ID A0A3B4FXE0_9CICH Unreviewed; 578 AA.
AC A0A3B4FXE0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000015272.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000015272.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A3B4FXE0; -.
DR STRING; 303518.ENSPNYP00000015272; -.
DR Ensembl; ENSPNYT00000015661.1; ENSPNYP00000015272.1; ENSPNYG00000011543.1.
DR GeneTree; ENSGT00390000010463; -.
DR Proteomes; UP000261460; Unplaced.
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:SF52; GLUTAMINASE; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 64..146
FT /note="Glutaminase EF-hand"
FT /evidence="ECO:0000259|Pfam:PF17959"
FT REPEAT 497..519
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 557..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 64797 MW; 1377B70761BAF65A CRC64;
MKQSTERRLL FSSCFQEALA CTGEQSSNCR WTEPSVREDF YRDKCRQTRC SRQRRNAGIL
PSLEDLLFYT VAEGQETIPA HKFLTALKAT GLRSGDPRLK ECMETLKETL KKTSDGVTLD
RHLFKKCVQS NIVLLTQAFR KKFVIPDFQS FTSHIDELYE NAKNLTGGQV ADYIPQLAKF
SPDLWAVSLC TVDGQRHTVG DTKVPFCMQS CVKPLKYAVA VHDHSTEYVH SFIGKEPSGL
RFNKLFLNED DKPHNPMVNA GAIVCTSLIK VKAVTLRPPP LCCSSLCDRF QSERESGDRN
FAIGYYLKEK KCFPEGTDMT SVLDLYFQLC SIEVTCESAS VMAATLANGG ICPITGERVL
SPEAVRNTLS LMHSCGMYDF SGQFAFHVGL PAKSGVSGGI LLVVPNVMGI VCWSPPLDKL
GNSVRGIQFC TDLVELFNFH NYDNLRHFAK KHDPRREGGD QRAKSVINLL FSAYTGDVSA
LRRFALSSMD MEQRDYDSRT ALHVAAAEGH IEVVRFLLEA CKVNPVPRDR WGNTPMDEAV
HFGHHDVVTM LQQYHEKYSP PSDDEHKTSP EKSLDSLL
//
