ASPG2_SCHPO
ID ASPG2_SCHPO Reviewed; 356 AA.
AC Q9UTS7;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable L-asparaginase 2;
DE EC=3.5.1.1;
DE AltName: Full=L-asparagine amidohydrolase 2;
DE Flags: Precursor;
GN ORFNames=SPAC977.12;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10712506; DOI=10.1091/mbc.11.3.873;
RA Albrecht E.B., Hunyady A.B., Stark G.R., Patterson T.E.;
RT "Mechanisms of sod2 gene amplification in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 11:873-886(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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: Secreted, cell wall {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR EMBL; AF192974; AAF13924.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB69634.1; -; Genomic_DNA.
DR PIR; T50284; T50284.
DR RefSeq; NP_592784.1; NM_001018184.2.
DR AlphaFoldDB; Q9UTS7; -.
DR SMR; Q9UTS7; -.
DR STRING; 4896.SPAC977.12.1; -.
DR SwissPalm; Q9UTS7; -.
DR MaxQB; Q9UTS7; -.
DR PaxDb; Q9UTS7; -.
DR EnsemblFungi; SPAC977.12.1; SPAC977.12.1:pep; SPAC977.12.
DR GeneID; 2543314; -.
DR KEGG; spo:SPAC977.12; -.
DR PomBase; SPAC977.12; -.
DR VEuPathDB; FungiDB:SPAC977.12; -.
DR eggNOG; KOG0503; Eukaryota.
DR HOGENOM; CLU_019134_1_2_1; -.
DR InParanoid; Q9UTS7; -.
DR OMA; AMNNQIN; -.
DR PhylomeDB; Q9UTS7; -.
DR PRO; PR:Q9UTS7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0009986; C:cell surface; NAS:PomBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; ISM:PomBase.
DR GO; GO:0006531; P:aspartate metabolic process; NAS:PomBase.
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; 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; PS51732; ASN_GLN_ASE_3; 1.
PE 3: Inferred from homology;
KW Cell wall; Glycoprotein; Hydrolase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..356
FT /note="Probable L-asparaginase 2"
FT /id="PRO_0000002364"
FT DOMAIN 36..356
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 46
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 126..127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 38115 MW; E7935A592DB2BFDA CRC64;
MWGFIVTCGI FLVLLCQLRL LSKRKSKSTP YNALLPNVTV FAMGGTIAGC ANSSLEIVNY
IPGSVGIEKL IEAVPAIKAI ANINGVQVTN MGSENLTPAD VLKLAKLILA EVAKPNVHGI
VITHGTDSLE ETAMFLDLTI STAKPIVVVG AMRPSTAIGA DGPMNLLNAV AVASSNQSMG
RGTLVLLNDR IGSAFYTTKT NGNTLDTFKS YEAGSLGIVL NQKPFYFFSP AVPTGKVFFD
IYNIKQLPRV DILYGYQGLN PKLAESAVHL GAKGLVLAAM GATSWTDDGN EVISSLIREH
NIPVVYSHRT AEGYSSNSCL GIPSYFLNPQ KARYMLMLAI SSGYSIRDIE DLFSIK
