ID D8JU70_HYPDA Unreviewed; 420 AA.
AC D8JU70;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE Flags: Precursor;
GN OrderedLocusNames=Hden_0843 {ECO:0000313|EMBL:ADJ22660.1};
OS Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS TK 0415).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ22660.1, ECO:0000313|Proteomes:UP000002033};
RN [1] {ECO:0000313|Proteomes:UP000002033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC {ECO:0000313|Proteomes:UP000002033};
RX PubMed=21705585; DOI=10.1128/JB.05453-11;
RG US DOE Joint Genome Institute;
RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL J. Bacteriol. 193:4567-4568(2011).
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; CP002083; ADJ22660.1; -; Genomic_DNA.
DR RefSeq; WP_013214875.1; NC_014313.1.
DR AlphaFoldDB; D8JU70; -.
DR STRING; 582899.Hden_0843; -.
DR KEGG; hdn:Hden_0843; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_1_5; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000002033; 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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADJ22660.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002033}.
FT DOMAIN 249..409
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 420 AA; 44883 MW; 6C8C5E374EF311CB CRC64;
MRGFSERLWN ARFFATVALG LALFLGAGPS QARQGRAVEA TAVRLLDDGK STTFELTISK
DLTAQVYTLA NPYRVVLDLP EMAFRLDAAA GKQARGVVSA FRYGLFAQNK ARVVLDTTGP
VGIVSAGMTR IPGSKALKLA VVLVPMDAAA FGGGTGASLA AATASELVPD QGLPETAERQ
RRNHAKPVIV IDPGHGGIDP GALGANNVAE KSVVLAVALQ LKAALAKTRR YEVKMTRTDD
VFISLERRLK FSAENDADLF ISLHADSIEE KSIADSIRGA TVYTLSDKAS DEQARIMADK
ENASDLIAGI GSVNNEGGEE VKNILIDLLK RETSNFSADF SNVLSKKLGQ AITMSRIPRK
SAAFKVLKQP HAPSVLVELG YISNTMQEQE MMTGDWQSKV AEAIASAVQS YFSKRTAAQP
//
