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Database: UniProt
Entry: A3X4E8_9RHOB
LinkDB: A3X4E8_9RHOB
Original site: A3X4E8_9RHOB 
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
//
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