ID   Q0B0M3_SYNWW            Unreviewed;       907 AA.
AC   Q0B0M3;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ABI67481.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:ABI67481.1};
GN   OrderedLocusNames=Swol_0126 {ECO:0000313|EMBL:ABI67481.1};
OS   Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Syntrophomonas.
OX   NCBI_TaxID=335541 {ECO:0000313|EMBL:ABI67481.1, ECO:0000313|Proteomes:UP000001968};
RN   [1] {ECO:0000313|Proteomes:UP000001968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2245B / Goettingen {ECO:0000313|Proteomes:UP000001968};
RX   PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA   Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA   McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT   "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT   metabolism and biohydrogen production.";
RL   Environ. Microbiol. 12:2289-2301(2010).
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010860}.
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DR   EMBL; CP000448; ABI67481.1; -; Genomic_DNA.
DR   RefSeq; WP_011639592.1; NC_008346.1.
DR   AlphaFoldDB; Q0B0M3; -.
DR   STRING; 335541.Swol_0126; -.
DR   KEGG; swo:Swol_0126; -.
DR   eggNOG; COG0860; Bacteria.
DR   eggNOG; COG3103; Bacteria.
DR   eggNOG; COG4991; Bacteria.
DR   HOGENOM; CLU_320018_0_0_9; -.
DR   OrthoDB; 9813450at2; -.
DR   Proteomes; UP000001968; 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; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 4.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR   InterPro; IPR036582; Mao_N_sf.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR003646; SH3-like_bac-type.
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; PF07833; Cu_amine_oxidN1; 2.
DR   Pfam; PF08239; SH3_3; 4.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 4.
DR   SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51781; SH3B; 3.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ABI67481.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001968};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          32..94
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          96..159
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          188..252
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   REGION          164..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  97081 MW;  BF2A8CEB545F8D6D CRC64;
     MKKALHIFNY TVLFSIFFSL ILILAWAQSS PAATAVIKGS VVNIRQGPGT GHEIAGTLYQ
     NTEVAILESK DGWKKIQHGS LNGWVADSLL QVKKEEIRLQ VTADKANLRS GPSTSSSQVG
     QLRQGDSLIL LDVEGEWYKV QVPGGSSAYI ASFLVSKTAV AANSSSTPAA GSQPETAATV
     PASSPAPAVT RQVEVISGPI NIRSGPGESY PKLGSIDEKT VYPVISKEGE WYKIRLANGS
     DAYVAGWLVK ESSMASSTVI PPAAASGSSA ATGGTAAGST APRVFLDGQA LSFEVPPIIE
     NDRTLVPLRA IFEALGATVD WDNATRTVTS RKGSTTVVLA IGSLAPTVNG QVRQLDVPAK
     IVADRTLAPL RFVGEAFGST VDWEGSTRTI NIKSPPAPGA PSVGSGKKAV AVTVNKEIIN
     LRSGPSTGHA QLDQARSGER MQVLAAQDGW YQVSRGGKIA WVSGEVVDVA WQENEPEAVP
     VTTSPGTPGN SSSELPPPAS PENIRILSSK DETGLKIIIG SGVELKGRLE ESGNNLRYYF
     TGRSIEGNTI IRENIAGEIL EVKAEQQGED AVIYISIPAN LKYRSASEEG GKKETIIISN
     FITGIERKTF GSKGERIILK TVLPLDYSSE QQGTQMKIKL PFLLKGSAPS EYSFDSQLMQ
     HLQLSESEVN GTQGMVLAIE TKNPAKFAFG KSAEGNQLHI LFVDQSDVQQ LGSAIVIDPG
     HGGKETGTIG SWLKEKEPNL DISLKVAALL RQRGMEIVLT RDDDSYVSLE ERADIANLYN
     ARLFVSIHNN ASQNNPAAQG SETHYYAPLD NPELFMQSAE RCRLATCIQE QLVSKLRRVD
     RGVKTGPSSN FSVLRNTRMP SALAEVVFLS NTEEEQLLQQ DYFRTLAAEA IADGITQYCG
     GSAEIKL
//