BSHB2_BACAN
ID BSHB2_BACAN Reviewed; 226 AA.
AC Q81WT0; E9RAP9; E9RAQ0; Q6HUY3; Q6KP59;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 2 {ECO:0000305};
DE Short=GlcNAc-Mal deacetylase 2 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000269|PubMed:23758290};
GN Name=bshB2 {ECO:0000303|PubMed:23758290};
GN Synonyms=bca {ECO:0000303|PubMed:23758290};
GN OrderedLocusNames=BA_3888 {ECO:0000312|EMBL:AAP27621.1},
GN BAS3602 {ECO:0000312|EMBL:AAT55906.1},
GN GBAA_3888 {ECO:0000312|EMBL:AAT33001.1};
GN ORFNames=BF27_3799 {ECO:0000312|EMBL:AJH89515.1},
GN TM00_18885 {ECO:0000312|EMBL:AJG30403.1};
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2002013094;
RA Davenport K.W., Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O.,
RA Coyne S.R., Daligault H.E., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pollino;
RA Fasanella A., Braun P., Grass G., Hanczaruk M., Aceti A., Serrecchia L.,
RA Marino L., Georgi E., Antwerpen M.H.;
RT "Genome sequence of Bacillus anthracis Pollino isolated from a bovine
RT anthrax-burial site in Italy.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23758290; DOI=10.1042/bj20130415;
RA Fang Z., Roberts A.A., Weidman K., Sharma S.V., Claiborne A.,
RA Hamilton C.J., Dos Santos P.C.;
RT "Cross-functionalities of Bacillus deacetylases involved in bacillithiol
RT biosynthesis and bacillithiol-S-conjugate detoxification pathways.";
RL Biochem. J. 454:239-247(2013).
CC -!- FUNCTION: Involved in bacillithiol (BSH) biosynthesis. Catalyzes the
CC second step of the pathway, the deacetylation of N-
CC acetylglucosaminylmalate (GlcNAc-Mal) to glucosamine malate (GlcN-Mal).
CC Could also be involved in bacillithiol-detoxifying pathways through
CC formation of S-mercapturic adducts. {ECO:0000269|PubMed:23758290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malyl N-acetyl-alpha-D-glucosaminide + H2O = (S)-malyl
CC alpha-D-glucosaminide + acetate; Xref=Rhea:RHEA:33411,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:64870,
CC ChEBI:CHEBI:64871; Evidence={ECO:0000269|PubMed:23758290};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q81FP2};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for GlcNAc-Mal {ECO:0000269|PubMed:23758290};
CC Note=kcat is 6.48 sec(-1) with GlcNAc-Mal. kcat is 0.031 with
CC bacillithiol-S-bimane (BSmB). {ECO:0000269|PubMed:23758290};
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR EMBL; AE016879; AAP27621.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33001.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT55906.1; -; Genomic_DNA.
DR EMBL; CP009902; AJH89515.1; -; Genomic_DNA.
DR EMBL; CP010813; AJG30403.1; -; Genomic_DNA.
DR RefSeq; NP_846135.1; NC_003997.3.
DR RefSeq; WP_000787327.1; NZ_WXXJ01000001.1.
DR RefSeq; YP_029855.1; NC_005945.1.
DR AlphaFoldDB; Q81WT0; -.
DR SMR; Q81WT0; -.
DR STRING; 260799.BAS3602; -.
DR DNASU; 1085379; -.
DR EnsemblBacteria; AAP27621; AAP27621; BA_3888.
DR EnsemblBacteria; AAT33001; AAT33001; GBAA_3888.
DR GeneID; 45023582; -.
DR KEGG; ban:BA_3888; -.
DR KEGG; bar:GBAA_3888; -.
DR KEGG; bat:BAS3602; -.
DR PATRIC; fig|198094.11.peg.3857; -.
DR eggNOG; COG2120; Bacteria.
DR HOGENOM; CLU_049311_4_2_9; -.
DR OMA; MHPERNW; -.
DR SABIO-RK; Q81WT0; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR023841; BshB2.
DR InterPro; IPR003737; GlcNAc_PI_deacetylase-related.
DR InterPro; IPR024078; LmbE-like_dom_sf.
DR PANTHER; PTHR12993; PTHR12993; 1.
DR Pfam; PF02585; PIG-L; 1.
DR SUPFAM; SSF102588; SSF102588; 1.
DR TIGRFAMs; TIGR04000; thiol_BshB2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..226
FT /note="Probable N-acetyl-alpha-D-glucosaminyl L-malate
FT deacetylase 2"
FT /id="PRO_0000433162"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q81FP2"
SQ SEQUENCE 226 AA; 25857 MW; 698D1AD61B0EFF4C CRC64;
MKNERHVLIV FPHPDDESYC VAGTILAYTQ RNVPLTYVCL TLGEMGRAMG NPPFATRESL
YAIREKELKR ATNILGIKDL RMMGYRDKTL EFETPGELRR VIQKCVEELN PSLVISFYPG
YAVHPDHDAT GEAVAEALAT IPENKRPTFY AVAFANNHEA EIGPPHVKNE VKEYVPKKLE
ALQAHASQFA TKVTELKREY EDGVTETVEW LEREPFWIYP FKDKNK
