ID   A0A1S3G2N6_DIPOR        Unreviewed;       632 AA.
AC   A0A1S3G2N6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN   Name=Gls {ECO:0000313|RefSeq:XP_012883073.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883073.1};
RN   [1] {ECO:0000313|RefSeq:XP_012883073.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883073.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
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DR   RefSeq; XP_012883073.1; XM_013027619.1.
DR   AlphaFoldDB; A0A1S3G2N6; -.
DR   STRING; 10020.ENSDORP00000024324; -.
DR   GeneID; 105994187; -.
DR   KEGG; dord:105994187; -.
DR   CTD; 2744; -.
DR   InParanoid; A0A1S3G2N6; -.
DR   OrthoDB; 537490at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.238.210; -; 1.
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:SF49; GLUTAMINASE KIDNEY ISOFORM, MITOCHONDRIAL; 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   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          103..185
FT                   /note="Glutaminase EF-hand"
FT                   /evidence="ECO:0000259|Pfam:PF17959"
FT   REPEAT          548..570
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          28..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..632
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   632 AA;  69554 MW;  E696006535783DCE CRC64;
     MMRLRGSATL RDLLLRPPAP VCAALRRAQP LATSSSPSEI LQELGKGGPQ PQAGASPPAA
     PPAPAPAPKD SAGETDAFGN SEGKELAAAG ENKIKQGLLP SLEDLLFYTI AEGQEKIPVH
     KFITALKSTG LRTSDPRLKE CMDMLRLTLQ TTSDGVMLDK DLFKKCVQSN IVLLTQAFRR
     KFVIPDFMSF TSHIDELYES AKKQSGGKVA DYIPQLAKFS PDLWGVSVCT VDGQRHSIGD
     TKVPFCLQSC VKPLKYAIAV NDLGTEYVHR YVGKEPSGLR FNKLFLNEDD KPHNPMVNAG
     AIVVTSLIKQ GVNNAEKFDY VMQFLNKMAG NEYVGFSNAT FQSERESGDR NFAIGYYLKE
     KKCFPEGTDM VGILDFYFQL CSIEVTCESA SVMAATLANG GFCPITGERV LSPEAVRNTL
     SLMHSCGMYD FSGQFAFHVG LPAKSGVAGG ILLVVPNVMG MMCWSPPLDK MGNSVKGIHF
     CHDLVSLCNF HNYDNLRHFA KKLDPRREGG DQRVKSVINL LFAAYTGDVS ALRRFALSAM
     DMEQRDYDSR TALHVAAAEG HVEVVKFLLE ACKVNPFPKD RWNNTPMDEA LHFGHHDVFK
     ILQEYQVQYT PQGDSDNGKE NQTVHKNLDG LL
//