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Database: UniProt
Entry: F8GHD2_NITSI
LinkDB: F8GHD2_NITSI
Original site: F8GHD2_NITSI 
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
//
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