ID A0A2T1M045_9CHRO Unreviewed; 342 AA.
AC A0A2T1M045;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Glutaminase {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918, ECO:0000256|HAMAP-Rule:MF_00313};
GN Name=glsA {ECO:0000256|HAMAP-Rule:MF_00313,
GN ECO:0000313|EMBL:PSF38058.1};
GN ORFNames=C7H19_06185 {ECO:0000313|EMBL:PSF38058.1};
OS Aphanothece hegewaldii CCALA 016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=2107694 {ECO:0000313|EMBL:PSF38058.1, ECO:0000313|Proteomes:UP000239001};
RN [1] {ECO:0000313|EMBL:PSF38058.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF38058.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSF38058.1, ECO:0000313|Proteomes:UP000239001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCALA 016 {ECO:0000313|EMBL:PSF38058.1,
RC ECO:0000313|Proteomes:UP000239001};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001062, ECO:0000256|HAMAP-
CC Rule:MF_00313};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|HAMAP-Rule:MF_00313}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076, ECO:0000256|HAMAP-Rule:MF_00313}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSF38058.1}.
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DR EMBL; PXOH01000005; PSF38058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1M045; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000239001; Unassembled WGS sequence.
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; 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:SF29; GLUTAMINASE; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00313};
KW Reference proteome {ECO:0000313|Proteomes:UP000239001}.
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 205
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 342 AA; 37816 MW; 64196FCF0C271998 CRC64;
MDNSGNLFSL ANSIHAVTSP FRNYLNELYE KYRSLNDGAV ADYIPELALA QPEWFGICVI
TSNGKIFEVG DCDKPFTIQS ISKAFVYGLA LEDHGREYVN GKVSVEPTGE AFNSIILDEK
TNRPYNPMVN AGAIATTDLI KGANTTERLK RLLEMFKRYT GRDHQINVPI FLSEKATGHR
NRAMAYLMLN FGMVSERIDE TLDLYFQQCS LLVTAKDLAM MGATLANGGI NPVTREKAID
EHYVQDVISV MLTCGMYDYS GEWVYRVGMP AKSGVGGGIT AVVPSKLGVG TFSPLLDAKG
NSTRGIKVCE DLSQDFGLHL FNVAKSERDL QAWIDGTNED EW
//
