ID A0A0B1TIH9_OESDE Unreviewed; 407 AA.
AC A0A0B1TIH9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=OESDEN_02649 {ECO:0000313|EMBL:KHJ97368.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ97368.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ97368.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ97368.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) 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 -!- SIMILARITY: Belongs to the glutaminase family.
CC {ECO:0000256|ARBA:ARBA00011076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KN549464; KHJ97368.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1TIH9; -.
DR Proteomes; UP000053660; 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 InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR PANTHER; PTHR12544; GLUTAMINASE; 1.
DR PANTHER; PTHR12544:SF7; GLUTAMINASE 2-RELATED; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF04960; Glutaminase; 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:UP000053660};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..407
FT /note="glutaminase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002062634"
FT REPEAT 368..390
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 407 AA; 44778 MW; FDB7F98F1C7B3E21 CRC64;
MELWQAIFLS LLVSRLNIGA SPYAPWMGSA KGLQVSFGDA KMSFCVQSVS KAFNYAIAAS
DLGADYVHTY VGEEPSGQLF NEICLDSNRK PHNPMVNSGA IIITSLIKNT IDTADRFDYV
SCSVLVTFTA KMSSNTLKVI TQYRKIAGGE YIGFNNATFL SERITADRNY ALAYYMKENK
CFPPETTSLN DALDFYFQLC SIEGNCESLS VMAATLANGG VCPITEEKCI DSNPCRDVLS
LMYSCGMYDA SGQFSFSVGL PAKSGVSGVM IVVVPNVMGI ALWSPPLDQM GNSSRGVAFC
KKLISKFNFH NYDCLLHTTS SKVDPRRRDL HREQECIAPA LYVVRSRDMV ALRRMFMQGY
DLSASDYDKR APLHVAASEG DVGIVKFLVN VAKVDVTAKD RCFSDFP
//
