GLSA_VIBC3
ID GLSA_VIBC3 Reviewed; 306 AA.
AC A5F9H5; C3M4P5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Glutaminase {ECO:0000255|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00313};
GN Name=glsA {ECO:0000255|HAMAP-Rule:MF_00313};
GN OrderedLocusNames=VC0395_A0006, VC395_0498;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(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 -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000255|HAMAP-
CC Rule:MF_00313}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ21307.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ACP08517.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000627; ABQ21307.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001235; ACP08517.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000805055.1; NZ_JAACZH010000015.1.
DR AlphaFoldDB; A5F9H5; -.
DR SMR; A5F9H5; -.
DR STRING; 345073.VC395_0498; -.
DR EnsemblBacteria; ABQ21307; ABQ21307; VC0395_A0006.
DR KEGG; vco:VC0395_A0006; -.
DR KEGG; vcr:VC395_0498; -.
DR PATRIC; fig|345073.21.peg.485; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_1_6; -.
DR Proteomes; UP000000249; Chromosome 2.
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 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..306
FT /note="Glutaminase"
FT /id="PRO_0000336042"
FT BINDING 64
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 242
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00313"
SQ SEQUENCE 306 AA; 32757 MW; 88E3BA76C39D862B CRC64;
MKPTAEILAS IIEEVRPLTG QGKVADYIPA LAKVPSEKLG IAVFTNQGEV ISAGDAQEGF
SIQSISKVLS LTLAMGLYQP NELWSRVGKE PSGQAFNSLI QLEMEHGIPR NPFINAGAIV
VCDMLQSRLS APRQRLLEFV RQLSGEPLIA YDKVVAASEM MHSDRNAAIA YLMRSFGNFH
NEVIPVLHNY FHACALKMSC VELAKTFSYL ANKGVSVVTG ETVITPTQSK QTNALLATCG
LYDGAGEFAY RVGMPGKSGV GGGIIAVVPG EMTIAVWSPA LDQSGNSLAG TRALELLAQR
IGRSIF