GLSA2_YERPE
ID GLSA2_YERPE Reviewed; 340 AA.
AC Q9ZC49; Q0WFL0;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
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};
GN OrderedLocusNames=YPO1939, y2372, YP_1682;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6/69;
RA Buchrieser C., Rusniok C., Couve E., Frangeul L., Billault A., Kunst F.,
RA Carniel E., Glaser P.;
RT "DNA sequence of the 102 kbases unstable region of Yersinia pestis.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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 -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00313}.
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DR EMBL; AL031866; CAA21362.1; -; Genomic_DNA.
DR EMBL; AL590842; CAL20577.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85930.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61912.1; -; Genomic_DNA.
DR PIR; AF0236; AF0236.
DR PIR; T47019; T47019.
DR RefSeq; YP_002346928.1; NC_003143.1.
DR AlphaFoldDB; Q9ZC49; -.
DR SMR; Q9ZC49; -.
DR IntAct; Q9ZC49; 1.
DR STRING; 214092.YPO1939; -.
DR PaxDb; Q9ZC49; -.
DR DNASU; 1147319; -.
DR EnsemblBacteria; AAM85930; AAM85930; y2372.
DR EnsemblBacteria; AAS61912; AAS61912; YP_1682.
DR KEGG; ype:YPO1939; -.
DR KEGG; ypk:y2372; -.
DR KEGG; ypm:YP_1682; -.
DR PATRIC; fig|214092.21.peg.2315; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_6; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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 3: Inferred from homology;
KW Hydrolase; Reference proteome.
FT CHAIN 1..340
FT /note="Glutaminase 2"
FT /id="PRO_0000110634"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 340 AA; 36180 MW; 95A0CE7C739E6D85 CRC64;
MEITDMPTDD SNNGIIDYVS TGHLPDPETV VKLVQEAHKR FSTDTAGVVS NVYPALERIP
ADLFGICMVG TNGKIHSAGD VDYEFTIMSV SKPFVFALVC QAIGAKTARE KLGVNSTGMA
FNSVTAIERA SDGRTNPMVN SGAIATTSLV PGATSDEQWK FIYDGLCRFA GRELTLNEEV
YQSACETNFR NRGIANVLQG YGRLGCDPII ATDLYTRQCS LNVSARDLAV MGATLADGGV
NPLTRERVVD NDICHYALAV MVTAGLYETS GDWLYDIGLP GKSGIGGGIV TVSPGKGGLG
TFAPLLDSAG NSIKGQLAAR FLSRSLGMDM FVSEPYTEKN
