位置:首页 > 蛋白库 > PGDA3_BACCR
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}.
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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024