ID   GLS2_CAEEL              Reviewed;         605 AA.
AC   Q19013;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 2.
DT   27-MAR-2024, entry version 161.
DE   RecName: Full=Putative glutaminase 2;
DE            Short=GLS;
DE            EC=3.5.1.2;
DE   AltName: Full=L-glutamine amidohydrolase;
GN   Name=glna-2; ORFNames=DH11.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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   -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
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DR   EMBL; Z49126; CAA88938.2; -; Genomic_DNA.
DR   PIR; T20384; T20384.
DR   RefSeq; NP_495675.1; NM_063274.3.
DR   AlphaFoldDB; Q19013; -.
DR   SMR; Q19013; -.
DR   BioGRID; 39614; 1.
DR   DIP; DIP-59881N; -.
DR   IntAct; Q19013; 1.
DR   STRING; 6239.DH11.1a.2; -.
DR   EPD; Q19013; -.
DR   PaxDb; 6239-DH11-1-2; -.
DR   PeptideAtlas; Q19013; -.
DR   EnsemblMetazoa; DH11.1a.1; DH11.1a.1; WBGene00008435.
DR   GeneID; 174282; -.
DR   KEGG; cel:CELE_DH11.1; -.
DR   UCSC; DH11.1.1; c. elegans.
DR   AGR; WB:WBGene00008435; -.
DR   WormBase; DH11.1a; CE28902; WBGene00008435; glna-2.
DR   eggNOG; KOG0506; Eukaryota.
DR   GeneTree; ENSGT00390000010463; -.
DR   HOGENOM; CLU_016439_1_0_1; -.
DR   InParanoid; Q19013; -.
DR   OMA; QFKECIA; -.
DR   OrthoDB; 537490at2759; -.
DR   PhylomeDB; Q19013; -.
DR   Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-CEL-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-CEL-8964539; Glutamate and glutamine metabolism.
DR   PRO; PR:Q19013; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00008435; Expressed in larva and 2 other cell types or tissues.
DR   ExpressionAtlas; Q19013; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; ISS:WormBase.
DR   GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006543; P:glutamine catabolic process; IBA:GO_Central.
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:SF7; GLUTAMINASE 2-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF17959; EF-hand_14; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
PE   3: Inferred from homology;
KW   ANK repeat; Hydrolase; Reference proteome; Repeat.
FT   CHAIN           1..605
FT                   /note="Putative glutaminase 2"
FT                   /id="PRO_0000110584"
FT   REPEAT          480..509
FT                   /note="ANK 1"
FT   REPEAT          513..543
FT                   /note="ANK 2"
FT   REGION          569..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         394
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         412
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   605 AA;  68336 MW;  CFBD8149DA535279 CRC64;
     MTSKPTTQKS VMYRIPSERT LESLHEMIGS RMSKMSLKNT LRGISNPYER DENEGSEDMI
     FELFKIPNKN EASIGKLLTV LRQLGLRDDD PRLVPMMEKI KDFEKIAEEK CSEATEQKHW
     KLTKEQFKEC IAPSIDIVSR ALQTDMVIPN WVTFVDQIRT LFNECKEIRE GQVATYIPQL
     ARQSPNLWAV SLCTVDGQRA SFGDVKHPFC VQSVSKAFNY AIVASDLGAD VVHSYVGQEP
     SGRLFNEICL DSTNKPHNPM VNSGAIVITS LIKSKTNMAD RFDFVLNQYR KIAGNEFIGF
     NNATFLSERA TADRNYALSY FMKENRCFPK ETESLTDALD FYFQLCSVEV TCESLAVMAS
     TLANGGVCPI TNETCVDPNP CRDVLSLMYS CGMYDASGQF SFNVGLPAKS GVSGAMIVVV
     PNVMGICLFS PPLDSLGNSC RGVAFCKKLV STFNFHNYDC LVHNSNIKSD PRRRDIRERD
     RLIPVFHVAR AGDLPTMRRL YMQGEDLNTS DHDDRTVLHI AATEGYETMI KFLVNVAKVD
     VDKKDRWGRT PLDEAKFFKH DHVSRFLEKA MKRPEQHRKD SVSSLDTDDE IDDDGFPEKP
     SFTID
//