ASPG_WOLSU
ID ASPG_WOLSU Reviewed; 330 AA.
AC P50286;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=L-asparaginase;
DE Short=L-ASNase;
DE EC=3.5.1.1;
DE AltName: Full=L-asparagine amidohydrolase;
GN Name=ansA; Synonyms=ansB; OrderedLocusNames=WS0660;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (2.2
RP ANGSTROMS).
RX PubMed=8898907; DOI=10.1111/j.1432-1033.1996.0201t.x;
RA Lubkowski J., Palm G.J., Gilliland G.L., Derst C., Roehm K.H., Wlodawer A.;
RT "Crystal structure and amino acid sequence of Wolinella succinogenes L-
RT asparaginase.";
RL Eur. J. Biochem. 241:201-207(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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=3.5.1.1;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE09790.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X89215; CAA61503.1; -; Genomic_DNA.
DR EMBL; X83689; CAA58658.1; -; Genomic_DNA.
DR EMBL; BX571658; CAE09790.1; ALT_INIT; Genomic_DNA.
DR PIR; S74205; S74205.
DR RefSeq; WP_011138590.1; NC_005090.1.
DR PDB; 1WSA; X-ray; 2.20 A; A/B=1-330.
DR PDB; 5K3O; X-ray; 1.70 A; A/B/C/D=1-330.
DR PDB; 5K45; X-ray; 1.63 A; A/B/C/D=1-330.
DR PDB; 5K4G; X-ray; 1.60 A; A/B/C/D=1-330.
DR PDB; 5K4H; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-330.
DR PDB; 6RUD; X-ray; 1.70 A; A/B/C/D=3-330.
DR PDB; 6RUE; X-ray; 1.65 A; A/B/C/D=3-330.
DR PDB; 6RUF; X-ray; 2.00 A; A/B/C/D=3-330.
DR PDB; 6SYH; X-ray; 1.50 A; A/B=3-330.
DR PDBsum; 1WSA; -.
DR PDBsum; 5K3O; -.
DR PDBsum; 5K45; -.
DR PDBsum; 5K4G; -.
DR PDBsum; 5K4H; -.
DR PDBsum; 6RUD; -.
DR PDBsum; 6RUE; -.
DR PDBsum; 6RUF; -.
DR PDBsum; 6SYH; -.
DR AlphaFoldDB; P50286; -.
DR SMR; P50286; -.
DR STRING; 273121.WS0660; -.
DR PRIDE; P50286; -.
DR EnsemblBacteria; CAE09790; CAE09790; WS0660.
DR KEGG; wsu:WS0660; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_1_2_7; -.
DR OrthoDB; 1659551at2; -.
DR BRENDA; 3.5.1.1; 6642.
DR EvolutionaryTrace; P50286; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-EC.
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; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..330
FT /note="L-asparaginase"
FT /id="PRO_0000171086"
FT DOMAIN 4..330
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 14
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000305"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 121
FT /note="S -> P (in Ref. 1; CAA61503/CAA58658)"
FT /evidence="ECO:0000305"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:6RUE"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5K3O"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6RUE"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:6SYH"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5K4G"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6RUE"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 241..248
FT /evidence="ECO:0007829|PDB:6SYH"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 270..280
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6SYH"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:5K45"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:6SYH"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:6SYH"
SQ SEQUENCE 330 AA; 34856 MW; B706B41958E924CE CRC64;
MAKPQVTILA TGGTIAGSGE SSVKSSYSAG AVTVDKLLAA VPAINDLATI KGEQISSIGS
QEMTGKVWLK LAKRVNELLA QKETEAVIIT HGTDTMEETA FFLNLTVKSQ KPVVLVGAMR
SGSSMSADGP MNLYNAVNVA INKASTNKGV VIVMNDEIHA AREATKLNTT AVNAFASPNT
GKIGTVYYGK VEYFTQSVRP HTLASEFDIS KIEELPRVDI LYAHPDDTDV LVNAALQAGA
KGIIHAGMGN GNPFPLTQNA LEKAAKSGVV VARSSRVGSG STTQEAEVDD KKLGFVATES
LNPQKARVLL MLALTKTSDR EAIQKIFSTY
