ASPQ_ACIGL
ID ASPQ_ACIGL Reviewed; 331 AA.
AC P10172;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 100.
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;
GN Name=ansB;
OS Acinetobacter glutaminasificans.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=474;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3379033; DOI=10.1016/s0021-9258(18)68344-9;
RA Tanaka S., Robinson E.A., Appella E., Miller M., Ammon H.L., Roberts J.,
RA Weber I.T., Wlodawer A.;
RT "Structures of amidohydrolases. Amino acid sequence of a glutaminase-
RT asparaginase from Acinetobacter glutaminasificans and preliminary
RT crystallographic data for an asparaginase from Erwinia chrysanthemi.";
RL J. Biol. Chem. 263:8583-8591(1988).
RN [2]
RP PROTEIN SEQUENCE OF 1-60.
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 (2.9 ANGSTROMS).
RX PubMed=15299349; DOI=10.1107/s0907444994003446;
RA Lubkowski J., Wlodawer A., Housset D., Weber I.T., Ammon H.L., Murphy K.C.,
RA Swain A.L.;
RT "Refined crystal structure of Acinetobacter glutaminasificans glutaminase-
RT asparaginase.";
RL Acta Crystallogr. D 50:826-832(1994).
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.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR PIR; A28063; A28063.
DR PDB; 1AGX; X-ray; 2.90 A; A=1-331.
DR PDBsum; 1AGX; -.
DR AlphaFoldDB; P10172; -.
DR SMR; P10172; -.
DR SABIO-RK; P10172; -.
DR EvolutionaryTrace; P10172; -.
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 CDD; cd08964; L-asparaginase_II; 1.
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..331
FT /note="Glutaminase-asparaginase"
FT /id="PRO_0000171087"
FT DOMAIN 2..331
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 12
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 92..93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 128..139
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:1AGX"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1AGX"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1AGX"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:1AGX"
SQ SEQUENCE 331 AA; 35485 MW; 70F1BF823E9B0D31 CRC64;
KNNVVIVATG GTIAGAGASS TNSATYSAAK VPVDALIKAV PQVNDLANIT GIQALQVASE
SITDKELLSL ARQVNDLVKK PSVNGVVITH GTDTMEETAF FLNLVVHTDK PIVLVGSMRP
STALSADGPL NLYSAVALAS SNEAKNKGVM VLMNDSIFAA RDVTKGINIH THAFVSQWGA
LGTLVEGKPY WFRSSVKKHT NNSEFNIEKI QGDALPGVQI VYGSDNMMPD AYQAFAKAGV
KAIIHAGTGN GSMANYLVPE VRKLHDEQGL QIVRSSRVAQ GFVLRNAEQP DDKYGWIAAH
DLNPQKARLL MALALTKTND AKEIQNMFWN Y
