ID A0A2P8WGB3_9CYAN Unreviewed; 343 AA.
AC A0A2P8WGB3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:PSN18799.1};
GN ORFNames=C7271_10610 {ECO:0000313|EMBL:PSN18799.1};
OS filamentous cyanobacterium CCP5.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107701 {ECO:0000313|EMBL:PSN18799.1, ECO:0000313|Proteomes:UP000240885};
RN [1] {ECO:0000313|EMBL:PSN18799.1, ECO:0000313|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|EMBL:PSN18799.1,
RC ECO:0000313|Proteomes:UP000240885};
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|Proteomes:UP000240885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP5 {ECO:0000313|Proteomes:UP000240885};
RA Moore K., Momper L.;
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:PSN18799.1}.
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DR EMBL; PYEQ01000171; PSN18799.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8WGB3; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000240885; 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:UP000240885}.
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 343 AA; 37608 MW; FBC3E0C594FCFC65 CRC64;
MTNLGNMQSL TSSITAVTSP FRRYLSDLHE KYQAFDEGAV ADYIPELALA KPEWFGICVV
TKAGQVFEVG DCDQLFTIQS ISKPFVFGQA LEDHGREYVN SKVSVEPTGE AFNSIVLDEE
TNRPYNPMVN AGAIATTDLI KGANGTERLK RMLAMFKRYT GRDLDINVPV FLSEKATGFR
NRAMSYLMLN FDMVSDKIDE TLDLYFQQCS IMVNARDLAM LSATLANGGV NPVTQERALD
ERYVQDVISI MMTCGMYDGS GEWAYRVGMP AKSGVGGGIT AVALDKLGIG TFSPLLDAKG
NSARGIKVCK DLSQDFGLHS FNVATPEREL AGWIAGEEGL DDW
//
