ASPG_ELIMR
ID ASPG_ELIMR Reviewed; 340 AA.
AC Q47898;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase;
DE EC=3.5.1.26;
DE AltName: Full=Aspartylglucosaminidase;
DE Short=AGA;
DE AltName: Full=Glycosylasparaginase;
DE AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
DE Contains:
DE RecName: Full=Glycosylasparaginase alpha chain;
DE Contains:
DE RecName: Full=Glycosylasparaginase beta chain;
DE Flags: Precursor;
OS Elizabethkingia miricola (Chryseobacterium miricola).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=172045;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 33958;
RX PubMed=7840643; DOI=10.1006/abbi.1995.1053;
RA Tarentino A.L., Quinones G., Hauer C.R., Changchien L.-M.,
RA Plummer T.H. Jr.;
RT "Molecular cloning and sequence analysis of Flavobacterium meningosepticum
RT glycosylasparaginase: a single gene encodes the alpha and beta subunits.";
RL Arch. Biochem. Biophys. 316:399-406(1995).
RN [2]
RP PROTEIN SEQUENCE OF 46-59 AND 197-211.
RX PubMed=8250923; DOI=10.1006/bbrc.1993.2457;
RA Tarentino A.L., Plummer T.H. Jr.;
RT "The first demonstration of a procaryotic glycosylasparaginase.";
RL Biochem. Biophys. Res. Commun. 197:179-186(1993).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS).
RX PubMed=9541410; DOI=10.1002/pro.5560070327;
RA Xuan J., Tarentino A.L., Grimwood B.G., Plummer T.H. Jr., Cui T., Guan C.,
RA van Roey P.;
RT "Crystal structure of glycosylasparaginase from Flavobacterium
RT meningosepticum.";
RL Protein Sci. 7:774-781(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), ACTIVE SITE, AND SUBUNIT.
RX PubMed=9685368; DOI=10.1074/jbc.273.32.20205;
RA Guo H.C., Xu Q., Buckley D., Guan C.;
RT "Crystal structures of Flavobacterium glycosylasparaginase. An N-terminal
RT nucleophile hydrolase activated by intramolecular proteolysis.";
RL J. Biol. Chem. 273:20205-20212(1998).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 47-340, ACTIVE SITE, CLEAVAGE BY
RP AUTOCATALYSIS, MUTAGENESIS OF THR-197, AND SUBUNIT.
RX PubMed=10490104; DOI=10.1016/s0092-8674(00)80052-5;
RA Xu Q., Buckley D., Guan C., Guo H.C.;
RT "Structural insights into the mechanism of intramolecular proteolysis.";
RL Cell 98:651-661(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT CYS-197 IN COMPLEX WITH
RP SUBSTRATE, ACTIVE SITE, CLEAVAGE BY AUTOCATALYSIS, SUBUNIT, AND MUTAGENESIS
RP OF THR-197.
RX PubMed=17157318; DOI=10.1016/j.jmb.2006.09.051;
RA Wang Y., Guo H.C.;
RT "Crystallographic snapshot of a productive glycosylasparaginase-substrate
RT complex.";
RL J. Mol. Biol. 366:82-92(2007).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 46-340 OF MUTANT CYS-197, ACTIVE
RP SITE, CLEAVAGE BY AUTOCATALYSIS, AND SUBUNIT.
RX PubMed=20800597; DOI=10.1016/j.jmb.2010.08.038;
RA Wang Y., Guo H.C.;
RT "Crystallographic snapshot of glycosylasparaginase precursor poised for
RT autoprocessing.";
RL J. Mol. Biol. 403:120-130(2010).
CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC the peptide of asparagine-linked glycoproteins. Requires that the
CC glycosylated asparagine moiety is not substituted on its N-(R1) and
CC C- (R2) terminus.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+)
CC + L-aspartate + N-acetyl-beta-D-glucosaminylamine;
CC Xref=Rhea:RHEA:11544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15947, ChEBI:CHEBI:29991, ChEBI:CHEBI:58080; EC=3.5.1.26;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000269|PubMed:10490104,
CC ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597,
CC ECO:0000269|PubMed:9685368}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme. The N-terminal residue of the beta subunit is
CC responsible for the nucleophile hydrolase activity.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; U08028; AAA68868.1; -; Genomic_DNA.
DR PIR; S69194; S69194.
