ID   A0A1X1Q937_9FIRM        Unreviewed;       358 AA.
AC   A0A1X1Q937;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ORU01311.1};
GN   ORFNames=D081_0130 {ECO:0000313|EMBL:ORU01311.1};
OS   Anaerovibrio sp. JC8.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Anaerovibrio.
OX   NCBI_TaxID=1240085 {ECO:0000313|EMBL:ORU01311.1, ECO:0000313|Proteomes:UP000192538};
RN   [1] {ECO:0000313|EMBL:ORU01311.1, ECO:0000313|Proteomes:UP000192538}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC8 {ECO:0000313|EMBL:ORU01311.1,
RC   ECO:0000313|Proteomes:UP000192538};
RA   Evans P.N., Cheung J.L., Rosewarne C.P., Morrison M.;
RT   "Genomic and phenotypic data suggests Anaerovibrio species JC8 from the
RT   bovine rumen reduces fumarate and sulphite to decrease the inhibitory
RT   effect of hydrogen.";
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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:ORU01311.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ANBM01000001; ORU01311.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1Q937; -.
DR   STRING; 1240085.D081_0130; -.
DR   Proteomes; UP000192538; Unassembled WGS sequence.
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; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..358
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012868860"
FT   DOMAIN          239..350
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   358 AA;  39991 MW;  238459358448A727 CRC64;
     MKKIWCRLLI VICCIMGFIG LGSVPAQAAV NHTLNYFHYN TFKDDDGRNW VRIEMGMNKG
     ELEYEVSENP DRPYHLILTL KNTNRGDVKK NIGLDRKIAR YMTLKNDHRD MVVTLAVTDS
     LSDHEYKVYT AEADRKAKKP YRLVIEVAAD KGAQHKALGD ESLEGVEGFT VVVDAGHGGS
     DTGAIGPSYV REKDVTLNIA LDVARILEAN GVNVVMTRTT DVDVYGPNAT DKQELQARVN
     VSRRHPEADI FVSIHCNAFT NSSARGTGTY YYAHGYRDSL LAQQIQDEMV AATGLRDRGI
     NQARFYVLRN SWIPATLVET AFISNPYEEN MLASAEMQHT MALAICKGIS NYFQSIGR
//