ID A0A109B900_HYPSL Unreviewed; 447 AA.
AC A0A109B900;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=APY04_3276 {ECO:0000313|EMBL:KWT64384.1};
OS Hyphomicrobium sulfonivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Hyphomicrobiaceae; Hyphomicrobium.
OX NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT64384.1, ECO:0000313|Proteomes:UP000059074};
RN [1] {ECO:0000313|EMBL:KWT64384.1, ECO:0000313|Proteomes:UP000059074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WDL6 {ECO:0000313|EMBL:KWT64384.1,
RC ECO:0000313|Proteomes:UP000059074};
RA Albers P.;
RT "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT consortium.";
RL Submitted (OCT-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:KWT64384.1}.
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DR EMBL; LMTR01000092; KWT64384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109B900; -.
DR STRING; 121290.APY04_3276; -.
DR PATRIC; fig|121290.4.peg.1928; -.
DR OMA; THERTGM; -.
DR Proteomes; UP000059074; 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; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KWT64384.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059074}.
FT DOMAIN 272..435
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 447 AA; 47958 MW; 1DD5AEF310D34C9D CRC64;
MFCMCALLCA QSPLQAQGLL DGAQKLLQSA DSLFTGSSNA SAATSVASAP EQRTRFVVGL
PKQTEFEVFS LNNPNRVVVQ VKETSLRLPA QPAEGPVGLI KSFQAGLSGA EHSRIIIYVT
QPVIVSSARI EKPAAGKDQH LVVEIASFTP ITASIPQPEE DAVGPIAATQ VAATRPSIPP
PTYALGASGL QPPLPRPAVP PDVRAERAFK PVIVIDPGHG GHDSGAMKNG AVEKEITLAF
SKLLAKKLEA TGRYKVLLTR DKDVFIPLGD RVAFGEKHNA NLFIAVHCDY ASTNASGATI
YSLRDSVANS LRRSTRGEVA GDVLSDDEIE QVKQVGSKKD VGMVQNILAD LAGREVDATR
DRTSVFARTV IENMGSSTTM RNKPDQQASF RVLKTAQFPS VLIELAYVTN KEDARKLKSS
EWRNKVSDSI KSAVDNYFSN QLAQLPM
//