GLSA1_BACSU
ID GLSA1_BACSU Reviewed; 327 AA.
AC O31465;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Glutaminase 1;
DE EC=3.5.1.2;
GN Name=glsA1; Synonyms=glsA, ybgJ; OrderedLocusNames=BSU02430;
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;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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, AND GENE NAME.
RC STRAIN=168;
RX PubMed=15995196; DOI=10.1128/jb.187.14.4813-4821.2005;
RA Satomura T., Shimura D., Asai K., Sadaie Y., Hirooka K., Fujita Y.;
RT "Enhancement of glutamine utilization in Bacillus subtilis through the
RT GlnK-GlnL two-component regulatory system.";
RL J. Bacteriol. 187:4813-4821(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP 5-OXO-L-NORLEUCINE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=18459799; DOI=10.1021/bi800097h;
RA Brown G., Singer A., Proudfoot M., Skarina T., Kim Y., Chang C.,
RA Dementieva I., Kuznetsova E., Gonzalez C.F., Joachimiak A., Savchenko A.,
RA Yakunin A.F.;
RT "Functional and structural characterization of four glutaminases from
RT Escherichia coli and Bacillus subtilis.";
RL Biochemistry 47:5724-5735(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000269|PubMed:18459799};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=27.6 mM for glutamine {ECO:0000269|PubMed:18459799};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18459799}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {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; AB006424; BAA33141.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12037.1; -; Genomic_DNA.
DR PIR; D69751; D69751.
DR RefSeq; NP_388125.1; NC_000964.3.
DR RefSeq; WP_003234829.1; NZ_JNCM01000030.1.
DR PDB; 1MKI; X-ray; 2.00 A; A/B=1-327.
DR PDB; 2OSU; X-ray; 2.29 A; A/B=1-327.
DR PDB; 3AGF; X-ray; 2.60 A; A/B=1-327.
DR PDB; 3BRM; X-ray; 2.29 A; A/B=1-327.
DR PDBsum; 1MKI; -.
DR PDBsum; 2OSU; -.
DR PDBsum; 3AGF; -.
DR PDBsum; 3BRM; -.
DR AlphaFoldDB; O31465; -.
DR SMR; O31465; -.
DR STRING; 224308.BSU02430; -.
DR DrugBank; DB04522; Dexfosfoserine.
DR DrugBank; DB01942; Formic acid.
DR PaxDb; O31465; -.
DR PRIDE; O31465; -.
DR DNASU; 938416; -.
DR EnsemblBacteria; CAB12037; CAB12037; BSU_02430.
DR GeneID; 938416; -.
DR KEGG; bsu:BSU02430; -.
DR PATRIC; fig|224308.179.peg.250; -.
DR eggNOG; COG2066; Bacteria.
DR InParanoid; O31465; -.
DR OMA; RNPMINS; -.
DR PhylomeDB; O31465; -.
DR BioCyc; BSUB:BSU02430-MON; -.
DR BRENDA; 3.5.1.2; 658.
DR BRENDA; 4.3.3.6; 658.
DR SABIO-RK; O31465; -.
DR EvolutionaryTrace; O31465; -.
DR PRO; PR:O31465; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006543; P:glutamine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..327
FT /note="Glutaminase 1"
FT /id="PRO_0000110594"
FT BINDING 74
FT /ligand="substrate"
FT BINDING 126
FT /ligand="substrate"
FT BINDING 170
FT /ligand="substrate"
FT BINDING 177
FT /ligand="substrate"
FT BINDING 201
FT /ligand="substrate"
FT BINDING 253
FT /ligand="substrate"
FT BINDING 271
FT /ligand="substrate"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:2OSU"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 90..94
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 141..156
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 194..205
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 211..222
FT /evidence="ECO:0007829|PDB:1MKI"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1MKI"
FT TURN 228..231
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 256..262
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1MKI"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:1MKI"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 293..298
FT /evidence="ECO:0007829|PDB:1MKI"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1MKI"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:1MKI"
SQ SEQUENCE 327 AA; 36187 MW; BE3A1C2366460287 CRC64;
MKELIKEHQK DINPALQLHD WVEYYRPFAA NGQSANYIPA LGKVNDSQLG ICVLEPDGTM
IHAGDWNVSF TMQSISKVIS FIAACMSRGI PYVLDRVDVE PTGDAFNSII RLEINKPGKP
FNPMINAGAL TIASILPGES AYEKLEFLYS VMETLIGKRP RIHEEVFRSE WETAHRNRAL
AYYLKETNFL EAEVEETLEV YLKQCAMEST TEDIALIGLI LAHDGYHPIR HEQVIPKDVA
KLAKALMLTC GMYNASGKYA AFVGVPAKSG VSGGIMALVP PSARREQPFQ SGCGIGIYGP
AIDEYGNSLT GGMLLKHMAQ EWELSIF
