PGDA3_BACCR
ID PGDA3_BACCR Reviewed; 213 AA.
AC Q81AF4;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Peptidoglycan-N-acetylglucosamine deacetylase BC_3618 {ECO:0000303|PubMed:15961396};
DE Short=Peptidoglycan GlcNAc deacetylase {ECO:0000303|PubMed:15961396};
DE EC=3.5.1.104 {ECO:0000269|PubMed:15961396};
GN OrderedLocusNames=BC_3618 {ECO:0000312|EMBL:AAP10549.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=15961396; DOI=10.1074/jbc.m407426200;
RA Psylinakis E., Boneca I.G., Mavromatis K., Deli A., Hayhurst E.,
RA Foster S.J., Vaarum K.M., Bouriotis V.;
RT "Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus,
RT highly conserved proteins in Bacillus anthracis.";
RL J. Biol. Chem. 280:30856-30863(2005).
CC -!- FUNCTION: Catalyzes the deacetylation of N-acetylglucosamine (GlcNAc)
CC residues in peptidoglycan. Also acts on soluble chitin substrates and
CC N-acetylchitooligomers. Acts on cell wall peptidoglycan from the Gram-
CC positive bacteria B.cereus and B.subtilis and the Gram-negative
CC bacterium H.pylori. Not active on acetylated xylan.
CC {ECO:0000269|PubMed:15961396}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peptidoglycan-N-acetyl-D-glucosamine + H2O = peptidoglycan-D-
CC glucosamine + acetate.; EC=3.5.1.104;
CC Evidence={ECO:0000269|PubMed:15961396};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q81EJ6};
CC -!- ACTIVITY REGULATION: Inhibited by CuCl(2) and ZnCl(2).
CC {ECO:0000269|PubMed:15961396}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 mM for GlcNAc(2) {ECO:0000269|PubMed:15961396};
CC KM=2.2 mM for GlcNAc(3) {ECO:0000269|PubMed:15961396};
CC KM=1.5 mM for GlcNAc(4) {ECO:0000269|PubMed:15961396};
CC KM=0.5 mM for GlcNAc(5) {ECO:0000269|PubMed:15961396};
CC KM=0.45 mM for GlcNAc(6) {ECO:0000269|PubMed:15961396};
CC Vmax=8.7 umol/min/mg enzyme with GlcNAc(2) as substrate
CC {ECO:0000269|PubMed:15961396};
CC Vmax=50 umol/min/mg enzyme with GlcNAc(3) as substrate
CC {ECO:0000269|PubMed:15961396};
CC Vmax=97.3 umol/min/mg enzyme with GlcNAc(4) as substrate
CC {ECO:0000269|PubMed:15961396};
CC Vmax=24.2 umol/min/mg enzyme with GlcNAc(5) as substrate
CC {ECO:0000269|PubMed:15961396};
CC Vmax=25 umol/min/mg enzyme with GlcNAc(6) as substrate
CC {ECO:0000269|PubMed:15961396};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:15961396};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:15961396};
CC -!- SIMILARITY: Belongs to the polysaccharide deacetylase family.
CC {ECO:0000305}.
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DR EMBL; AE016877; AAP10549.1; -; Genomic_DNA.
DR RefSeq; NP_833348.1; NC_004722.1.
DR AlphaFoldDB; Q81AF4; -.
DR SMR; Q81AF4; -.
DR STRING; 226900.BC_3618; -.
DR EnsemblBacteria; AAP10549; AAP10549; BC_3618.
DR KEGG; bce:BC3618; -.
DR PATRIC; fig|226900.8.peg.3716; -.
DR HOGENOM; CLU_021264_0_1_9; -.
DR OMA; NHAMRDE; -.
DR BRENDA; 3.5.1.104; 648.
DR SABIO-RK; Q81AF4; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR014132; PdaB-like.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
DR TIGRFAMs; TIGR02764; spore_ybaN_pdaB; 1.
DR PROSITE; PS51677; NODB; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..213
FT /note="Peptidoglycan-N-acetylglucosamine deacetylase
FT BC_3618"
FT /id="PRO_0000447694"
FT DOMAIN 22..203
FT /note="NodB homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 29
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81EJ6"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81EJ6"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81EJ6"
SQ SEQUENCE 213 AA; 24455 MW; ACEC86CA8EB8E4A2 CRC64;
MLLRKELEPT GYVTWEVPNN EKIIAITFDD GPDPTYTPQV LDLLRQYKAE ATFFMIGFRV
QRNPYLVKQV LKEGHEIGNH TMNHLYASNS SDEKLENDIL DGKKFFEKWV KEPLLFRPPG
GYINDAVFKT AKEAGYQTVL WSWHQDPRDW ANPGVESIVN HVVKNAKSGD IVLLHDGGND
RSQTVAALAK ILPELKKQGY RFVTVSELLR YKH