ID A0A0S3EU58_9SPHN Unreviewed; 427 AA.
AC A0A0S3EU58;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=ATN00_00230 {ECO:0000313|EMBL:ALR18976.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR18976.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR18976.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR18976.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
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};
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DR EMBL; CP013264; ALR18976.1; -; Genomic_DNA.
DR RefSeq; WP_062060709.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3EU58; -.
DR STRING; 1332080.ATN00_00230; -.
DR KEGG; sbd:ATN00_00230; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000056968; 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 Reference proteome {ECO:0000313|Proteomes:UP000056968};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..427
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006611644"
FT DOMAIN 257..411
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 427 AA; 45239 MW; 7479AD4FF11D222A CRC64;
MIFGWTANAT ALHKRRMLQS LAMAGAIFAA APGFAGGISA VDVQGDRVVV RFDDSVEGAS
AFLLDGPRRL ALDISGAQAG RGQSYAGSNA AVAAVRQGQL NEGTARVVLD LALPATLGNA
RIAPDGKSLS FSLQGVSDNA FRTVLGRGRT QFDAPAHMSA RPRQRVHSIT VPIPRAAKGV
ALPPIEGPRD GARPLVVIDA GHGGHDPGAI NPQTGKREKD VTLAIAQAIR DELVKAGRVR
VALTRDDDRF LVLQERYGIA RKLNADLFIS VHADSAENDT ARGATVYTLS ETASDREAAR
LAARENKADI INGVNLGGQS SDVSSILIDL TQRESMNISS NFARLLQREA SPYVPFRSAY
HRFASLMVLK APDMPSVLFE TGYISNFEDA AFLSSKEGQG RIAKGVARAI EVHFARKLAL
RGSGAGG
//
