ID A0A076H3M5_9SYNE Unreviewed; 554 AA.
AC A0A076H3M5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=KR100_11395 {ECO:0000313|EMBL:AII43961.1};
OS Synechococcus sp. KORDI-100.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1280380 {ECO:0000313|EMBL:AII43961.1, ECO:0000313|Proteomes:UP000028591};
RN [1] {ECO:0000313|EMBL:AII43961.1, ECO:0000313|Proteomes:UP000028591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KORDI-100 {ECO:0000313|EMBL:AII43961.1,
RC ECO:0000313|Proteomes:UP000028591};
RA Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT "Genome sequence of Synechococcus sp. KORDI-100.";
RL Submitted (JUN-2013) 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};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
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DR EMBL; CP006269; AII43961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A076H3M5; -.
DR STRING; 1280380.KR100_11395; -.
DR KEGG; synk:KR100_11395; -.
DR eggNOG; COG0664; Bacteria.
DR eggNOG; COG2066; Bacteria.
DR HOGENOM; CLU_027932_3_1_3; -.
DR Proteomes; UP000028591; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR018490; cNMP-bd_dom_sf.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR Pfam; PF01740; STAS; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF52091; SpoIIaa-like; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000028591}.
FT DOMAIN 295..356
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 415..518
FT /note="Cyclic nucleotide-binding"
FT /evidence="ECO:0000259|PROSITE:PS50042"
SQ SEQUENCE 554 AA; 61046 MW; 8E45CB4C685F449C CRC64;
MGDTAKDFTI QSISKPFAFG LALKLLSSDH MLAKVGVEPS GDAFNAISLH PVTGIPRNPM
INAGAIATTA LIWAHDPERA ESLLLDFLSD MAGTPKRLSV DEDVFRSERD TGHRNRAIGY
LLRNSDVITS SPEQALDLYF RECSVSVSCR DLAVMAATLA CQGRNPITNV VGLDAMCNTD
VLAVMGSCGM YDYTGQWLYN VGMPAKSGVG GGVMAVVPGR LGIAVYSPPL DTYGNSCRGI
AVCEELSKRL ELHLFDQPNR GGMVIRSSTS GQKRYSRRWR SKVDFDLLKE HGERIKVLQV
QGVLDFAAVE ELLAHLEGST TNESFVVLDL AQVLALPEVS VQLLRDALSN LQKQGICCLA
CRGEHLKNFW PTEESEAAGW FESLDRALET VENRLLEQLH RTQVGERLPH NSITLLADLG
EQTRTRLMPL LERRHYNTND LLCRKGDAGS ELFLVETGLI SAGIESSTRS KRIRFATFSS
GVCIGEIAFL NNLPRTADLV ADEDSTCLVL HRDTFEQLQH EEPDVAIDII LALHRDLARK
VDRANQQLSL LKQR
//