ASPG2_HAEIN
ID ASPG2_HAEIN Reviewed; 349 AA.
AC P43843;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable L-asparaginase periplasmic;
DE Short=L-ASNase;
DE EC=3.5.1.1;
DE AltName: Full=L-asparagine amidohydrolase;
DE Flags: Precursor;
GN Name=ansB; OrderedLocusNames=HI_0745;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP PROTEIN SEQUENCE OF 22-26.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
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: Periplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR EMBL; L42023; AAC22403.1; -; Genomic_DNA.
DR PIR; A64090; A64090.
DR RefSeq; NP_438904.1; NC_000907.1.
DR RefSeq; WP_005652322.1; NC_000907.1.
DR AlphaFoldDB; P43843; -.
DR SMR; P43843; -.
DR STRING; 71421.HI_0745; -.
DR EnsemblBacteria; AAC22403; AAC22403; HI_0745.
DR KEGG; hin:HI_0745; -.
DR PATRIC; fig|71421.8.peg.782; -.
DR eggNOG; COG0252; Bacteria.
DR HOGENOM; CLU_019134_1_2_6; -.
DR OMA; RKNHTSR; -.
DR PhylomeDB; P43843; -.
DR BioCyc; HINF71421:G1GJ1-783-MON; -.
DR Proteomes; UP000000579; Chromosome.
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 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 Direct protein sequencing; Disulfide bond; Hydrolase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10675023"
FT CHAIN 22..349
FT /note="Probable L-asparaginase periplasmic"
FT /id="PRO_0000002357"
FT DOMAIN 25..349
FT /note="Asparaginase/glutaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT ACT_SITE 35
FT /note="O-isoaspartyl threonine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT ECO:0000255|PROSITE-ProRule:PRU10100"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 112..113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 100..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 37212 MW; 45EA79CAC215F8A9 CRC64;
MKLTKLALCT LFGLGVSIAN AADLPNITIL ATGGTIAGSG QSSVNSAYKA GQLSIDTLIE
AVPEMKNIAN IKGEQIVKIG SQDMNDEVWL KLAKAINAQC KSTDGFVITH GTDTMEETAY
FLDLTVKCEK PVVLVGAMRP ATEKSADGPL NLYNAVVVAA DKKSSGRGVL VAMNNEVLGA
RDVTKTSTTA VQTFHSPNYG SLGYIHNSKV DYERSPESKH TINTPFNVEK LDSLPKVGII
YAYSNAPVEP LNALLNAGYQ GIVSAGVGNG NVNAAHLDRL EKAAKDSVVV VRSSRVPTGY
TTRDAEVDDS KYGFVASGTL NPQKARVLLQ LALTQTKDPK VIQQYFEDF
