ID V3ZLC8_LOTGI Unreviewed; 526 AA.
AC V3ZLC8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=LOTGIDRAFT_133855 {ECO:0000313|EMBL:ESO83195.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO83195.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO83195.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
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DR EMBL; KB203771; ESO83195.1; -; Genomic_DNA.
DR RefSeq; XP_009066145.1; XM_009067897.1.
DR AlphaFoldDB; V3ZLC8; -.
DR STRING; 225164.V3ZLC8; -.
DR EnsemblMetazoa; LotgiT133855; LotgiP133855; LotgiG133855.
DR GeneID; 20233489; -.
DR KEGG; lgi:LOTGIDRAFT_133855; -.
DR CTD; 20233489; -.
DR HOGENOM; CLU_016439_1_0_1; -.
DR OMA; RWGNRPI; -.
DR OrthoDB; 537490at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
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: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; 1.
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:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 4..92
FT /note="Glutaminase EF-hand"
FT /evidence="ECO:0000259|Pfam:PF17959"
FT REPEAT 455..478
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 526 AA; 59546 MW; 5E76F1D035B35BEB CRC64;
MDDIEDRIFD SLCDSEQYLP ILKFKSQLRK AGLRETDPRL AETMKNLAQF QRSVAEMEGV
HSIHLDRDTF RKCVGDNIIL ISKAFHNNFI IPEFQTFCQS IDDLYWKVKS NTNGKVASYI
PQLARYSADF WGVSICTIDG QRYSIGDVNI PLCLQSISKP LTYALALNEH SPDLVHEYVG
HEPSGRQFNE IKLNADDKPH NPMINAGAIV LCSLLKQGSN LADRFDYTSE MFKKLAGNEH
ISFNNSVFLS ERETADRNFA LAYYLREYKC FPKGTHVMET LDFYFQLCSV EVTCQSGSVI
AASLANGGIC PITGERILNP YSVRNTLSLM HSCGMYDYSG QFAFDVGLPS KSGVSGGVML
VVPNVMGIFL WAPPLDIYGN SCKGIQFCEE LVDNFNFHNY DNLRYTQRKQ DPRLQKFTHR
ANSVVQLLFA AKNGDITALR RCYLSGLDMN LTDYDGRTAL HVASAEGHTE AVIFLLEKCK
VSPFECDRWD YTALDDAKKF HKTEVVTILE KYMSTNPKQQ DNSQQK
//