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Database: UniProt
Entry: C8W565_DESAS
LinkDB: C8W565_DESAS
Original site: C8W565_DESAS 
ID   C8W565_DESAS            Unreviewed;       233 AA.
AC   C8W565;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ACV62047.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:ACV62047.1};
GN   OrderedLocusNames=Dtox_1162 {ECO:0000313|EMBL:ACV62047.1};
OS   Desulfofarcimen acetoxidans (strain ATCC 49208 / DSM 771 / KCTC 5769 / VKM
OS   B-1644 / 5575) (Desulfotomaculum acetoxidans).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV62047.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV62047.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S., Chen F.,
RA   Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Chain P., Saunders E., Brettin T., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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DR   EMBL; CP001720; ACV62047.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8W565; -.
DR   STRING; 485916.Dtox_1162; -.
DR   KEGG; dae:Dtox_1162; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_7_1_9; -.
DR   Proteomes; UP000002217; Chromosome.
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; 3.40.630.40; Zn-dependent exopeptidases; 1.
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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ACV62047.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN          117..227
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   233 AA;  26428 MW;  D8C7328E45A8A65B CRC64;
     MEQIMRTIFV LIFVSIVAAI FWVSQPVSTV AEKLIENNKQ AEQKIIVIDP GHGGYDPGAV
     HGSILEKDIN LSICEKLKKV LEANNYRVIL TRTGDYNHAI KGIHGREAKL YDMKKRVEIA
     QEAMADIIIT LHVNSVKKTS YQGAEAFYYP ISREGKTLAL AIQEEFITIP DMNKRSAKIS
     MCYMLRYSKM PSVLVEVGYL SNPRERKLLL ESKYRDLLAD KIAAGVIKYF NNK
//
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