ID A0A226DZC7_FOLCA Unreviewed; 569 AA.
AC A0A226DZC7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=Fcan01_15224 {ECO:0000313|EMBL:OXA50400.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA50400.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA50400.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA50400.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA50400.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXA50400.1}.
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DR EMBL; LNIX01000009; OXA50400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226DZC7; -.
DR STRING; 158441.A0A226DZC7; -.
DR OMA; QFKECIA; -.
DR Proteomes; UP000198287; 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; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR041541; Glutaminase_EF-hand.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR Pfam; PF17959; EF-hand_14; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 138..236
FT /note="Glutaminase EF-hand"
FT /evidence="ECO:0000259|Pfam:PF17959"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 63601 MW; 2CEA14F4BB95C845 CRC64;
MPFAHPAIPN GSFSAASPTP SSSQTAARIL HLYDKVYETE NLREGEATRK TVTFKEDGAE
VDVEEDDMSS TRGGRLSIPT PTFDGRPEKQ RDRSASLVWV DFLTAPSDTS PFSTDDESDG
EESSTGRQYG TLKKSTRIDD AIFNQFSDGS DHILIGKFLA MLENAGLKRT DYRLHELFQS
LRRILKEQEA IHRGHMNDNF VGSIETLHIT RDVFQEVIIP NIFIISTAYR NHFIIPKFDL
FCQMVEDIFL DCKDITAGTV APYLNKLALV NPTCWGVSFC SIDGQRYSVG DSTMPVTLHA
LSKPLMYAYA LQEIGKVKVH KYVGQEPSGY RFNELVLDPE KRPHNPIINA GSLMIHALLQ
QFCHPELSSA ERFDETHRLF EKLSGGEYVG FSNGMFLNKR QASDRNWALV HFMKEHNCFP
PGIDLADVIE YYLQTSSMET TVDVLSVIAS TFANGGICPI TGQRVLSEEV VADVLSVMFS
CGMLEFSGKF AFRVGLPAKS SIAGVILLVI PNVGGFAVWS PPLDKFGNSV RGVEFCEKLV
KTFNFHCFDV DKRGKIDPTR RTYVIIITF
//
