BSHA_BACSU
ID BSHA_BACSU Reviewed; 377 AA.
AC P42982;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=N-acetyl-alpha-D-glucosaminyl L-malate synthase {ECO:0000250|UniProtKB:Q81ST7};
DE Short=GlcNAc-Mal synthase {ECO:0000250|UniProtKB:Q81ST7};
DE EC=2.4.1.- {ECO:0000269|PubMed:20308541, ECO:0000269|PubMed:22569254};
DE AltName: Full=L-malic acid glycosyltransferase BshA {ECO:0000303|PubMed:20308541};
GN Name=bshA {ECO:0000303|PubMed:20308541}; Synonyms=jojH, ypjH;
GN OrderedLocusNames=BSU22460;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=20308541; DOI=10.1073/pnas.1000928107;
RA Gaballa A., Newton G.L., Antelmann H., Parsonage D., Upton H., Rawat M.,
RA Claiborne A., Fahey R.C., Helmann J.D.;
RT "Biosynthesis and functions of bacillithiol, a major low-molecular-weight
RT thiol in Bacilli.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6482-6486(2010).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=168 / JH642;
RX PubMed=22569254; DOI=10.1016/j.febslet.2012.02.028;
RA Upton H., Newton G.L., Gushiken M., Lo K., Holden D., Fahey R.C., Rawat M.;
RT "Characterization of BshA, bacillithiol glycosyltransferase from
RT Staphylococcus aureus and Bacillus subtilis.";
RL FEBS Lett. 586:1004-1008(2012).
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:20308541, ECO:0000269|PubMed:22569254}.
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:20308541, ECO:0000269|PubMed:22569254};
CC -!- ACTIVITY REGULATION: Inhibited by BSH. {ECO:0000269|PubMed:22569254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.41 mM for L-malate {ECO:0000269|PubMed:22569254};
CC KM=0.37 mM for UDP-GlcNAc {ECO:0000269|PubMed:22569254};
CC Vmax=11200 nmol/min/mg enzyme toward L-malate
CC {ECO:0000269|PubMed:22569254};
CC Vmax=8700 nmol/min/mg enzyme toward UDP-GlcNAc
CC {ECO:0000269|PubMed:22569254};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:22569254}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not produce bacillithiol.
CC {ECO:0000269|PubMed:20308541}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; L38424; AAA92877.1; ALT_SEQ; Genomic_DNA.
DR EMBL; L47709; AAB38445.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14162.1; -; Genomic_DNA.
DR PIR; G69937; G69937.
DR RefSeq; NP_390127.1; NC_000964.3.
DR RefSeq; WP_003230645.1; NZ_JNCM01000036.1.
DR PDB; 5D00; X-ray; 2.15 A; A/B=1-377.
DR PDB; 5D01; X-ray; 2.02 A; A/B=1-377.
DR PDBsum; 5D00; -.
DR PDBsum; 5D01; -.
DR AlphaFoldDB; P42982; -.
DR SMR; P42982; -.
DR STRING; 224308.BSU22460; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PaxDb; P42982; -.
DR PRIDE; P42982; -.
DR EnsemblBacteria; CAB14162; CAB14162; BSU_22460.
DR GeneID; 939029; -.
DR KEGG; bsu:BSU22460; -.
DR PATRIC; fig|224308.179.peg.2450; -.
DR eggNOG; COG0438; Bacteria.
DR InParanoid; P42982; -.
DR OMA; APVPWFP; -.
DR PhylomeDB; P42982; -.
DR BioCyc; BSUB:BSU22460-MON; -.
DR BioCyc; MetaCyc:BSU22460-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
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..377
FT /note="N-acetyl-alpha-D-glucosaminyl L-malate synthase"
FT /id="PRO_0000080315"
FT BINDING 17
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000250|UniProtKB:Q81ST7"
FT BINDING 95
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000250|UniProtKB:Q81ST7"
FT BINDING 123
FT /ligand="(S)-malate"
FT /ligand_id="ChEBI:CHEBI:15589"
FT /evidence="ECO:0000250|UniProtKB:Q81ST7"
FT BINDING 207
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q81ST7"
FT BINDING 263
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q81ST7"
FT BINDING 291
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q81ST7"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:5D01"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5D01"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 71..86
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:5D01"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 307..310
FT /evidence="ECO:0007829|PDB:5D01"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:5D01"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 339..355
FT /evidence="ECO:0007829|PDB:5D01"
FT HELIX 359..373
FT /evidence="ECO:0007829|PDB:5D01"
SQ SEQUENCE 377 AA; 41979 MW; 2DB1AB344D6536AA CRC64;
MRKLKIGITC YPSVGGSGII ATELGKQLAE KGHEIHFITS SIPFRLNTYH PNIHFHEVEV
NQYAVFKYPP YDLTLASKIA EVAERENLDI IHAHYALPHA VCAYLAKQML KRNIGIVTTL
HGTDITVLGY DPSLKDLIRF AIESSDRVTA VSSALAAETY DLIKPEKKIE TIYNFIDERV
YLKKNTAAIK EKHGILPDEK VVIHVSNFRK VKRVQDVIRV FRNIAGKTKA KLLLVGDGPE
KSTACELIRK YGLEDQVLML GNQDRVEDLY SISDLKLLLS EKESFGLVLL EAMACGVPCI
GTNIGGIPEV IKNNVSGFLV DVGDVTAATA RAMSILEDEQ LSNRFTKAAI EMLENEFSSK
KIVSQYEQIY ADLAEPE
