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Beta-hexosaminidase (EC 3.2.1.52) (Beta-N-acetylhexosaminidase) (N-acetyl-beta-glucosaminidase)

 A0A1B4X1V0_9PSED        Unreviewed;       336 AA.
A0A1B4X1V0;
02-NOV-2016, integrated into UniProtKB/TrEMBL.
02-NOV-2016, sequence version 1.
25-OCT-2017, entry version 5.
RecName: Full=Beta-hexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634276};
EC=3.2.1.52 {ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634280};
AltName: Full=Beta-N-acetylhexosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
AltName: Full=N-acetyl-beta-glucosaminidase {ECO:0000256|HAMAP-Rule:MF_00364};
Name=nagZ {ECO:0000256|HAMAP-Rule:MF_00364};
ORFNames=LAB08_3521 {ECO:0000313|EMBL:BAV28791.1};
Pseudomonas sp. LAB-08.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=143813 {ECO:0000313|EMBL:BAV28791.1};
[1] {ECO:0000313|EMBL:BAV28791.1}
NUCLEOTIDE SEQUENCE.
Suzuki K., Fatma A., Inuzuka Y., Tashiro Y., Futamata H.;
"Draft genome sequence of Pseudomonassp. LAB-08 isolated from TCE
contaminated aquifer soil.";
Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Plays a role in peptidoglycan recycling by cleaving the
terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from
peptide-linked peptidoglycan fragments, giving rise to free
GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic
acid-linked peptides. {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634279}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634277}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
{ECO:0000256|HAMAP-Rule:MF_00364, ECO:0000256|SAAS:SAAS00634259}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634271}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. NagZ
subfamily. {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634275}.
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EMBL; AP017423; BAV28791.1; -; Genomic_DNA.
UniPathway; UPA00544; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-UniRule.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.20.20.300; -; 1.
HAMAP; MF_00364; NagZ; 1.
InterPro; IPR022956; Beta_hexosaminidase_bac.
InterPro; IPR019800; Glyco_hydro_3_AS.
InterPro; IPR001764; Glyco_hydro_3_N.
InterPro; IPR036962; Glyco_hydro_3_N_sf.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF00933; Glyco_hydro_3; 1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
3: Inferred from homology;
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634262};
Cell division {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634262};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634255};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634281};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634266};
Glycosidase {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00656367};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00656367};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00364,
ECO:0000256|SAAS:SAAS00634255}.
DOMAIN 10 285 Glyco_hydro_3.
{ECO:0000259|Pfam:PF00933}.
REGION 165 166 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_00364}.
ACT_SITE 178 178 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00364}.
ACT_SITE 248 248 Nucleophile. {ECO:0000256|HAMAP-
Rule:MF_00364}.
BINDING 66 66 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00364}.
BINDING 74 74 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00364}.
BINDING 135 135 Substrate. {ECO:0000256|HAMAP-
Rule:MF_00364}.
SITE 176 176 Important for catalytic activity.
{ECO:0000256|HAMAP-Rule:MF_00364}.
SEQUENCE 336 AA; 36485 MW; 43BC31AB699136FE CRC64;
MTAGLQGSLM VDVAGTWLTA EDRHLLRQPE VGGLIIFARN IEHPRQVREL SAAIRAMRPD
LLLAVDQEGG RVQRLRQGFV RLPAMRAIAD NPNAEYLAEQ CGWIMATEVL AVGLDLSFAP
VLDLDYQRSA VVGTRSFEGD PERAALLAGA FIRGMNSAGM AATGKHFPGH GWAEADSHVA
IPNDERSLDE IRANDLVPFA RLSKQLAAVM PAHVIYPQVD AQPAGFSRRW LQDILRGELQ
FDGVIFSDDL SMAGAHVVGD AASRIEAALT AGCDMGLVCN DRAAAELALS AAQRMKVKPS
PRIARMRGQS YARTDYRQDP RWLAAVGALK DAQLID


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