ID GLSA1_ECOLI Reviewed; 310 AA.
AC P77454; Q2MBU2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 24-JAN-2024, entry version 160.
DE RecName: Full=Glutaminase 1 {ECO:0000255|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN Name=glsA1 {ECO:0000255|HAMAP-Rule:MF_00313}; Synonyms=ybaS;
GN OrderedLocusNames=b0485, JW0474;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF
RP LYS-69; ASN-117; SER-160; GLU-161; GLN-162; ASN-168; TYR-192; TYR-244 AND
RP SER-260, 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=7.3 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}.
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; U82664; AAB40239.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73587.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76264.1; -; Genomic_DNA.
DR PIR; D64779; D64779.
DR RefSeq; NP_415018.1; NC_000913.3.
DR RefSeq; WP_000883034.1; NZ_SSZK01000009.1.
DR PDB; 1U60; X-ray; 1.61 A; A/B/C/D=1-310.
DR PDBsum; 1U60; -.
DR AlphaFoldDB; P77454; -.
DR SMR; P77454; -.
DR BioGRID; 4261985; 19.
DR DIP; DIP-11307N; -.
DR IntAct; P77454; 3.
DR STRING; 511145.b0485; -.
DR DrugBank; DB01942; Formic acid.
DR iPTMnet; P77454; -.
DR jPOST; P77454; -.
DR PaxDb; 511145-b0485; -.
DR EnsemblBacteria; AAC73587; AAC73587; b0485.
DR GeneID; 946187; -.
DR KEGG; ecj:JW0474; -.
DR KEGG; eco:b0485; -.
DR PATRIC; fig|1411691.4.peg.1791; -.
DR EchoBASE; EB3036; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_6; -.
DR InParanoid; P77454; -.
DR OMA; RNPMINS; -.
DR OrthoDB; 9788822at2; -.
DR PhylomeDB; P77454; -.
DR BioCyc; EcoCyc:G6261-MONOMER; -.
DR BioCyc; MetaCyc:G6261-MONOMER; -.
DR BRENDA; 3.5.1.2; 2026.
DR SABIO-RK; P77454; -.
DR EvolutionaryTrace; P77454; -.
DR PRO; PR:P77454; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
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; IBA:GO_Central.
DR GO; GO:0045926; P:negative regulation of growth; IMP:EcoliWiki.
DR GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF48; GLUTAMINASE 1; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Hydrolase; Reference proteome.
FT CHAIN 1..310
FT /note="Glutaminase 1"
FT /id="PRO_0000110607"
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"
FT MOD_RES 294
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313,
FT ECO:0000269|PubMed:18723842"
FT MUTAGEN 69
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 117
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 160
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 161
FT /note="E->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 162
FT /note="Q->A: No effect."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 168
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 192
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 244
FT /note="Y->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT MUTAGEN 260
FT /note="S->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18459799"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:1U60"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 202..213
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1U60"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1U60"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:1U60"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1U60"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:1U60"
SQ SEQUENCE 310 AA; 32903 MW; 4448BA0549E3C851 CRC64;
MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY
RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA
IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY
LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM
EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA
KQLGYNVFKG
//
