ID A0A0N5CGC7_STREA Unreviewed; 681 AA.
AC A0A0N5CGC7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
OS Strongyloides papillosus (Intestinal threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=174720 {ECO:0000313|Proteomes:UP000046392, ECO:0000313|WBParaSite:SPAL_0001690500.1};
RN [1] {ECO:0000313|WBParaSite:SPAL_0001690500.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) 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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
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DR AlphaFoldDB; A0A0N5CGC7; -.
DR STRING; 174720.A0A0N5CGC7; -.
DR WBParaSite; SPAL_0001690500.1; SPAL_0001690500.1; SPAL_0001690500.
DR Proteomes; UP000046392; 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: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; 3.
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; 2.
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 86..174
FT /note="Glutaminase EF-hand"
FT /evidence="ECO:0000259|Pfam:PF17959"
FT REPEAT 506..538
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 539..563
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 681 AA; 76920 MW; 7C6575AF6FDC7A19 CRC64;
MKDLAEYQKD SSSFSESPTD TIISQILERS HSMTSITSTS EEYRHSEQTL KAIGDILNRK
HSVAQILNET MEGLNHSYEF KKSSQEDLIF ELFRIRSTEE ASMGKLISVL KSFGIRDDDP
RMKQTIEKMM LYEQESGDDC DTRHNRLSRE KFKICIQPSI ALISQALRNQ LVIPNWSEFI
KRIKDIFDSL KNETDGKVAT YIPQLARQSP NRWGMSICTI DGQRYSLGDS KSAFCFQSVS
KAFNYAIAAS DVGADVVHSY VGHEPSGRLF NEICLDNQGK PHNPMINAGA IIVTSLLKRE
LSMADRYDFV LDQYRKLAGG GYIGFNNATF LSERATADRN YSLSYYMKEN GCFPKEMTNL
TETLDLYFQL CSLETNCDSA AVMAATLANG GVCPLTYKKC VESRPCRDVL SLMYSCGMYD
YSGQFSFHVG LPAKSGVSGA MIVVIPNLMG ICLWSPPLDR LGNTVRGVKF CQRLIETFNF
HNYDSLLHTD EKKIDPRRRV GNKDTDLVVS LLYAAKNGEI QTVRRLYLQG ANLNMSDYDG
RTALHLAACE GHPNLVKFLL TVGKVNHASQ DRWGRTPYDE AKAFGKEECA KILYTYSTRR
RKTITRETTV DAVIHEERND DIITTTELND TIRNTDSDSG GTSEQDEDHN GLSMLNDISE
ESSDNYHRRQ SIVIRSYSLD E
//
