GLSA_RHIEC
ID GLSA_RHIEC Reviewed; 309 AA.
AC O87405; Q2K7U5;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Thermolabile glutaminase;
DE EC=3.5.1.2;
DE AltName: Full=Glutaminase A;
GN Name=glsA; OrderedLocusNames=RHE_CH02311;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10095071; DOI=10.1016/s0167-4781(99)00026-3;
RA Calderon J., Huerta-Saquero A., Du Pont G., Duran S.;
RT "Sequence and molecular analysis of the Rhizobium etli glsA gene, encoding
RT a thermolabile glutaminase.";
RL Biochim. Biophys. Acta 1444:451-456(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251;
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN [3]
RP CHARACTERIZATION.
RX PubMed=9126674; DOI=10.1007/bf00570126;
RA Duran S., Sanchez-Linares L., Huerta-Saquero A., Du Pont G.,
RA Huerta-Zepeda A., Calderon J.;
RT "Identification of two glutaminases in Rhizobium etli.";
RL Biochem. Genet. 34:453-465(1996).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR EMBL; AF057158; AAC63991.1; -; Genomic_DNA.
DR EMBL; CP000133; ABC91091.1; -; Genomic_DNA.
DR RefSeq; WP_011425571.1; NC_007761.1.
DR AlphaFoldDB; O87405; -.
DR SMR; O87405; -.
DR STRING; 347834.RHE_CH02311; -.
DR EnsemblBacteria; ABC91091; ABC91091; RHE_CH02311.
DR GeneID; 61480721; -.
DR KEGG; ret:RHE_CH02311; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_5; -.
DR OMA; RPRNPFI; -.
DR Proteomes; UP000001936; Chromosome.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
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..309
FT /note="Thermolabile glutaminase"
FT /id="PRO_0000110619"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 94
FT /note="A -> T (in Ref. 1; AAC63991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 32987 MW; CC678FB5E6A048FD CRC64;
MADLQATLDS IYTDILPRIG EGKVADYIPE LAKIDPRQFG MAIVTVDGQV FRVGDADIAF
SIQSISKVFM LTLALGKVGE GLWKRVGREP SGSAFNSIVQ LEHESGIPRN PFINAGAIAV
TDVVMAGHAP REAIGELLRF VRYLADDESI TIDDKVARSE TQTGYRNVAL ANFMRAYRNL
DHPVDHVLGV YFHQCALAMS CEQLARAGLF LAARGSNPMT GHSVVSPKRA RRINALMLTC
GHYDGSGDFA YHVGLPGKSG VGGGIFAVAP GIASIAVWSP GLNKVGNSQL GAVALEMLAA
RTGWSVFGD