ID   GLS3_CAEEL              Reviewed;         583 AA.
AC   Q93650; Q95QP4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Putative glutaminase 3;
DE            Short=GLS;
DE            EC=3.5.1.2;
DE   AltName: Full=L-glutamine amidohydrolase;
GN   Name=glna-3; ORFNames=F30F8.2;
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; Z81073; CAB03030.2; -; Genomic_DNA.
DR   EMBL; Z79752; CAB03030.2; JOINED; Genomic_DNA.
DR   PIR; T21575; T21575.
DR   RefSeq; NP_492162.1; NM_059761.3.
DR   AlphaFoldDB; Q93650; -.
DR   SMR; Q93650; -.
DR   STRING; 6239.F30F8.2; -.
DR   EPD; Q93650; -.
DR   PaxDb; Q93650; -.
DR   PeptideAtlas; Q93650; -.
DR   PRIDE; Q93650; -.
DR   EnsemblMetazoa; F30F8.2.1; F30F8.2.1; WBGene00009271.
DR   GeneID; 172547; -.
DR   KEGG; cel:CELE_F30F8.2; -.
DR   UCSC; F30F8.2; c. elegans.
DR   CTD; 172547; -.
DR   WormBase; F30F8.2; CE28553; WBGene00009271; glna-3.
DR   eggNOG; KOG0506; Eukaryota.
DR   GeneTree; ENSGT00390000010463; -.
DR   HOGENOM; CLU_016439_1_0_1; -.
DR   InParanoid; Q93650; -.
DR   OMA; QYFKRFA; -.
DR   OrthoDB; 349094at2759; -.
DR   PhylomeDB; Q93650; -.
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:Q93650; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00009271; Expressed in adult organism and 4 other tissues.
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; 1.25.40.20; -; 1.
DR   Gene3D; 3.40.710.10; -; 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   PANTHER; PTHR12544; PTHR12544; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF17959; EF-hand_14; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
PE   3: Inferred from homology;
KW   ANK repeat; Hydrolase; Reference proteome; Repeat.
FT   CHAIN           1..583
FT                   /note="Putative glutaminase 3"
FT                   /id="PRO_0000110585"
FT   REPEAT          482..514
FT                   /note="ANK 1"
FT   REPEAT          515..548
FT                   /note="ANK 2"
FT   REPEAT          549..581
FT                   /note="ANK 3"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         216
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         344
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         396
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         414
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   583 AA;  66361 MW;  C09BC143CCEF9198 CRC64;
     MDNKEKEDEE LSDELKDQPG PSEKPRTPTV VAFTKPSFYR VNTVISDVKV CRSMSYDMCG
     NHQQELLFDL YKDETTGKVY LPRFFKALLE SGIRKDDPRI DKMIQNIKDA DLLDDFVWGT
     QHIYLEKDTF KRYIGSSIGV VTKALKKQMI IPDWERFVSD MGEIFEDVRS HNEGDLATYI
     PQLSRVAPDS WAMSVCTIDG QRKMWGDALK PFCLQSVSKP FTYALVHDDI GPEELHAHVG
     QEPSGRLFND ISLDHNKKPH NPLINAGAIV VASLLKNKLP LADRFDFMIH ACRKFVGSGY
     IGFDNSVFLS ERETADRNYA LSYYMREHKV FPKDLNLQDT LDLYFQICSI ETNCDSLAVM
     AATLANGGVN PMNGERIVNN RACRDTLSLM YSCGMYDWSG QFAFHVGLPA KSGVSGDMII
     VIPNVMGIAL YSPRLDKLGN TVRGVKFAEQ LVQKYNFHNY DSLIYSDNKK IDPRRQLKDD
     HDGQNRFMYA TKLGDIAAIK RFLLMGHDIH CKDYDDRTVL HVAAAEGDVV TLEYVLSKWQ
     EDPNPCDRYD RTPLDDAKHF NHTACVKLLE EAITVYNLKG QDD