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Database: UniProt
Entry: A0A061QIN4_9PROT
LinkDB: A0A061QIN4_9PROT
Original site: A0A061QIN4_9PROT 
ID   A0A061QIN4_9PROT        Unreviewed;       254 AA.
AC   A0A061QIN4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   Name=amiD {ECO:0000313|EMBL:GAK34084.1};
GN   ORFNames=AQ1_01980 {ECO:0000313|EMBL:GAK34084.1};
OS   alpha proteobacterium Q-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1492281 {ECO:0000313|EMBL:GAK34084.1, ECO:0000313|Proteomes:UP000027360};
RN   [1] {ECO:0000313|EMBL:GAK34084.1, ECO:0000313|Proteomes:UP000027360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q-1 {ECO:0000313|EMBL:GAK34084.1,
RC   ECO:0000313|Proteomes:UP000027360};
RX   PubMed=22447601; DOI=10.1128/AEM.00084-12;
RA   Suzuki M., Eda Y., Ohsawa S., Kanesaki Y., Yoshikawa H., Tanaka K.,
RA   Muramatsu Y., Yoshikawa J., Sato I., Fujii T., Amachi S.;
RT   "Iodide oxidation by a novel multicopper oxidase from the
RT   alphaproteobacterium strain Q-1.";
RL   Appl. Environ. Microbiol. 78:3941-3949(2012).
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   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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:GAK34084.1}.
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DR   EMBL; BAYV01000024; GAK34084.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061QIN4; -.
DR   STRING; 1492281.AQ1_01980; -.
DR   Proteomes; UP000027360; 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; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027360}.
FT   DOMAIN          16..152
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   254 AA;  28235 MW;  71DFEA1B61ED2625 CRC64;
     MDSHLTQIHR PSPNFGPRHP LLGRDLPDLV VLHYTGMISA KAALARLCDP RSLVSAHYLI
     DEDGTLYGLV AEDHRAWHAG KSCWEGISDV NSRSIGIELV NPGHGFGYRP FPTPQIDRLI
     ALLHDIRQRH PIADWHLLGH SDVAPARKID PGERFPWALL ARHGLGLFPE IKALGSACNI
     SVTDLQYDLM AFGYDLDPNG LYDHKTMQIV RAAQRHFTPD HITGVAQPAL VAFLKALCYA
     KAQQGKVTDE QEFP
//
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