GLSA2_BACSU
ID GLSA2_BACSU Reviewed; 309 AA.
AC O07637;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutaminase 2 {ECO:0000255|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN Name=glsA2 {ECO:0000255|HAMAP-Rule:MF_00313}; Synonyms=ylaM;
GN OrderedLocusNames=BSU14830;
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 Purnelle B., Presecan E., Glaser P., Richou A., Danchin A., Goffeau A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (JUN-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 CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 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:0000255|HAMAP-Rule:MF_00313,
CC ECO:0000269|PubMed:18459799};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.6 mM for glutamine {ECO:0000269|PubMed:18459799};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313,
CC ECO:0000269|PubMed:18459799}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00313}.
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DR EMBL; Z97025; CAB09718.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13356.1; -; Genomic_DNA.
DR PIR; C69873; C69873.
DR RefSeq; NP_389366.1; NC_000964.3.
DR RefSeq; WP_003245206.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O07637; -.
DR SMR; O07637; -.
DR STRING; 224308.BSU14830; -.
DR PaxDb; O07637; -.
DR PRIDE; O07637; -.
DR EnsemblBacteria; CAB13356; CAB13356; BSU_14830.
DR GeneID; 939852; -.
DR KEGG; bsu:BSU14830; -.
DR PATRIC; fig|224308.179.peg.1617; -.
DR eggNOG; COG2066; Bacteria.
DR InParanoid; O07637; -.
DR OMA; RPRNPFI; -.
DR PhylomeDB; O07637; -.
DR BioCyc; BSUB:BSU14830-MON; -.
DR BRENDA; 3.5.1.2; 658.
DR SABIO-RK; O07637; -.
DR PRO; PR:O07637; -.
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 Hydrolase; Reference proteome.
FT CHAIN 1..309
FT /note="Glutaminase 2"
FT /id="PRO_0000110595"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 117
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 193
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 309 AA; 34012 MW; E1DFEF1A0723C1A5 CRC64;
MVCQHNDELE ALVKKAKKVT DKGEVASYIP ALAKADKHDL SVAIYYSNNV CLSAGDVEKT
FTLQSISKVL SLALVLMEYG KDKVFSYVGQ EPTGDPFNSI IKLETVNPSK PLNPMINAGA
LVVTSLIRGR TVKERLDYLL SFIRRLTNNQ EITYCREVAE SEYSTSMINR AMCYYMKQYG
IFEDDVEAVM DLYTKQCAIE MNSLDLAKIG SVFALNGRHP ETGEQVISKD VARICKTFMV
TCGMYNASGE FAIKVGIPAK SGVSGGIMGI SPYDFGIGIF GPALDEKGNS IAGVKLLEIM
SEMYRLSIF