DR PDB; 1AYY; X-ray; 2.32 A; A/C=46-196, B/D=197-340.
DR PDB; 1P4K; X-ray; 1.90 A; A/C=46-340.
DR PDB; 1P4V; X-ray; 1.90 A; A/C=46-340.
DR PDB; 2GAC; X-ray; 2.10 A; A/C=46-196, B/D=198-340.
DR PDB; 2GAW; X-ray; 2.20 A; A/C=46-196, B/D=197-340.
DR PDB; 2GL9; X-ray; 2.00 A; A/C=46-196, B/D=197-340.
DR PDB; 3LJQ; X-ray; 1.90 A; A/C=46-340.
DR PDB; 4R4Y; X-ray; 2.10 A; A/B=46-340.
DR PDB; 5V2I; X-ray; 1.83 A; A/B=46-340.
DR PDB; 9GAA; X-ray; 2.10 A; A/C=46-340.
DR PDB; 9GAC; X-ray; 1.90 A; A/C=46-340.
DR PDB; 9GAF; X-ray; 1.90 A; A/C=46-340.
DR PDBsum; 1AYY; -.
DR PDBsum; 1P4K; -.
DR PDBsum; 1P4V; -.
DR PDBsum; 2GAC; -.
DR PDBsum; 2GAW; -.
DR PDBsum; 2GL9; -.
DR PDBsum; 3LJQ; -.
DR PDBsum; 4R4Y; -.
DR PDBsum; 5V2I; -.
DR PDBsum; 9GAA; -.
DR PDBsum; 9GAC; -.
DR PDBsum; 9GAF; -.
DR AlphaFoldDB; Q47898; -.
DR SMR; Q47898; -.
DR DIP; DIP-61331N; -.
DR STRING; 172045.KS04_17310; -.
DR MEROPS; T02.007; -.
DR eggNOG; COG1446; Bacteria.
DR BRENDA; 3.5.1.26; 14254.
DR EvolutionaryTrace; Q47898; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IEA:UniProtKB-EC.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR10188; PTHR10188; 2.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Direct protein sequencing; Hydrolase;
KW Periplasm; Protease; Signal.
FT SIGNAL 1..45
FT /evidence="ECO:0000269|PubMed:8250923"
FT CHAIN 46..196
FT /note="Glycosylasparaginase alpha chain"
FT /id="PRO_0000002347"
FT CHAIN 197..340
FT /note="Glycosylasparaginase beta chain"
FT /id="PRO_0000002348"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:10490104,
FT ECO:0000269|PubMed:17157318, ECO:0000269|PubMed:20800597,
FT ECO:0000269|PubMed:9685368"
FT BINDING 225..228
FT /ligand="substrate"
FT BINDING 248..251
FT /ligand="substrate"
FT MUTAGEN 197
FT /note="T->A: Abolishes autocatalytic cleavage."
FT /evidence="ECO:0000269|PubMed:10490104,
FT ECO:0000269|PubMed:17157318"
FT MUTAGEN 197
FT /note="T->C: Strongly reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:10490104,
FT ECO:0000269|PubMed:17157318"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:5V2I"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:4R4Y"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:9GAF"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 171..180
FT /evidence="ECO:0007829|PDB:5V2I"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4R4Y"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:1P4K"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:5V2I"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5V2I"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 273..290
FT /evidence="ECO:0007829|PDB:5V2I"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 311..317
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 329..333
FT /evidence="ECO:0007829|PDB:5V2I"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:5V2I"
SQ SEQUENCE 340 AA; 37263 MW; 4C56E5061B4E53D7 CRC64;
MRIIYKQQTM NNNRRDFIKK LGIATAAIAI NPLEAKNLLD TSEPKTTNKP IVLSTWNFGL
HANVEAWKVL SKGGKALDAV EKGVRLVEDD PTERSVGYGG RPDRDGRVTL DACIMDENYN
IGSVACMEHI KNPISVARAV MEKTPHVMLV GDGALEFALS QGFKKENLLT AESEKEWKEW
LKTSQYKPIV NIENHDTIGM IALDAQGNLS GACTTSGMAY KMHGRVGDSP IIGAGLFVDN
EIGAATATGH GEEVIRTVGT HLVVELMNQG RTPQQACKEA VERIVKIVNR RGKNLKDIQV
GFIALNKKGE YGAYCIQDGF NFAVHDQKGN RLETPGFALK
