ID K8GK48_9CYAN Unreviewed; 308 AA.
AC K8GK48;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ORFNames=OsccyDRAFT_2669 {ECO:0000313|EMBL:EKQ68154.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ68154.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ68154.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ68154.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) 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:EKQ68154.1}.
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DR EMBL; AJUB01000011; EKQ68154.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GK48; -.
DR STRING; 864702.OsccyDRAFT_2669; -.
DR PATRIC; fig|864702.5.peg.2873; -.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_1_0_3; -.
DR Proteomes; UP000001332; 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; 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:UP000001332}.
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 123
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 198
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ SEQUENCE 308 AA; 33113 MW; FE6B985E6758A167 CRC64;
MQGFPLSTDS LTPATLEFWL DEARARAIAG RIPAYIPRLG IADRQWLAMQ FRLADGRQIQ
VGDTDRSFAL MSVIKPFVVL FLLEQFGSEV VFSTVGMLPS DQPFHSIEQL AADQGFPRNP
MINSGAIALA GRLPGETGER RCRALSDWLN VRSGAQLHLD EAMLASVRSV GNETNRAIAQ
MLAAAGYLDA IEVALDTYNQ ICCLSGTVDD LARLGLLLAS PHEKISVVNQ RTVNALMLTC
GLYEASGQFA VQIGLPAKSG VSGALLAVVP RYGAIACYSP ALDDTGNSIA GLFLLEKLTR
SLNLNIFG
//
