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Database: UniProt
Entry: W5MBZ8_LEPOC
LinkDB: W5MBZ8_LEPOC
Original site: W5MBZ8_LEPOC 
ID   W5MBZ8_LEPOC            Unreviewed;       609 AA.
AC   W5MBZ8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005907.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000005907.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
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DR   EMBL; AHAT01018728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01018729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015199717.1; XM_015344231.1.
DR   AlphaFoldDB; W5MBZ8; -.
DR   STRING; 7918.ENSLOCP00000005907; -.
DR   Ensembl; ENSLOCT00000005915.1; ENSLOCP00000005907.1; ENSLOCG00000004907.1.
DR   GeneID; 102694598; -.
DR   CTD; 27165; -.
DR   eggNOG; KOG0506; Eukaryota.
DR   GeneTree; ENSGT00390000010463; -.
DR   HOGENOM; CLU_016439_1_0_1; -.
DR   InParanoid; W5MBZ8; -.
DR   OMA; CISARPC; -.
DR   OrthoDB; 537490at2759; -.
DR   Proteomes; UP000018468; Linkage group LG4.
DR   Bgee; ENSLOCG00000004907; Expressed in muscle tissue and 13 other cell types or 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; 1.10.238.210; -; 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:SF33; GLUTAMINASE LIVER 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:UP000018468};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          81..163
FT                   /note="Glutaminase EF-hand"
FT                   /evidence="ECO:0000259|Pfam:PF17959"
FT   REPEAT          526..546
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          587..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..609
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   609 AA;  67716 MW;  7718F80A58A90B58 CRC64;
     MHCFRLLRAT HAGVRDVLVR DVFPKGAGAP GICRGSLFRR RRPGRQFCTG SASHLQQNAV
     DRDHAPWQRG ASKKGQFLGL EDLLFYTITE GEEQIPVARF IAALKSRGLW TSDPRLRDCM
     DLLRQSVQDT VGGSMMDREL FRKCVGSNIV LLTQAFRNKF VIPDFESFTA HINQLYRNAQ
     AQTIGKVADY IPQLAKFSPD LWGVSLCTVD GQRHSVGDTK VPFCLQSCVK PLEYAIALHE
     AGTERVHRYV GKEPSGLKFN KLFLNEEDKP HNPMVNAGAI VISSLIKPGS NKAEKFDCVM
     EFLMKMAGRE FVGFSNATFQ SEKETGDRNF AIGYYLKEKK CFPSGVDMIA ALDFYFQLCS
     IEVTCESGSV MAATLANGGI CPITGERVLS AEAVRNTLSL MHSCGMYDFS GQFAFHVGLP
     AKSGVSGAVL LVVPNVMGLM CWSPPLDKVG NSVRGIHFCQ ELVSLFNFHN YDNLRHFAKK
     LDPRREPGDV RNKSVVNLLF AAYSGDVSAL RRFALSATNM EQKDYDSRTA LHVAAAEGHV
     EVVLFLTDTC KVNPFVKDRW GNIPLDDAVQ FGHEAVVKVL KEYQQHYSPR EPNSEAEDRG
     KLETLEGMV
//
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