GLSA2_ECOLI
ID GLSA2_ECOLI Reviewed; 308 AA.
AC P0A6W0; P77470;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=yneH;
GN OrderedLocusNames=b1524, JW1517;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
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=30.6 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; U00096; AAC74597.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15206.1; -; Genomic_DNA.
DR PIR; G64906; G64906.
DR RefSeq; NP_416041.1; NC_000913.3.
DR RefSeq; WP_000257409.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P0A6W0; -.
DR SMR; P0A6W0; -.
DR BioGRID; 4261695; 8.
DR DIP; DIP-12757N; -.
DR IntAct; P0A6W0; 3.
DR STRING; 511145.b1524; -.
DR jPOST; P0A6W0; -.
DR PaxDb; P0A6W0; -.
DR PRIDE; P0A6W0; -.
DR EnsemblBacteria; AAC74597; AAC74597; b1524.
DR EnsemblBacteria; BAA15206; BAA15206; BAA15206.
DR GeneID; 66674622; -.
DR GeneID; 944973; -.
DR KEGG; ecj:JW1517; -.
DR KEGG; eco:b1524; -.
DR PATRIC; fig|1411691.4.peg.742; -.
DR EchoBASE; EB3577; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_6; -.
DR InParanoid; P0A6W0; -.
DR OMA; RPRNPFI; -.
DR PhylomeDB; P0A6W0; -.
DR BioCyc; EcoCyc:G6810-MON; -.
DR BioCyc; MetaCyc:G6810-MON; -.
DR BRENDA; 3.5.1.2; 2026.
DR SABIO-RK; P0A6W0; -.
DR PRO; PR:P0A6W0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IDA:EcoCyc.
DR GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR GO; GO:0006543; P:glutamine catabolic process; IMP:EcoCyc.
DR GO; GO:0045926; P:negative regulation of growth; IMP:EcoliWiki.
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..308
FT /note="Glutaminase 2"
FT /id="PRO_0000110608"
FT BINDING 66
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 161
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 308 AA; 33516 MW; DDC39D9DC0D8A651 CRC64;
MAVAMDNAIL ENILRQVRPL IGQGKVADYI PALATVDGSR LGIAICTVDG QLFQAGDAQE
RFSIQSISKV LSLVVAMRHY SEEEIWQRVG KDPSGSPFNS LVQLEMEQGI PRNPFINAGA
LVVCDMLQGR LSAPRQRMLE VVRGLSGVSD ISYDTVVARS EFEHSARNAA IAWLMKSFGN
FHHDVTTVLQ NYFHYCALKM SCVELARTFV FLANQGKAIH IDEPVVTPMQ ARQINALMAT
SGMYQNAGEF AWRVGLPAKS GVGGGIVAIV PHEMAIAVWS PELDDAGNSL AGIAVLEQLT
KQLGRSVY
