BSHB1_BACCR
ID BSHB1_BACCR Reviewed; 234 AA.
AC Q81FP2;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=N-acetyl-alpha-D-glucosaminyl L-malate deacetylase 1 {ECO:0000305};
DE Short=GlcNAc-Mal deacetylase 1 {ECO:0000305};
DE EC=3.5.1.- {ECO:0000269|PubMed:23758290};
DE AltName: Full=B.cereus zinc-binding protein {ECO:0000303|PubMed:17501983};
DE Short=BcZBP {ECO:0000303|PubMed:17501983};
GN Name=bshB1 {ECO:0000250|UniProtKB:Q81ST8};
GN Synonyms=bshB {ECO:0000303|PubMed:23758290};
GN OrderedLocusNames=BC_1534 {ECO:0000312|EMBL:AAP08514.1};
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-112.
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).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION AS A
RP DEACETYLASE, COFACTOR, AND SUBUNIT.
RX PubMed=17501983; DOI=10.1111/j.1742-4658.2007.05834.x;
RA Fadouloglou V.E., Deli A., Glykos N.M., Psylinakis E., Bouriotis V.,
RA Kokkinidis M.;
RT "Crystal structure of the BcZBP, a zinc-binding protein from Bacillus
RT cereus.";
RL FEBS J. 274:3044-3054(2007).
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 {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:0000269|PubMed:17501983};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for GlcNAc-Mal {ECO:0000269|PubMed:23758290};
CC KM=16.9 mM for GlcNAc {ECO:0000269|PubMed:23758290};
CC Note=kcat is 10.8 with GlcNAc-Mal. {ECO:0000269|PubMed:23758290};
CC -!- SUBUNIT: Homohexamer. Trimer of dimers. {ECO:0000269|PubMed:17501983}.
CC -!- SIMILARITY: Belongs to the PIGL family. {ECO:0000305}.
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DR EMBL; AE016877; AAP08514.1; -; Genomic_DNA.
DR RefSeq; NP_831313.1; NC_004722.1.
DR RefSeq; WP_000015673.1; NZ_CP034551.1.
DR PDB; 2IXD; X-ray; 1.80 A; A/B=1-234.
DR PDBsum; 2IXD; -.
DR AlphaFoldDB; Q81FP2; -.
DR SMR; Q81FP2; -.
DR STRING; 226900.BC_1534; -.
DR EnsemblBacteria; AAP08514; AAP08514; BC_1534.
DR GeneID; 67506236; -.
DR KEGG; bce:BC1534; -.
DR PATRIC; fig|226900.8.peg.1511; -.
DR HOGENOM; CLU_049311_3_1_9; -.
DR OMA; EIVLCNA; -.
DR SABIO-RK; Q81FP2; -.
DR EvolutionaryTrace; Q81FP2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071793; P:bacillithiol biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.10320; -; 1.
DR InterPro; IPR023842; Bacillithiol_biosynth_BshB1.
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; TIGR04001; thiol_BshB1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..234
FT /note="N-acetyl-alpha-D-glucosaminyl L-malate deacetylase
FT 1"
FT /id="PRO_0000433161"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17501983,
FT ECO:0007744|PDB:2IXD"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17501983,
FT ECO:0007744|PDB:2IXD"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:17501983,
FT ECO:0007744|PDB:2IXD"
FT MUTAGEN 112
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:23758290"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 83..96
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 111..127
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:2IXD"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2IXD"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2IXD"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:2IXD"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:2IXD"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2IXD"
SQ SEQUENCE 234 AA; 26221 MW; 7E6458D8C34C6BE6 CRC64;
MSGLHILAFG AHADDVEIGM AGTIAKYTKQ GYEVGICDLT EADLSSNGTI ELRKEEAKVA
ARIMGVKTRL NLAMPDRGLY MKEEYIREIV KVIRTYKPKL VFAPYYEDRH PDHANCAKLV
EEAIFSAGIR KYMPELSPHR VESFYNYMIN GFHKPNFCID ISEYLSIKVE ALEAYESQFS
TGSDGVKTPL TEGYVETVIA REKMFGKEVG VLYAEGFMSK KPVLLHADLL GGCK
