ASPQ_PSEAE
ID ASPQ_PSEAE Reviewed; 362 AA.
AC Q9I407;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Glutaminase-asparaginase;
DE EC=3.5.1.38;
DE AltName: Full=L-ASNase/L-GLNase;
DE AltName: Full=L-asparagine/L-glutamine amidohydrolase;
DE Flags: Precursor;
GN Name=ansB; OrderedLocusNames=PA1337;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 64-77; 84-105; 181-194; 209-221; 242-264 AND 317-337.
RC STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
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=3.5.1.38;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.38;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04726.1; -; Genomic_DNA.
DR PIR; C83478; C83478.
DR RefSeq; NP_250028.1; NC_002516.2.
DR RefSeq; WP_003104093.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I407; -.
DR SMR; Q9I407; -.
DR STRING; 287.DR97_457; -.
DR PaxDb; Q9I407; -.
DR PRIDE; Q9I407; -.
DR DNASU; 882207; -.
DR EnsemblBacteria; AAG04726; AAG04726; PA1337.
DR GeneID; 882207; -.
DR KEGG; pae:PA1337; -.
DR PATRIC; fig|208964.12.peg.1389; -.
DR PseudoCAP; PA1337; -.
DR HOGENOM; CLU_019134_1_2_6; -.
DR InParanoid; Q9I407; -.
DR OMA; RKNHTSR; -.
DR PhylomeDB; Q9I407; -.
DR BioCyc; PAER208964:G1FZ6-1363-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0050417; F:glutamin-(asparagin-)ase activity; IEA:UniProtKB-EC.
DR GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR GO; GO:0006530; P:asparagine catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1170; -; 1.
DR Gene3D; 3.40.50.40; -; 1.
DR InterPro; IPR004550; AsnASE_II.
DR InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR InterPro; IPR006034; Asparaginase/glutaminase-like.
DR InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR InterPro; IPR040919; Asparaginase_C.
DR InterPro; IPR027473; L-asparaginase_C.
DR InterPro; IPR027474; L-asparaginase_N.
DR InterPro; IPR037152; L-asparaginase_N_sf.
DR Pfam; PF00710; Asparaginase; 1.
DR Pfam; PF17763; Asparaginase_C; 1.
DR PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR PRINTS; PR00139; ASNGLNASE.
DR SMART; SM00870; Asparaginase; 1.
DR SUPFAM; SSF53774; SSF53774; 1.
DR TIGRFAMs; TIGR00520; asnASE_II; 1.
DR PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..362
FT /note="Glutaminase-asparaginase"
FT /id="PRO_0000002359"
FT DOMAIN 35..362
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 45
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125..126
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 38644 MW; 6158A98ADF981431 CRC64;
MKPLLHAFAP GVMALMLLLP QAAQAKEVAP QQKLSNVVIL ATGGTIAGAG ASAANSATYT
AAKVPVDQLL ASVPQLKDIA NVRGEQVFQI ASESFTNENL LELGKTVAKL ADSDDVDGIV
ITHGTDTLEE TAYFLTLVEH TEKPIVVVGS MRPGTAMSAD GMLNLYNAVA VAGDKSARGK
GVLITMNDEI LSGRDASKMV NIKTEAFKSP WGPLGMVVEG KSYWFRAPVK RHTVNSEFDI
KQISALAPVE IAYSYGNVSD TAYKALAQAG AKAIIHAGTG NGSVPARVVP TLQELRKQGV
QIIRSSHVNA GGFVLRNAEQ PDDKNDWIVA HDLNPQKARI LAAVAMTKTQ DSKELQRIFW
EY
