ID A0A2T1DMP1_9CYAN Unreviewed; 303 AA.
AC A0A2T1DMP1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:PSB21768.1};
GN ORFNames=C7B65_03840 {ECO:0000313|EMBL:PSB21768.1};
OS Phormidesmis priestleyi ULC007.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Phormidesmis.
OX NCBI_TaxID=1920490 {ECO:0000313|EMBL:PSB21768.1, ECO:0000313|Proteomes:UP000238634};
RN [1] {ECO:0000313|EMBL:PSB21768.1, ECO:0000313|Proteomes:UP000238634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC007 {ECO:0000313|EMBL:PSB21768.1,
RC ECO:0000313|Proteomes:UP000238634};
RA Cohen D.B., Kent A.D.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB21768.1, ECO:0000313|Proteomes:UP000238634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULC007 {ECO:0000313|EMBL:PSB21768.1,
RC ECO:0000313|Proteomes:UP000238634};
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.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:PSB21768.1}.
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DR EMBL; PVWG01000002; PSB21768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1DMP1; -.
DR STRING; 1920490.GCA_001895925_01758; -.
DR OrthoDB; 9788822at2; -.
DR Proteomes; UP000238634; 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:UP000238634}.
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 303 AA; 32270 MW; 55A118EA0108209D CRC64;
MIGLDALAQD QLDAWVSDAK TKTQLGRLPD YIPLLTQTKP NTVAVEIQTT KGKIFSAGEV
TQPFALMSVI KPFLLLFVLE RSGADEVFKQ VGMKPSDQPF HSLTQLSSDR GYPRNPMINS
GAIALAALLP GKDGAARCKA LCDWLNRLAD THLTLDRAML TSVRSMANES NRAIAHMLSQ
AGHLTSVEMA LDTYNHICCL SGTVEDLARL GLLLASSSGI ARQHQQIVNA LMLTCGLYEA
SGAFAVRIGL PTKSGVSGAL LSIVPKEGAI AAYSPAIDPT GNSVAGLFLL EKLATHLKLS
IFG
//
