ID A0A231MUE5_9GAMM Unreviewed; 181 AA.
AC A0A231MUE5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=CGX12_17500 {ECO:0000313|EMBL:OXS13837.1};
OS Zobellella denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Zobellella.
OX NCBI_TaxID=347534 {ECO:0000313|EMBL:OXS13837.1, ECO:0000313|Proteomes:UP000215233};
RN [1] {ECO:0000313|EMBL:OXS13837.1, ECO:0000313|Proteomes:UP000215233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZD1 {ECO:0000313|EMBL:OXS13837.1,
RC ECO:0000313|Proteomes:UP000215233};
RA Wu Y.-W., Chu K.-H.;
RT "Draft genome of Zobellella denitrificans ZD1.";
RL Submitted (JUL-2017) 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:OXS13837.1}.
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DR EMBL; NMUO01000116; OXS13837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231MUE5; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000215233; 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}.
FT DOMAIN 19..169
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 181 AA; 20100 MW; 39D3B7F841978E5F CRC64;
MPFQLTPAGW LTPARHCASP HWDERPLGEI SLLVVHCISL PPGRFGGPYI DDLFMGRLDP
AGDPYFAGIH QLRVSAHCLI RRDGELVQYV PFDKRAWHAG LSCFEGREQC NDFSVGIELE
GTDTGTYTHA QYHVLAEVSR LLMATYPAIT PGRITGHSDI APGRKTDPGP GFDWARFRAM
L
//
