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Database: UniProt
Entry: A0A1M4M336_9FIRM
LinkDB: A0A1M4M336_9FIRM
Original site: A0A1M4M336_9FIRM 
ID   A0A1M4M336_9FIRM        Unreviewed;       687 AA.
AC   A0A1M4M336;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:SCG82090.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:SCG82090.1};
GN   ORFNames=DW1_0470 {ECO:0000313|EMBL:SCG82090.1};
OS   Proteiniborus sp. DW1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Proteiniborus.
OX   NCBI_TaxID=1889883 {ECO:0000313|EMBL:SCG82090.1, ECO:0000313|Proteomes:UP000185208};
RN   [1] {ECO:0000313|EMBL:SCG82090.1, ECO:0000313|Proteomes:UP000185208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW1 {ECO:0000313|EMBL:SCG82090.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FMDO01000007; SCG82090.1; -; Genomic_DNA.
DR   RefSeq; WP_074349025.1; NZ_FMDO01000007.1.
DR   AlphaFoldDB; A0A1M4M336; -.
DR   STRING; 1889883.DW1_0470; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000185208; 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; -; 2.
DR   Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR036582; Mao_N_sf.
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; 2.
DR   Pfam; PF07833; Cu_amine_oxidN1; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SCG82090.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185208};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..687
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012318801"
FT   DOMAIN          562..679
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   687 AA;  76547 MW;  B466FDC9AC048EDB CRC64;
     MKKIVAAFMV FIMLMGLGAS VMAASKQSTK VSINGRQLDV ATANVIFDGK PIETDIPPII
     LKDRTLVPIR SIGNHLGAEV GWNQQTKEAT VKTANQEIVL TLNSSMVSVN GTKKEIPYGV
     PAIIVNDARI MVPLRFVSEV LGCIVDWDQD TMTGIITSQV SENIEITNIT VEESSESSPK
     IKLTTTGKIE YSEEYLSEPD RLIIDVHNSR LNISDKSIVD SNGVVNIEVN KSPIKSIRMA
     EFSKEPEIVR IVIDLDKHIG YNISTSMEDK LTTISFLNNV QDISLESING KEAIVINNSE
     EFKYSMFTLT NPNRVVIDIL DSKLWTDSLQ FDVDAEYVKS VRSSQYIPDS SVEGQDNIVR
     VVLDIKENRA IPNIKVDMKK NSLIIFVDDE GFENISYSNK NEDGGLITVH AEKRTDYSIE
     YNEKSRQMQI RVDKDDIDLA KGIVAINDDY ISNITVDEDD EYKKITFSFK QKIAYEVLSS
     STDDLIEVAF EKIEENNGAR LIVIDAGHGG KDPGAVSPYS KTKEKDLNLS VALKLDKKLR
     ELGFRTILTR STDEFIVLQE RADIANRNGA DAFISVHFNA NDKSSIAGVQ TLYCPAFNSE
     VKEEDQYPFA KAIQDALLSG LNREDRKIVK RPDLVVVRET KMVAALAELG FLTNPEEEKL
     IITEAYHEKA AQALANGIVN YFNSLGK
//
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