ID F9ZV89_METMM Unreviewed; 329 AA.
AC F9ZV89;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
DE EC=3.2.1.52 {ECO:0000256|HAMAP-Rule:MF_00364};
DE AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
DE AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
GN Name=nagZ {ECO:0000256|HAMAP-Rule:MF_00364};
GN OrderedLocusNames=Metme_2295 {ECO:0000313|EMBL:AEG00699.1};
OS Methylomonas methanica (strain MC09).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG00699.1, ECO:0000313|Proteomes:UP000008888};
RN [1] {ECO:0000313|EMBL:AEG00699.1, ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|EMBL:AEG00699.1,
RC ECO:0000313|Proteomes:UP000008888};
RX PubMed=22123758; DOI=10.1128/JB.06267-11;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L., Murrell J.C.;
RT "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT methanica MC09.";
RL J. Bacteriol. 193:7001-7002(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MC09;
RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA Stein L.Y., Murrell C.;
RT "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT methanica MC09.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000008888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT "Complete sequence of Methylomonas methanica MC09.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
CC terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-
CC linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-
CC acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
CC {ECO:0000256|HAMAP-Rule:MF_00364}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001231, ECO:0000256|HAMAP-
CC Rule:MF_00364};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000256|HAMAP-Rule:MF_00364}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00364}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002738; AEG00699.1; -; Genomic_DNA.
DR AlphaFoldDB; F9ZV89; -.
DR STRING; 857087.Metme_2295; -.
DR KEGG; mmt:Metme_2295; -.
DR eggNOG; COG1472; Bacteria.
DR HOGENOM; CLU_008392_0_0_6; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000008888; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.300; Glycoside hydrolase, family 3, N-terminal domain; 1.
DR HAMAP; MF_00364; NagZ; 1.
DR InterPro; IPR022956; Beta_hexosaminidase_bac.
DR InterPro; IPR001764; Glyco_hydro_3_N.
DR InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR30480:SF13; BETA-HEXOSAMINIDASE; 1.
DR PANTHER; PTHR30480; BETA-HEXOSAMINIDASE-RELATED; 1.
DR Pfam; PF00933; Glyco_hydro_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00364};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00364};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_00364};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00364};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00364}; Reference proteome {ECO:0000313|Proteomes:UP000008888}.
FT DOMAIN 10..285
FT /note="Glycoside hydrolase family 3 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00933"
FT ACT_SITE 167
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT BINDING 154..155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
FT SITE 165
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00364"
SQ SEQUENCE 329 AA; 35721 MW; F5628A9F817E762D CRC64;
MIDLEGHDLS ALDKEKINHP NTGALILFAR NVDNPEQIQA LVKAIRAARK GDILVAVDQE
GGRVQRFKNG FTRLPPAICY AENPELAETA GWLMAAEVLS VDVDFSFAPV LDVDCGISEI
IGNRAFALEP EQAAQLAGAF VKGMRAAGMA ATGKHFPGHG AVAADSHLAL PVDPRPLAEI
RARDLLPFRR LIEQGLEAVM PAHVVYSQVD DMPAGFSKIW LQQILRKELG FDGAIFSDDL
SMEGAAGVGD FLDRAQLAQQ AGCDMLLVCN NPSAAEQVLD KLPVTLNSDR ERHLQAMRGQ
SKIDRAHLLK SEKWRQAAAQ ILQLTETHA
//
