ID C9RCM7_AMMDK Unreviewed; 476 AA.
AC C9RCM7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ACX52004.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:ACX52004.1};
GN OrderedLocusNames=Adeg_0864 {ECO:0000313|EMBL:ACX52004.1};
OS Ammonifex degensii (strain DSM 10501 / KC4).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Ammonifex.
OX NCBI_TaxID=429009 {ECO:0000313|EMBL:ACX52004.1, ECO:0000313|Proteomes:UP000002620};
RN [1] {ECO:0000313|EMBL:ACX52004.1, ECO:0000313|Proteomes:UP000002620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10501 / KC4 {ECO:0000313|Proteomes:UP000002620};
RG US DOE Joint Genome Institute;
RA Kerfeld C., Goodner B., Huber H., Stetter K., Lucas S., Copeland A.,
RA Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L.,
RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Ovchinnikova G., Richardson P.;
RT "Complete sequence of chromosome of Ammonifex degensii KC4.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP001785; ACX52004.1; -; Genomic_DNA.
DR RefSeq; WP_015738881.1; NC_013385.1.
DR AlphaFoldDB; C9RCM7; -.
DR STRING; 429009.Adeg_0864; -.
DR KEGG; adg:Adeg_0864; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG2861; Bacteria.
DR HOGENOM; CLU_573229_0_0_9; -.
DR OrthoDB; 9772024at2; -.
DR Proteomes; UP000002620; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd10936; CE4_DAC2; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR006837; Divergent_DAC.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30105:SF2; DIVERGENT POLYSACCHARIDE DEACETYLASE SUPERFAMILY; 1.
DR PANTHER; PTHR30105; UNCHARACTERIZED YIBQ-RELATED; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF04748; Polysacc_deac_2; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ACX52004.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002620};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..476
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003001501"
FT DOMAIN 104..212
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 476 AA; 52263 MW; 6B247C2DA1B86174 CRC64;
MLCRLFLLVS FFFFLFSFPY AAKAGSLEGK TIVLDPGHGG CDPGAVEPRL GIYEKHINLA
VARRLQEMLR AAGARVLLTH NDPDKMEREG EVWCLPYISL RERVRLANDH RADVFISLHV
NSFSDPRRTG QEIFFARGSE AGHRLAEAFR RELAKLGGNT SCHPSSFYVL EHTCMPAVVV
EMGYLSSAAE AARLLDPGYQ QRIAEALCAG LEAYFAQANS LPAGGKLHSP RARVAIVIDD
FAGPSEKKGT REFLSLNKPL TFAVLPNYPL SAPTAREAVK AGFEVLVHLP MEPLKGDPSW
LGPGAIYVHL NDEEIERRVE RAIASVPGAV GMNNHMGSRA TADPRVIRAV LRVAKRHNLF
FLDSKTTNKS VIPQIAKELG VPYAEDGLFL DAVNDVGHIK EQLRKLAQLA LKNGSAIAIG
HVGVTGPNTV RAIKEMLPEF ERLGIELVYV STLLKHPASA GTKPEQKENH MTESER
//
