ASPG_DEIRA
ID ASPG_DEIRA Reviewed; 322 AA.
AC Q9RRX9;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable L-asparaginase;
DE Short=L-ASNase;
DE EC=3.5.1.1;
DE AltName: Full=L-asparagine amidohydrolase;
GN Name=ansA; OrderedLocusNames=DR_2353;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF11899.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000513; AAF11899.1; ALT_INIT; Genomic_DNA.
DR PIR; G75283; G75283.
DR RefSeq; NP_296074.1; NC_001263.1.
DR RefSeq; WP_034350512.1; NC_001263.1.
DR AlphaFoldDB; Q9RRX9; -.
DR SMR; Q9RRX9; -.
DR STRING; 243230.DR_2353; -.
DR EnsemblBacteria; AAF11899; AAF11899; DR_2353.
DR KEGG; dra:DR_2353; -.
DR PATRIC; fig|243230.17.peg.2587; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_1_0_0; -.
DR InParanoid; Q9RRX9; -.
DR OMA; RKNHTSR; -.
DR OrthoDB; 1659551at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0006530; P:asparagine catabolic process; IBA:GO_Central.
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 PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..322
FT /note="Probable L-asparaginase"
FT /id="PRO_0000171078"
FT DOMAIN 6..320
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT REGION 13..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 16
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 33807 MW; 0339A30B5A7E130E CRC64;
MPASLPRLAL IHTGGTIASR PSPDGRGLTP QTPPALPGLE GVQVSEHQPF NLPSPHVTPA
HMQQLAHLIE QLAGGHDAVV VTHGTDTLEE TAFFLHLCLP AGLPVVLTGS MRHAEEVSWD
GPGNLLDAAQ VALCPQTAGR GPLVVFGGDI FDARTVTKVH TSAVDAFGGY PGPIGRIDRT
AAGPQVHYFA RPEPRPTFRP VTLERRVEIL YAYAGWQGEG YAGALERADG LVIAALGTGN
LPPELLPLIA ATDKPVVLAT RTHAGPILPV YGYAGGGATL VEAGAIPASF LNAHKARLLL
LVLLNLGASR EDIRRVFTQG VF
