ID   F4BIL9_9GAMM            Unreviewed;       514 AA.
AC   F4BIL9;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
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   OrderedLocusNames=FN3523_0156 {ECO:0000313|EMBL:AEB28013.1};
OS   Francisella hispaniensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=622488 {ECO:0000313|EMBL:AEB28013.1, ECO:0000313|Proteomes:UP000008303};
RN   [1] {ECO:0000313|Proteomes:UP000008303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3523 {ECO:0000313|Proteomes:UP000008303};
RX   PubMed=21666011; DOI=10.1128/AEM.00337-11;
RA   Siddaramappa S., Challacombe J.F., Petersen J.M., Pillai S., Hogg G.,
RA   Kuske C.R.;
RT   "Common ancestry and novel genetic traits of Francisella novicida-like
RT   isolates from North America and Australia as revealed by comparative
RT   genomic analyses.";
RL   Appl. Environ. Microbiol. 77:5110-5122(2011).
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}.
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DR   EMBL; CP002558; AEB28013.1; -; Genomic_DNA.
DR   RefSeq; WP_014547492.1; NC_017449.1.
DR   AlphaFoldDB; F4BIL9; -.
DR   KEGG; fcn:FN3523_0156; -.
DR   PATRIC; fig|676032.3.peg.158; -.
DR   eggNOG; COG0666; Bacteria.
DR   eggNOG; COG2066; Bacteria.
DR   HOGENOM; CLU_016439_1_0_6; -.
DR   Proteomes; UP000008303; Chromosome.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   HAMAP; MF_00313; Glutaminase; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   InterPro; IPR041541; Glutaminase_EF-hand.
DR   NCBIfam; TIGR03814; Gln_ase; 1.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF17959; EF-hand_14; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|HAMAP-Rule:MF_00313};
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00313};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          19..94
FT                   /note="Glutaminase EF-hand"
FT                   /evidence="ECO:0000259|Pfam:PF17959"
FT   REPEAT          456..488
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         338
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
FT   BINDING         356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00313"
SQ   SEQUENCE   514 AA;  57257 MW;  90E01AB0E190D997 CRC64;
     MKTKLIRAGS TGKDYYTNIF NAICDKDGFL TKIDILAILD DAGIASDDPR TTKLRAEINK
     LTVIDKIDFK KFREMTSDST GIIEKAVNKG FIIPNFKDFR KEIEKIYEET KKNVSGKNAT
     YIPQLARVDS ELFAVAFCSV DGQMITLGDF EHPYCVQSTA KPITYCIATE ENGEDKVHKH
     VGREPSGITF NAIALNKYDR PHNPMINSGA IMMCSLIKPE WNLADRFEYI TNVWENLAGG
     ETIGFDNAVY HSEKETANRN YALAYFMKEV GAFPQNTNID TSLDFYFQTC SIQVNAKKMS
     KIMSSIANGG ICPFTHKKIF SPTTIRNCLS MMYSCGMYDF SGEYAFSVGL PAKSGVSGAL
     AIAIPNVGGF AIFSPRLDNN HNSVRGVEFS KRLVEKFSFH NYDHIAHCDK INPVEGRGTI
     DSNLTLELIW AASNGDLSEI KRAVALGVDI SKGDYDKRTA LHLAAAEGHE DIVKYLIRKG
     ANPNAKDRWN RTPLEDAIAN NHHHIARLLE KVSS
//