ID A0A067GCN1_CITSI Unreviewed; 247 AA.
AC A0A067GCN1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN ORFNames=CISIN_1g024993mg {ECO:0000313|EMBL:KDO73227.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO73227.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO73227.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-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 PdxT/SNO family.
CC {ECO:0000256|ARBA:ARBA00008345}.
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DR EMBL; KK784886; KDO73227.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067GCN1; -.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:InterPro.
DR CDD; cd01749; GATase1_PB; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01615; PdxT; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002161; PdxT/SNO.
DR InterPro; IPR021196; PdxT/SNO_CS.
DR NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR Pfam; PF01174; SNO; 1.
DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS01236; PDXT_SNO_1; 1.
DR PROSITE; PS51130; PDXT_SNO_2; 1.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT ACT_SITE 78
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT ACT_SITE 192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 192
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT BINDING 46..48
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 108
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 142..143
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
SQ SEQUENCE 247 AA; 26387 MW; E806945439DD4A70 CRC64;
MVVGVLALQG SFNEHIAALK RLGVKGVEIR KPDQLQNVSS LIIPGGESTT MARLAEYHNL
FPALREFVKM GKPVWGTCAG LIFLANKAVG QKLGGQELVG GLDCTVHRNF FGSQIQSFEA
ELSVPALASQ EGGPETFRGV FIRAPAVLDV GPDVDVLADY PVPSNKENAM PEKKVIVAVR
QGNLLGTAFH PELTADTRWH SYFLKMMSEV GEGTSSGGKG TSSGIVVVGG ENLGFNQQPK
IDLPIFQ
//
