BSHA_BACAN
ID BSHA_BACAN Reviewed; 381 AA.
AC Q81ST7; E9QTS5; E9QTS6; Q6I117; Q6KUX0;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=N-acetyl-alpha-D-glucosaminyl L-malate synthase {ECO:0000303|PubMed:20799687};
DE Short=GlcNAc-Mal synthase {ECO:0000303|PubMed:20799687};
DE EC=2.4.1.- {ECO:0000269|PubMed:20799687};
DE AltName: Full=L-malic acid glycosyltransferase BshA {ECO:0000250|UniProtKB:P42982};
GN Name=bshA {ECO:0000303|PubMed:20799687};
GN OrderedLocusNames=BA_1558 {ECO:0000312|EMBL:AAP25494.1},
GN BAS1445 {ECO:0000312|EMBL:AAT53765.1},
GN GBAA_1558 {ECO:0000312|EMBL:AAT30656.1};
GN ORFNames=BF27_423 {ECO:0000312|EMBL:AJH86298.1},
GN TM00_07900 {ECO:0000312|EMBL:AJG28382.1};
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 X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS).
RX PubMed=18712829; DOI=10.1002/prot.22171;
RA Ruane K.M., Davies G.J., Martinez-Fleites C.;
RT "Crystal structure of a family GT4 glycosyltransferase from Bacillus
RT anthracis ORF BA1558.";
RL Proteins 73:784-787(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) IN COMPLEX WITH (R)-MALIC ACID AND
RP UDP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=20799687; DOI=10.1021/bi100698n;
RA Parsonage D., Newton G.L., Holder R.C., Wallace B.D., Paige C.,
RA Hamilton C.J., Dos Santos P.C., Redinbo M.R., Reid S.D., Claiborne A.;
RT "Characterization of the N-acetyl-alpha-D-glucosaminyl L-malate synthase
RT and deacetylase functions for bacillithiol biosynthesis in Bacillus
RT anthracis.";
RL Biochemistry 49:8398-8414(2010).
CC -!- FUNCTION: Involved in bacillithiol (BSH) biosynthesis. Catalyzes the
CC first step of the pathway, the formation of N-acetylglucosaminylmalate
CC (GlcNAc-Mal) from UDP-N-acetylglucosamine (UDP-GlcNAc) and L-malate.
CC {ECO:0000269|PubMed:20799687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-malate + UDP-N-acetyl-alpha-D-glucosamine = (S)-malyl N-
CC acetyl-alpha-D-glucosaminide + H(+) + UDP; Xref=Rhea:RHEA:33383,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:64870;
CC Evidence={ECO:0000269|PubMed:20799687};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.37 mM for UDP-GlcNAc {ECO:0000269|PubMed:20799687};
CC KM=58 uM for L-malate {ECO:0000269|PubMed:20799687};
CC Note=kcat is 28 sec(-1). {ECO:0000269|PubMed:20799687};
CC -!- SUBUNIT: Dimer of tetramers. {ECO:0000269|PubMed:20799687}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not produce bacillithiol.
CC {ECO:0000269|PubMed:20799687}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {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; AE016879; AAP25494.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT30656.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53765.1; -; Genomic_DNA.
DR EMBL; CP009902; AJH86298.1; -; Genomic_DNA.
DR EMBL; CP010813; AJG28382.1; -; Genomic_DNA.
DR RefSeq; NP_844008.1; NC_003997.3.
DR RefSeq; WP_000768296.1; NZ_WXXJ01000001.1.
DR RefSeq; YP_027714.1; NC_005945.1.
DR PDB; 2JJM; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-381.
DR PDB; 3MBO; X-ray; 3.31 A; A/B/C/D/E/F/G/H=1-381.
DR PDBsum; 2JJM; -.
DR PDBsum; 3MBO; -.
DR AlphaFoldDB; Q81ST7; -.
DR SMR; Q81ST7; -.
DR STRING; 261594.GBAA_1558; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR DNASU; 1086392; -.
DR EnsemblBacteria; AAP25494; AAP25494; BA_1558.
DR EnsemblBacteria; AAT30656; AAT30656; GBAA_1558.
DR GeneID; 45021530; -.
DR GeneID; 64203021; -.
DR KEGG; ban:BA_1558; -.
DR KEGG; bar:GBAA_1558; -.
DR KEGG; bat:BAS1445; -.
DR PATRIC; fig|198094.11.peg.1528; -.
DR eggNOG; COG0438; Bacteria.
DR HOGENOM; CLU_009583_2_5_9; -.
DR OMA; APVPWFP; -.
DR SABIO-RK; Q81ST7; -.
DR EvolutionaryTrace; Q81ST7; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0071793; P:bacillithiol biosynthetic process; IEA:InterPro.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR023881; Thiol_BshA.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR03999; thiol_BshA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..381
FT /note="N-acetyl-alpha-D-glucosaminyl L-malate synthase"
FT /id="PRO_0000433154"
FT BINDING 16
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:20799687,
FT ECO:0007744|PDB:3MBO"
FT BINDING 94
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:20799687,
FT ECO:0007744|PDB:3MBO"
FT BINDING 122
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000269|PubMed:20799687,
FT ECO:0007744|PDB:3MBO"
FT BINDING 206
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:20799687,
FT ECO:0007744|PDB:3MBO"
FT BINDING 262
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:20799687,
FT ECO:0007744|PDB:3MBO"
FT BINDING 290
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:20799687,
FT ECO:0007744|PDB:3MBO"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:3MBO"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:3MBO"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 240..248
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:3MBO"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 286..293
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:2JJM"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:2JJM"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 338..355
FT /evidence="ECO:0007829|PDB:2JJM"
FT HELIX 358..371
FT /evidence="ECO:0007829|PDB:2JJM"
SQ SEQUENCE 381 AA; 42843 MW; AB939D5FCE9A7345 CRC64;
MKLKIGITCY PSVGGSGVVG TELGKQLAER GHEIHFITSG LPFRLNKVYP NIYFHEVTVN
QYSVFQYPPY DLALASKMAE VAQRENLDIL HVHYAIPHAI CAYLAKQMIG ERIKIVTTLH
GTDITVLGSD PSLNNLIRFG IEQSDVVTAV SHSLINETHE LVKPNKDIQT VYNFIDERVY
FKRDMTQLKK EYGISESEKI LIHISNFRKV KRVQDVVQAF AKIVTEVDAK LLLVGDGPEF
CTILQLVKNL HIEDRVLFLG KQDNVAELLA MSDLMLLLSE KESFGLVLLE AMACGVPCIG
TRVGGIPEVI QHGDTGYLCE VGDTTGVADQ AIQLLKDEEL HRNMGERARE SVYEQFRSEK
IVSQYETIYY DVLRDDKNGK I
