ID F8GHD2_NITSI Unreviewed; 487 AA.
AC F8GHD2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Nit79A3_1563 {ECO:0000313|EMBL:AEJ01383.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ01383.1};
RN [1] {ECO:0000313|EMBL:AEJ01383.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ01383.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; CP002876; AEJ01383.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GHD2; -.
DR STRING; 261292.Nit79A3_1563; -.
DR KEGG; nii:Nit79A3_1563; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_4; -.
DR OMA; THERTGM; -.
DR OrthoDB; 9806267at2; -.
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; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
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; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEJ01383.1}.
FT DOMAIN 311..468
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 203..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54032 MW; 5360BA3DE3C0468F CRC64;
MLDTVEKSER SVIAYLNGNQ SAPIRHAFLP SFILSFLFFL LFLSQSALAA DTTVQSVRVG
LTPDYTRITL ESDQPLEYEL SMLENPYRVV IDLSHTKLSQ ALTALPQKVD AIDPFVQKIR
VGQFKPHVIR LVFDLKSNVV PRTFVIEPKE NFAHRLILDI YHPDKAGKAD LNARIDPSAI
ADFETDVLDE LVATLVHDGN KLKTNQTPLI RPHSPKPQLN QTKQPVSLQA AQARKPSKAP
QKILVPRIII VAIDPGHGGK DPGAVGYQGT HEKDITLAIA RKLKERIDKE PNMRAVLTRD
GDYYISLPQR RINARRVNAD LFVSIHADAN PKSHAHGSSV FTLSEHGATS TTASWLANKE
NSVDSDLMGG IDITSKSKDI KELLLDLSLN ATINDSVKLA EYVLKQLGGI NHLHKRNVEQ
AGFAVLKSPD IPSILVETAF LSNPKEEEKL RSKNYQDKMA DAMYLGIKKY FADNPALARA
AEMAQVK
//