GenomeNet

Database: UniProt
Entry: A0A109B900_HYPSL
LinkDB: A0A109B900_HYPSL
Original site: A0A109B900_HYPSL 
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}.
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; 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
//
DBGET integrated database retrieval system