ID A0A0S4XRH7_CAEEL Unreviewed; 346 AA.
AC A0A0S4XRH7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN Name=glna-2 {ECO:0000313|EMBL:CUV67068.1,
GN ECO:0000313|WormBase:DH11.1c};
GN ORFNames=CELE_DH11.1 {ECO:0000313|EMBL:CUV67068.1}, DH11.1
GN {ECO:0000313|WormBase:DH11.1c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CUV67068.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CUV67068.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CUV67068.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
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 Evidence={ECO:0000256|ARBA:ARBA00001062};
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
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DR EMBL; BX284602; CUV67068.1; -; Genomic_DNA.
DR RefSeq; NP_001305215.1; NM_001318286.1.
DR AlphaFoldDB; A0A0S4XRH7; -.
DR SMR; A0A0S4XRH7; -.
DR EnsemblMetazoa; DH11.1c.1; DH11.1c.1; WBGene00008435.
DR EnsemblMetazoa; DH11.1c.2; DH11.1c.2; WBGene00008435.
DR EnsemblMetazoa; DH11.1c.3; DH11.1c.3; WBGene00008435.
DR EnsemblMetazoa; DH11.1c.4; DH11.1c.4; WBGene00008435.
DR AGR; WB:WBGene00008435; -.
DR WormBase; DH11.1c; CE51167; WBGene00008435; glna-2.
DR OrthoDB; 537490at2759; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008435; Expressed in larva and 2 other cell types or tissues.
DR ExpressionAtlas; A0A0S4XRH7; baseline and differential.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
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 InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF7; GLUTAMINASE 2-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Proteomics identification {ECO:0007829|EPD:A0A0S4XRH7,
KW ECO:0007829|PeptideAtlas:A0A0S4XRH7};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT REGION 310..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 346 AA; 38909 MW; 6A3946E2BE2F87ED CRC64;
MVNSGAIVIT SLIKSKTNMA DRFDFVLNQY RKIAGNEFIG FNNATFLSER ATADRNYALS
YFMKENRCFP KETESLTDAL DFYFQLCSVE VTCESLAVMA STLANGGVCP ITNETCVDPN
PCRDVLSLMY SCGMYDASGQ FSFNVGLPAK SGVSGAMIVV VPNVMGICLF SPPLDSLGNS
CRGVAFCKKL VSTFNFHNYD CLVHNSNIKS DPRRRDIRER DRLIPVFHVA RAGDLPTMRR
LYMQGEDLNT SDHDDRTVLH IAATEGYETM IKFLVNVAKV DVDKKDRWGR TPLDEAKFFK
HDHVSRFLEK AMKRPEQHRK DSVSSLDTDD EIDDDGFPEK PSFTID
//