XM47_01305 {ECO:0000313|EMBL:KMT67004.1};
OS Catenovulum maritimum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1513271 {ECO:0000313|EMBL:KMT67004.1, ECO:0000313|Proteomes:UP000037600};
RN [1] {ECO:0000313|EMBL:KMT67004.1, ECO:0000313|Proteomes:UP000037600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:KMT67004.1,
RC ECO:0000313|Proteomes:UP000037600};
RA Li Y., Li D., Chen G., Du Z.;
RT "Draft Genome Sequence of the Novel Agar-Digesting Marine Bacterium Q1.";
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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:KMT67004.1}.
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DR EMBL; LAZL01000002; KMT67004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8H0N4; -.
DR STRING; 1513271.XM47_01305; -.
DR PATRIC; fig|1513271.3.peg.274; -.
DR Proteomes; UP000037600; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR PANTHER; PTHR30417:SF4; 1,6-ANHYDRO-N-ACETYLMURAMYL-L-ALANINE AMIDASE AMPD; 1.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000037600}.
FT DOMAIN 15..166
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 179 AA; 20453 MW; A42B2C5549193757 CRC64;
MNHQHIYQNA VYRHSPHFNQ RPEKIAISLL VIHCISLPEG QFGLNHIDDL FLGCINCNAH
PDFKDLAGLE VSAHILIRRD GQVIQYVPFD KRAWHAGVSE FNGVPNCNDF SIGIELEGCD
NLAYEDIQYK TLAELTKEIQ IRYPDITQQR IVGHSDIAPG RKTDPGKAFD WEHYFSLID
//
