ASPQ_PSEPK
ID ASPQ_PSEPK Reviewed; 362 AA.
AC Q88K39;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, 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=PP_2453;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN68065.1; -; Genomic_DNA.
DR RefSeq; NP_744601.1; NC_002947.4.
DR RefSeq; WP_010953400.1; NC_002947.4.
DR PDB; 6WYW; X-ray; 2.13 A; A/B/C/D=26-362.
DR PDB; 6WYX; X-ray; 1.48 A; A/B/C/D=26-362.
DR PDB; 6WYY; X-ray; 1.35 A; A/B/C/D=26-362.
DR PDB; 6WYZ; X-ray; 1.70 A; A/B/C/D=26-362.
DR PDB; 6WZ4; X-ray; 1.58 A; A/B/C/D=26-362.
DR PDB; 6WZ6; X-ray; 1.15 A; A/B/C/D=26-362.
DR PDB; 6WZ8; X-ray; 1.70 A; A/B/C/D=26-362.
DR PDBsum; 6WYW; -.
DR PDBsum; 6WYX; -.
DR PDBsum; 6WYY; -.
DR PDBsum; 6WYZ; -.
DR PDBsum; 6WZ4; -.
DR PDBsum; 6WZ6; -.
DR PDBsum; 6WZ8; -.
DR AlphaFoldDB; Q88K39; -.
DR SMR; Q88K39; -.
DR STRING; 160488.PP_2453; -.
DR DrugBank; DB04388; 4-Carboxy-4-Aminobutanal.
DR DrugBank; DB02571; Allysine.
DR EnsemblBacteria; AAN68065; AAN68065; PP_2453.
DR KEGG; ppu:PP_2453; -.
DR PATRIC; fig|160488.4.peg.2599; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_1_2_6; -.
DR OMA; RKNHTSR; -.
DR PhylomeDB; Q88K39; -.
DR BioCyc; PPUT160488:G1G01-2623-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004067; F:asparaginase activity; IEA:InterPro.
DR GO; GO:0050417; F:glutamin-(asparagin-)ase activity; IEA:UniProtKB-EC.
DR GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR GO; GO:0006528; P:asparagine metabolic process; IEA:InterPro.
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 3D-structure; Hydrolase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..362
FT /note="Glutaminase-asparaginase"
FT /id="PRO_0000002361"
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"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 81..90
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 97..111
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6WYY"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6WYY"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:6WZ6"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 261..268
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:6WZ6"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:6WZ6"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:6WZ6"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:6WZ6"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 335..345
FT /evidence="ECO:0007829|PDB:6WZ6"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:6WZ6"
FT HELIX 352..361
FT /evidence="ECO:0007829|PDB:6WZ6"
SQ SEQUENCE 362 AA; 38608 MW; C33F185DB17053F0 CRC64;
MNAALKTFAP SALALLLILP SSASAKEAET QQKLANVVIL ATGGTIAGAG ASAANSATYQ
AAKLGVDKLI AGVPELADIA NVRGEQVMQI ASESISNDDL LKLGKRVAEL AESKDVDGIV
ITHGTDTLEE TAFFLNLVEK TDKPIVVVGS MRPGTAMSAD GMLNLYNAVA VASDKQSRGK
GVLVTMNDEI QSGRDVSKAV NIKTEAFKSA WGPMGMVVEG KSYWFRLPAK RHTVNSEFDI
KQISSLPQVD IAYGYGNVTD TAYKALAQNG AKALIHAGTG NGSVSSRVVP ALQELRKNGV
QIIRSSHVNQ GGFVLRNAEQ PDDKNDWVVA HDLNPQKARI LAMVAMTKTQ DSKELQRIFW
EY
