ID A0A016S2H0_9BILA Unreviewed; 490 AA.
AC A0A016S2H0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN Name=Acey_s0315.g2274 {ECO:0000313|EMBL:EYB84507.1};
GN ORFNames=Y032_0315g2274 {ECO:0000313|EMBL:EYB84507.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB84507.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYB84507.1}.
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DR EMBL; JARK01001651; EYB84507.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016S2H0; -.
DR Proteomes; UP000024635; 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; 1.25.40.20; 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 NCBIfam; TIGR03814; Gln_ase; 1.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF7; GLUTAMINASE 2-RELATED; 1.
DR Pfam; PF12796; Ank_2; 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|PROSITE-ProRule:PRU00023};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635}.
FT REPEAT 389..411
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 447..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 54442 MW; 8C057F2D87C66E1F CRC64;
MLQSRCVACS LELVSQALQN NLVIPSWHTF VDQIRIFYQE CAEIRDGSVA TYIPQLARQS
PDQWGVSICT VDGQRVSFGD SKKPFCVQSV SKAFNYAIAA SDLGADYVHS YVGEEPSGRL
FNDICLDSRK KPHNPMVNSG AIIVTSLIKN TSNMADRFDY VITQYRKIAG GEYIGFNNAT
FLSERATADR NYALSYYMKE NKCFPPETTS LTDALDFYFQ LCSIEGNCES LSVMAATLAN
GGVCPITNEK CIDSNPCRDV LSLMYSCGMY DASGQFSFSV GLPAKSGVSG VMIVVVPNVM
GIALWSPALD GMGNSCRGVA FCKKLIAKFN FHNYDCLLHT TSNKVDPRRR DHRERECIVP
ALYVARSRDM VALRRLYMQG VDLSASDYDK RTPLHVAASE GDLTMLKFLV NVAKVDITAQ
DRWGRSPLDD ARFFKHQNCV QFLEKALSRP EGNRSQSVSS EDSEEEANAD YSERSDPPRA
VFTIDSMGNY
//
