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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   03-AUG-2022, entry version 154.
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., 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}.
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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; 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   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_027932_1_0_6; -.
DR   InParanoid; P77454; -.
DR   OMA; RNPMINS; -.
DR   PhylomeDB; P77454; -.
DR   BioCyc; EcoCyc:G6261-MON; -.
DR   BioCyc; MetaCyc:G6261-MON; -.
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; -; 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   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
 
 
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