ASPQ_PSES7
ID ASPQ_PSES7 Reviewed; 337 AA.
AC P10182;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 98.
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 Short=PGA;
GN Name=ansB;
OS Pseudomonas sp. (strain ATCC 29598 / 7A).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=313;
RN [1]
RP PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8068664; DOI=10.1021/bi00200a005;
RA Lubkowski J., Wlodawer A., Ammon H.L., Copeland T.D., Swain A.L.;
RT "Structural characterization of Pseudomonas 7A glutaminase-asparaginase.";
RL Biochemistry 33:10257-10265(1994).
RN [2]
RP PROTEIN SEQUENCE OF 1-26.
RX PubMed=619999; DOI=10.1021/bi00596a005;
RA Holcenberg J.S., Ericsson L., Roberts J.;
RT "Amino acid sequence of the diazooxonorleucine binding site of
RT Acinetobacter and Pseudomonas 7A glutaminase-asparaginase enzymes.";
RL Biochemistry 17:411-417(1978).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=9020792; DOI=10.1021/bi961979x;
RA Jakob C.G., Lewinski K., Lacount M.W., Roberts J., Lebioda L.;
RT "Ion binding induces closed conformation in Pseudomonas 7A glutaminase-
RT asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at
RT 1.7-A resolution.";
RL Biochemistry 36:923-931(1997).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 8-337 IN COMPLEXES WITH
RP 6-DIAZO-5-OXO-L-NORLEUCINE AND 5-DIAZO-4-OXO-L-NORVALINE, ACTIVE SITE, AND
RP SUBUNIT.
RX PubMed=10684596; DOI=10.1021/bi991797d;
RA Ortlund E., Lacount M.W., Lewinski K., Lebioda L.;
RT "Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues
RT of glutamine and asparagine result in unexpected covalent inhibitions and
RT suggests an unusual catalytic triad Thr-Tyr-Glu.";
RL Biochemistry 39:1199-1204(2000).
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:0000269|PubMed:10684596}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR PDB; 1DJO; X-ray; 2.00 A; A/B=8-337.
DR PDB; 1DJP; X-ray; 1.90 A; A/B=8-337.
DR PDB; 3PGA; X-ray; 2.00 A; 1/2/3/4=8-337.
DR PDB; 4PGA; X-ray; 1.70 A; A/B=1-337.
DR PDBsum; 1DJO; -.
DR PDBsum; 1DJP; -.
DR PDBsum; 3PGA; -.
DR PDBsum; 4PGA; -.
DR AlphaFoldDB; P10182; -.
DR SMR; P10182; -.
DR BRENDA; 3.5.1.38; 5085.
DR EvolutionaryTrace; P10182; -.
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; Direct protein sequencing; Hydrolase; Periplasm.
FT CHAIN 1..337
FT /note="Glutaminase-asparaginase"
FT /id="PRO_0000171089"
FT DOMAIN 10..337
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 20
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100,
FT ECO:0000269|PubMed:10684596"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100..101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 7
FT /note="Q -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 12
FT /note="V -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3PGA"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 56..65
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:1DJP"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4PGA"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:3PGA"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:3PGA"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3PGA"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:4PGA"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:4PGA"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:4PGA"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:4PGA"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 310..320
FT /evidence="ECO:0007829|PDB:4PGA"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4PGA"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:4PGA"
SQ SEQUENCE 337 AA; 36200 MW; 11DEEC467CB1475E CRC64;
KEVENQQKLA NVVILATGGT IAGAGASAAN SATYQAAKVG VDKLIAGVPE LADLANVRGE
QVMQIASESI TNDDLLKLGK RVAELADSND VDGIVITHGT DTLEETAYFL DLTLNTDKPI
VVVGSMRPGT AMSADGMLNL YNAVAVASNK DSRGKGVLVT MNDEIQSGRD VSKSINIKTE
AFKSAWGPLG MVVEGKSYWF RLPAKRHTVN SEFDIKQISS LPQVDIAYSY GNVTDTAYKA
LAQNGAKALI HAGTGNGSVS SRLTPALQTL RKTGTQIIRS SHVNQGGFVL RNAEQPDDKN
DWVVAHDLNP EKARILVELA MVKTQDSKEL QRIFWEY
