ID A3X4E8_9RHOB Unreviewed; 411 AA.
AC A3X4E8;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=MED193_21104 {ECO:0000313|EMBL:EAQ47732.1};
OS Roseobacter sp. MED193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=314262 {ECO:0000313|EMBL:EAQ47732.1, ECO:0000313|Proteomes:UP000005943};
RN [1] {ECO:0000313|EMBL:EAQ47732.1, ECO:0000313|Proteomes:UP000005943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED193 {ECO:0000313|EMBL:EAQ47732.1,
RC ECO:0000313|Proteomes:UP000005943};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (JAN-2006) 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:EAQ47732.1}.
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DR EMBL; AANB01000001; EAQ47732.1; -; Genomic_DNA.
DR RefSeq; WP_009811701.1; NZ_CH902583.1.
DR AlphaFoldDB; A3X4E8; -.
DR STRING; 314262.MED193_21104; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_1_5; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000005943; 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}.
FT DOMAIN 241..396
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 411 AA; 43749 MW; C5D588803119F03F CRC64;
MGKLHAAMAA LWLGGLSLMG SLASGQEFSG LARITSEISQ VRDTGRGAAI QLGLSQGVPY
RLFTLDEPAR LVLDFQEVDW TGLNADEFLT GEAITSVQFG TYVPGWSRMV LELSGPMAVG
AAELDVDPVT AAAVLTLALA PSTPEDFARG AGAPQDERWD LPAPQALDVV PPRDENAPLL
VVLDPGHGGI DPGAKAEGGV VEKDLMLQFA LELGEILVRS GQFDVQVTRD GDYFVSLERR
TALAHQAGAD LFISLHADSL TQGHAHGSTV YILSEEASDA ASASLAERHD RADLLSGTDL
SHTDDLVAGV MLDLARQETQ PRSVALAQAL VAGLKQQGGP VNRKPLRSAG FSVLKSADIP
SVLVEIGFLS SARDLANLQN PEWRRQTATA MLKGLIDWRI EDEARRALVR Q
//