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Database: UniProt/SWISS-PROT
Entry: GLSA1_ECOLI
LinkDB: GLSA1_ECOLI
Original site: GLSA1_ECOLI 
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   28-MAR-2018, entry version 130.
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; Proteobacteria; 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.,
RA   Mau B., 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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND IDENTIFICATION BY
RP   MASS 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,
RP   MUTAGENESIS OF LYS-69; ASN-117; SER-160; GLU-161; GLN-162; ASN-168;
RP   TYR-192; TYR-244 AND SER-260, 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.,
RA   Savchenko A., 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: L-glutamine + H(2)O = L-glutamate + NH(3).
CC       {ECO:0000255|HAMAP-Rule:MF_00313, 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}.
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_LN832404.1.
DR   PDB; 1U60; X-ray; 1.61 A; A/B/C/D=1-310.
DR   PDBsum; 1U60; -.
DR   ProteinModelPortal; P77454; -.
DR   SMR; P77454; -.
DR   BioGrid; 4261985; 19.
DR   DIP; DIP-11307N; -.
DR   IntAct; P77454; 3.
DR   STRING; 316385.ECDH10B_0442; -.
DR   DrugBank; DB01942; Formic Acid.
DR   iPTMnet; P77454; -.
DR   PaxDb; P77454; -.
DR   PRIDE; P77454; -.
DR   EnsemblBacteria; AAC73587; AAC73587; b0485.
DR   EnsemblBacteria; BAE76264; BAE76264; BAE76264.
DR   GeneID; 946187; -.
DR   KEGG; ecj:JW0474; -.
DR   KEGG; eco:b0485; -.
DR   PATRIC; fig|1411691.4.peg.1791; -.
DR   EchoBASE; EB3036; -.
DR   EcoGene; EG13247; glsA1.
DR   eggNOG; ENOG4105CSV; Bacteria.
DR   eggNOG; COG2066; LUCA.
DR   HOGENOM; HOG000216890; -.
DR   InParanoid; P77454; -.
DR   KO; K01425; -.
DR   OMA; MYTCGMY; -.
DR   PhylomeDB; P77454; -.
DR   BioCyc; EcoCyc:G6261-MONOMER; -.
DR   BioCyc; MetaCyc:G6261-MONOMER; -.
DR   BRENDA; 3.5.1.2; 2026.
DR   EvolutionaryTrace; P77454; -.
DR   PRO; PR:P77454; -.
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; IBA:GO_Central.
DR   GO; GO:0045926; P:negative regulation of growth; IMP:EcoliWiki.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR   GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
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; Acetylation; Complete proteome; Hydrolase;
KW   Reference proteome.
FT   CHAIN         1    310       Glutaminase 1.
FT                                /FTId=PRO_0000110607.
FT   BINDING      66     66       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     117    117       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     161    161       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     168    168       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     192    192       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     244    244       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313}.
FT   BINDING     262    262       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00313}.
FT   MOD_RES     294    294       N6-acetyllysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00313,
FT                                ECO:0000269|PubMed:18723842}.
FT   MUTAGEN      69     69       K->A: Loss of activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     117    117       N->A: Loss of activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     160    160       S->A: Loss of activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     161    161       E->A: Strongly reduced activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     162    162       Q->A: No effect.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     168    168       N->A: Loss of activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     192    192       Y->A: Loss of activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     244    244       Y->A: Loss of activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   MUTAGEN     260    260       S->A: Reduced activity.
FT                                {ECO:0000269|PubMed:18459799}.
FT   HELIX         4     18       {ECO:0000244|PDB:1U60}.
FT   HELIX        31     34       {ECO:0000244|PDB:1U60}.
FT   STRAND       42     47       {ECO:0000244|PDB:1U60}.
FT   STRAND       52     57       {ECO:0000244|PDB:1U60}.
FT   HELIX        65     67       {ECO:0000244|PDB:1U60}.
FT   HELIX        68     80       {ECO:0000244|PDB:1U60}.
FT   HELIX        82     88       {ECO:0000244|PDB:1U60}.
FT   HELIX       101    106       {ECO:0000244|PDB:1U60}.
FT   TURN        107    109       {ECO:0000244|PDB:1U60}.
FT   HELIX       117    126       {ECO:0000244|PDB:1U60}.
FT   HELIX       132    147       {ECO:0000244|PDB:1U60}.
FT   HELIX       155    162       {ECO:0000244|PDB:1U60}.
FT   HELIX       166    178       {ECO:0000244|PDB:1U60}.
FT   HELIX       185    195       {ECO:0000244|PDB:1U60}.
FT   STRAND      198    200       {ECO:0000244|PDB:1U60}.
FT   HELIX       202    213       {ECO:0000244|PDB:1U60}.
FT   STRAND      216    218       {ECO:0000244|PDB:1U60}.
FT   TURN        219    222       {ECO:0000244|PDB:1U60}.
FT   HELIX       228    230       {ECO:0000244|PDB:1U60}.
FT   HELIX       231    241       {ECO:0000244|PDB:1U60}.
FT   HELIX       244    246       {ECO:0000244|PDB:1U60}.
FT   HELIX       247    253       {ECO:0000244|PDB:1U60}.
FT   STRAND      258    260       {ECO:0000244|PDB:1U60}.
FT   STRAND      264    270       {ECO:0000244|PDB:1U60}.
FT   TURN        271    273       {ECO:0000244|PDB:1U60}.
FT   STRAND      274    279       {ECO:0000244|PDB:1U60}.
FT   HELIX       290    303       {ECO:0000244|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
//
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